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Conserved domains on  [gi|1988312908|ref|NP_001380453|]
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microtubule-associated serine/threonine-protein kinase 4 isoform 8 [Homo sapiens]

Protein Classification

microtubule-associated serine/threonine-protein kinase( domain architecture ID 13758936)

microtubule-associated serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
572-851 0e+00

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: 670.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05609      1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYE 731
Cdd:cd05609     81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNLYE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 GHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:cd05609    161 GHIEKDTREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDDA 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  812 PPPDAQDLITLLLRQNPLERLGTGGAYEVKQHRFFRSLDW 851
Cdd:cd05609    241 LPDDAQDLITRLLQQNPLERLGTGGAEEVKQHPFFQDLDW 280
DUF1908 pfam08926
Domain of unknown function (DUF1908); This domain is found in a set of hypothetical/structural ...
258-534 7.79e-164

Domain of unknown function (DUF1908); This domain is found in a set of hypothetical/structural eukaryotic proteins.


:

Pssm-ID: 462637  Cd Length: 281  Bit Score: 506.17  E-value: 7.79e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  258 PQDSPRNFSPSASAHFSFA--RR---NDRTDGRRWSLASLPSSGYGTNTPSSTVSSSCSSQEKLHQLPYQPTPDELHFLS 332
Cdd:pfam08926    1 PLDSPRNFSPSNPAHFSFAsiKRpapRADDDGRRWSVASLPSSGYGTTPGSSNVSSQCSSQERLHQLPFQPTVDELHFLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  333 KHFCTTESIATENRCRNTPMRPRSRSLSPGRSPACCDHEIIMMNHVYKERFPKATAQMEERLKEIITSYSPDNVLPLADG 412
Cdd:pfam08926   81 KHFSSNESIPDEDGRRSPRFRPRSRSLSPGRSPVSFDNEIVMMNHVYKERFPKATAQMEERLKEFINENSPESVLPLADG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  413 VLSFTHHQIIELARDCLDKSHQGLITSRYFLELQHKLDKLLQEAHDRSeSGELAFIKQLVRKILIVIARPARLLECLEFD 492
Cdd:pfam08926  161 ILRFVHHQVIELARDCLQKSEEGLITSRYFYELQENLEKLLQEAKEKS-SEAVAFITGLVKKLLLIISRPARLLECLEFD 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  493 PEEFYYLLEAAEGHAKEGQGIKTDIPRYIISQLGLNKDPLEE 534
Cdd:pfam08926  240 PEEFYHLLEAAEGHAKEGQGIKTDIPQYIISQLGLTRDPLEE 281
PDZ_MAST4 cd23076
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ ...
1141-1235 7.48e-60

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST4, and related domains. MAST4 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST4 is a component of the AICD-MAST4-FOXO1-RTKN2 neuroprotective pathway; MAST4 phosphorylation of forkhead box protein O1 (FOXO1) regulates rhotekin 2 (RTKN2) expression. As this pathway is repressed in Alzheimer's Disease (AD), MAST4 may play a role in preventing AD pathogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST4 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


:

Pssm-ID: 467289 [Multi-domain]  Cd Length: 95  Bit Score: 200.64  E-value: 7.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1141 PHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKS 1220
Cdd:cd23076      1 PHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKS 80
                           90
                   ....*....|....*
gi 1988312908 1221 GNKVSITTTPFENTS 1235
Cdd:cd23076     81 GNKVSITTTPFENTS 95
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1814-2192 3.32e-09

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 3.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1814 SGPQASKTELPSPESAQSPSPSGDVRASVPpvlPSSSGKKNDTTSARELSPSSLKMNKSyllePWFLPPSRGlqnsPAVS 1893
Cdd:PHA03247  2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAP---GRVSRPRRARRLGRAAQASSPPQRPR----RRAARPTVG----SLTS 2697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1894 LPDPEFKRDRKGPHPTARSPGTVMESNPQQREGSSPKHQ----------------DHTTDPKLLTCLGQNLHSPDLAR-- 1955
Cdd:PHA03247  2698 LADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPaapappavpagpatpgGPARPARPPTTAGPPAPAPPAAPaa 2777
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1956 ---PRCPLPPEASPSREKPGLRESSERGPPTARSERSAARADTCREPSMELCFPETAKTSDNSKNllsvgrthPDFYTQT 2032
Cdd:PHA03247  2778 gppRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP--------PGPPPPS 2849
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2033 QAMEKAWAPGgktnhkdGPGEARPPPRDnsslhSAGIPCEKELGKVRRGVEPKPEALLARRSLQPPGIESEKSEKLSSFP 2112
Cdd:PHA03247  2850 LPLGGSVAPG-------GDVRRRPPSRS-----PAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2113 SLQKDgAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSP---SHASGREPGAK---PSTAEPSSSPQDPPKPV 2186
Cdd:PHA03247  2918 QPQPQ-PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlgALVPGRVAVPRfrvPQPAPSREAPASSTPPL 2996

                   ....*.
gi 1988312908 2187 AAHSES 2192
Cdd:PHA03247  2997 TGHSLS 3002
PHA03247 super family cl33720
large tegument protein UL36; Provisional
2138-2437 3.65e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2138 PPPLTAKDLSSPAARQHCSSPSHA-SGREPGAKPSTAEPSSSPQdPPKPVAAHSESSSHKPRPGPDPGPPKTKHPDRSLS 2216
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPPPRPApRPSEPAVTSRARRPDAPPQ-SARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPP 2629
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2217 SQKPSVGATKGKEPATQSLGGSSREGKGHSKSGPDVFPATPGSQNKASDGIgQGEGGPSVPLHTdrAPLDAKPQPTSGGR 2296
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP-QRPRRRAARPTV--GSLTSLADPPPPPP 2706
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2297 PLEvlekpvhlPRPGHPGPSEPADQKLSAVGEKQTLSPKHPKPSTVKDCPTLCKQTDNRQTDKSPSQPAANTDRRAEGKK 2376
Cdd:PHA03247  2707 TPE--------PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908 2377 CTEALYAPAEGDKLEAGLSFVHSENrlkGAERPAAGVGKGFPEARGKGPGPQKPPTEADKP 2437
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWD---PADPPAAVLAPAAALPPAASPAGPLPPPTSAQP 2836
 
Name Accession Description Interval E-value
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
572-851 0e+00

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: 670.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05609      1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYE 731
Cdd:cd05609     81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNLYE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 GHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:cd05609    161 GHIEKDTREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDDA 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  812 PPPDAQDLITLLLRQNPLERLGTGGAYEVKQHRFFRSLDW 851
Cdd:cd05609    241 LPDDAQDLITRLLQQNPLERLGTGGAEEVKQHPFFQDLDW 280
DUF1908 pfam08926
Domain of unknown function (DUF1908); This domain is found in a set of hypothetical/structural ...
258-534 7.79e-164

Domain of unknown function (DUF1908); This domain is found in a set of hypothetical/structural eukaryotic proteins.


Pssm-ID: 462637  Cd Length: 281  Bit Score: 506.17  E-value: 7.79e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  258 PQDSPRNFSPSASAHFSFA--RR---NDRTDGRRWSLASLPSSGYGTNTPSSTVSSSCSSQEKLHQLPYQPTPDELHFLS 332
Cdd:pfam08926    1 PLDSPRNFSPSNPAHFSFAsiKRpapRADDDGRRWSVASLPSSGYGTTPGSSNVSSQCSSQERLHQLPFQPTVDELHFLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  333 KHFCTTESIATENRCRNTPMRPRSRSLSPGRSPACCDHEIIMMNHVYKERFPKATAQMEERLKEIITSYSPDNVLPLADG 412
Cdd:pfam08926   81 KHFSSNESIPDEDGRRSPRFRPRSRSLSPGRSPVSFDNEIVMMNHVYKERFPKATAQMEERLKEFINENSPESVLPLADG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  413 VLSFTHHQIIELARDCLDKSHQGLITSRYFLELQHKLDKLLQEAHDRSeSGELAFIKQLVRKILIVIARPARLLECLEFD 492
Cdd:pfam08926  161 ILRFVHHQVIELARDCLQKSEEGLITSRYFYELQENLEKLLQEAKEKS-SEAVAFITGLVKKLLLIISRPARLLECLEFD 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  493 PEEFYYLLEAAEGHAKEGQGIKTDIPRYIISQLGLNKDPLEE 534
Cdd:pfam08926  240 PEEFYHLLEAAEGHAKEGQGIKTDIPQYIISQLGLTRDPLEE 281
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
573-846 1.58e-93

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.68  E-value: 1.58e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvgLMSMTTNLYEg 732
Cdd:smart00220   79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR--QLDPGEKLTT- 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   733 hiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD-TPEELFGQVISDEINWPEKDEA 811
Cdd:smart00220  156 -------------FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPEWD 222
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1988312908   812 PPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:smart00220  223 ISPEAKDLIRKLLVKDPEKRL---TAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
571-883 2.78e-81

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 271.69  E-value: 2.78e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:PTZ00263    18 SDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnly 730
Cdd:PTZ00263    98 EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAK----------- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiEKDAREFldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDE 810
Cdd:PTZ00263   167 ----KVPDRTF---TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFD 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  811 ApppDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQK-AEFIP-QLESEDDTSYFDTRSEKYHH 883
Cdd:PTZ00263   240 G---RARDLVKGLLQTDHTKRLGTlkGGVADVKNHPYFHGANWDKLYARYyPAPIPvRVKSPGDTSNFEKYPDSPVD 313
PDZ_MAST4 cd23076
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ ...
1141-1235 7.48e-60

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST4, and related domains. MAST4 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST4 is a component of the AICD-MAST4-FOXO1-RTKN2 neuroprotective pathway; MAST4 phosphorylation of forkhead box protein O1 (FOXO1) regulates rhotekin 2 (RTKN2) expression. As this pathway is repressed in Alzheimer's Disease (AD), MAST4 may play a role in preventing AD pathogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST4 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467289 [Multi-domain]  Cd Length: 95  Bit Score: 200.64  E-value: 7.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1141 PHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKS 1220
Cdd:cd23076      1 PHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKS 80
                           90
                   ....*....|....*
gi 1988312908 1221 GNKVSITTTPFENTS 1235
Cdd:cd23076     81 GNKVSITTTPFENTS 95
Pkinase pfam00069
Protein kinase domain;
573-846 7.54e-50

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 177.05  E-value: 7.54e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEK-IKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEylhnygivhrdlkpdnllvtsmGHIKLTDFglskvglmsmttnlyeg 732
Cdd:pfam00069   80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE----------------------SGSSLTTF----------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAP 812
Cdd:pfam00069  121 --------------VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNL 186
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  813 PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:pfam00069  187 SEEAKDLLKKLLKKDPSKRL---TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
573-831 3.19e-49

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 184.06  E-value: 3.19e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:COG0515      9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVL-RPELAADPEARERFRrEARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlye 731
Cdd:COG0515     88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQ--- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekdareflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:COG0515    165 -----------TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRP 233
                          250       260
                   ....*....|....*....|.
gi 1988312908  812 P-PPDAQDLITLLLRQNPLER 831
Cdd:COG0515    234 DlPPALDAIVLRALAKDPEER 254
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
610-791 5.94e-29

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 124.91  E-value: 5.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  610 ILRNQIQ--QAFVERdiltF-------AE--NPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMArMYFA 678
Cdd:NF033483    39 VLRPDLArdPEFVAR----FrreaqsaASlsHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEA-VEIM 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  679 ETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK-VGLMSMT-TNlyeghiekdarefldkQVCGTPEYIAP 755
Cdd:NF033483   114 IQILsALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARaLSSTTMTqTN----------------SVLGTVHYLSP 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1988312908  756 EvilrQGYGKPV----DWWAMGIILYEFLVGCVPFFGDTP 791
Cdd:NF033483   178 E----QARGGTVdarsDIYSLGIVLYEMLTGRPPFDGDSP 213
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
649-831 8.48e-15

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: 81.04  E-value: 8.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---HIKLTDFGLSkvglmsm 725
Cdd:TIGR03903   57 VFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIG------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 tTNLYEGHIEKDAREFLDKQVCGTPEYIAPEvilrQGYGKPV----DWWAMGIILYEFLVGCVPFFGDTPEE-LFGQVIS 800
Cdd:TIGR03903  130 -TLLPGVRDADVATLTRTTEVLGTPTYCAPE----QLRGEPVtpnsDLYAWGLIFLECLTGQRVVQGASVAEiLYQQLSP 204
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1988312908  801 DEINWPEKDEAPPpdAQDLITLLLRQNPLER 831
Cdd:TIGR03903  205 VDVSLPPWIAGHP--LGQVLRKALNKDPRQR 233
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1145-1227 1.71e-14

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 70.87  E-value: 1.71e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  1145 IVIHSSGKNYGFTIRairvyvgDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKV 1224
Cdd:smart00228    5 VELEKGGGGLGFSLV-------GGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ...
gi 1988312908  1225 SIT 1227
Cdd:smart00228   78 TLT 80
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
1176-1224 1.60e-09

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 55.61  E-value: 1.60e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908 1176 IVWNVEEGSPACQAGLKAGDLITHINGEPVHGLvhTEVIELLLKSGNKV 1224
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSL--EDVARLLQGSAGES 47
PHA03247 PHA03247
large tegument protein UL36; Provisional
1814-2192 3.32e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 3.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1814 SGPQASKTELPSPESAQSPSPSGDVRASVPpvlPSSSGKKNDTTSARELSPSSLKMNKSyllePWFLPPSRGlqnsPAVS 1893
Cdd:PHA03247  2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAP---GRVSRPRRARRLGRAAQASSPPQRPR----RRAARPTVG----SLTS 2697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1894 LPDPEFKRDRKGPHPTARSPGTVMESNPQQREGSSPKHQ----------------DHTTDPKLLTCLGQNLHSPDLAR-- 1955
Cdd:PHA03247  2698 LADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPaapappavpagpatpgGPARPARPPTTAGPPAPAPPAAPaa 2777
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1956 ---PRCPLPPEASPSREKPGLRESSERGPPTARSERSAARADTCREPSMELCFPETAKTSDNSKNllsvgrthPDFYTQT 2032
Cdd:PHA03247  2778 gppRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP--------PGPPPPS 2849
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2033 QAMEKAWAPGgktnhkdGPGEARPPPRDnsslhSAGIPCEKELGKVRRGVEPKPEALLARRSLQPPGIESEKSEKLSSFP 2112
Cdd:PHA03247  2850 LPLGGSVAPG-------GDVRRRPPSRS-----PAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2113 SLQKDgAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSP---SHASGREPGAK---PSTAEPSSSPQDPPKPV 2186
Cdd:PHA03247  2918 QPQPQ-PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlgALVPGRVAVPRfrvPQPAPSREAPASSTPPL 2996

                   ....*.
gi 1988312908 2187 AAHSES 2192
Cdd:PHA03247  2997 TGHSLS 3002
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1167-1227 1.10e-08

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 59.50  E-value: 1.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908 1167 DSDIYTVHHIVwnveEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLL-KSGNKVSIT 1227
Cdd:COG0793     69 EDGKVVVVSVI----PGSPAEKAGIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLT 126
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
621-722 1.67e-07

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 57.27  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  621 ERDILTFAENPFVVSMYCsfETRR---HLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDL 697
Cdd:NF033442   556 EAEVLGRLRHPRIVALVE--GPLEiggRTALLLEYAGEQTLAERLRKEGRLSLDLLERFGDDLLSAVVHLEGQGVWHRDI 633
                           90       100
                   ....*....|....*....|....*....
gi 1988312908  698 KPDNLLVTSMG----HIKLTDFGLSKVGL 722
Cdd:NF033442   634 KPDNIGIRPRPsrtlHLVLFDFSLAGAPA 662
PHA03247 PHA03247
large tegument protein UL36; Provisional
2138-2437 3.65e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2138 PPPLTAKDLSSPAARQHCSSPSHA-SGREPGAKPSTAEPSSSPQdPPKPVAAHSESSSHKPRPGPDPGPPKTKHPDRSLS 2216
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPPPRPApRPSEPAVTSRARRPDAPPQ-SARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPP 2629
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2217 SQKPSVGATKGKEPATQSLGGSSREGKGHSKSGPDVFPATPGSQNKASDGIgQGEGGPSVPLHTdrAPLDAKPQPTSGGR 2296
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP-QRPRRRAARPTV--GSLTSLADPPPPPP 2706
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2297 PLEvlekpvhlPRPGHPGPSEPADQKLSAVGEKQTLSPKHPKPSTVKDCPTLCKQTDNRQTDKSPSQPAANTDRRAEGKK 2376
Cdd:PHA03247  2707 TPE--------PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908 2377 CTEALYAPAEGDKLEAGLSFVHSENrlkGAERPAAGVGKGFPEARGKGPGPQKPPTEADKP 2437
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWD---PADPPAAVLAPAAALPPAASPAGPLPPPTSAQP 2836
 
Name Accession Description Interval E-value
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
572-851 0e+00

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: 670.27  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05609      1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYE 731
Cdd:cd05609     81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNLYE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 GHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:cd05609    161 GHIEKDTREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGDDA 240
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  812 PPPDAQDLITLLLRQNPLERLGTGGAYEVKQHRFFRSLDW 851
Cdd:cd05609    241 LPDDAQDLITRLLQQNPLERLGTGGAEEVKQHPFFQDLDW 280
DUF1908 pfam08926
Domain of unknown function (DUF1908); This domain is found in a set of hypothetical/structural ...
258-534 7.79e-164

Domain of unknown function (DUF1908); This domain is found in a set of hypothetical/structural eukaryotic proteins.


Pssm-ID: 462637  Cd Length: 281  Bit Score: 506.17  E-value: 7.79e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  258 PQDSPRNFSPSASAHFSFA--RR---NDRTDGRRWSLASLPSSGYGTNTPSSTVSSSCSSQEKLHQLPYQPTPDELHFLS 332
Cdd:pfam08926    1 PLDSPRNFSPSNPAHFSFAsiKRpapRADDDGRRWSVASLPSSGYGTTPGSSNVSSQCSSQERLHQLPFQPTVDELHFLS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  333 KHFCTTESIATENRCRNTPMRPRSRSLSPGRSPACCDHEIIMMNHVYKERFPKATAQMEERLKEIITSYSPDNVLPLADG 412
Cdd:pfam08926   81 KHFSSNESIPDEDGRRSPRFRPRSRSLSPGRSPVSFDNEIVMMNHVYKERFPKATAQMEERLKEFINENSPESVLPLADG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  413 VLSFTHHQIIELARDCLDKSHQGLITSRYFLELQHKLDKLLQEAHDRSeSGELAFIKQLVRKILIVIARPARLLECLEFD 492
Cdd:pfam08926  161 ILRFVHHQVIELARDCLQKSEEGLITSRYFYELQENLEKLLQEAKEKS-SEAVAFITGLVKKLLLIISRPARLLECLEFD 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  493 PEEFYYLLEAAEGHAKEGQGIKTDIPRYIISQLGLNKDPLEE 534
Cdd:pfam08926  240 PEEFYHLLEAAEGHAKEGQGIKTDIPQYIISQLGLTRDPLEE 281
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
579-851 2.46e-144

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: 450.13  E-value: 2.46e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd05579      1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYEGHIEKDA 738
Cdd:cd05579     81 YSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKLSIQKKSNGA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  739 REFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEaPPPDAQD 818
Cdd:cd05579    161 PEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDPE-VSDEAKD 239
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1988312908  819 LITLLLRQNPLERLGTGGAYEVKQHRFFRSLDW 851
Cdd:cd05579    240 LISKLLTPDPEKRLGAKGIEEIKNHPFFKGIDW 272
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
579-846 9.73e-118

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: 373.01  E-value: 9.73e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd05123      1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlyeghiekda 738
Cdd:cd05123     81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRT---------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  739 refldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKdeaPPPDAQD 818
Cdd:cd05123    151 -----YTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEY---VSPEAKS 222
                          250       260
                   ....*....|....*....|....*...
gi 1988312908  819 LITLLLRQNPLERLGTGGAYEVKQHRFF 846
Cdd:cd05123    223 LISGLLQKDPTKRLGSGGAEEIKAHPFF 250
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
571-875 9.49e-108

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: 348.51  E-value: 9.49e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05573      1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvGL------MS 724
Cdd:cd05573     81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCT-KMnksgdrES 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTTNLYEGHIEKDAREFLDKQ---------VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELF 795
Cdd:cd05573    160 YLNDSVNTLFQDNVLARRRPHkqrrvraysAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETY 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  796 GQVisdeINWPE-----KDEAPPPDAQDLITLLLRqNPLERLGTggAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDD 870
Cdd:cd05573    240 SKI----MNWKEslvfpDDPDVSPEAIDLIRRLLC-DPEDRLGS--AEEIKAHPFFKGIDWENLRESPPPFVPELSSPTD 312

                   ....*
gi 1988312908  871 TSYFD 875
Cdd:cd05573    313 TSNFD 317
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
571-875 8.63e-99

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: 321.87  E-value: 8.63e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05599      1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAEADNPWVVKLYYSFQDEENLYLIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnly 730
Cdd:cd05599     81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT----------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 egHIEKDAREFldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVisdeINWPEK-- 808
Cdd:cd05599    150 --GLKKSHLAY---STVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKI----MNWRETlv 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  809 --DEAP-PPDAQDLITLLLrQNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDDTSYFD 875
Cdd:cd05599    221 fpPEVPiSPEAKDLIERLL-CDAEHRLGANGVEEIKSHPFFKGVDWDHIRERPAPILPEVKSILDTSNFD 289
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
571-876 3.39e-98

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: 320.42  E-value: 3.39e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05598      1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQDKENLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglmsmTTNLY 730
Cdd:cd05598     81 DYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL--------CTGFR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHiekDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVisdeINWPEKDE 810
Cdd:cd05598    153 WTH---DSKYYLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKV----INWRTTLK 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  811 APP-----PDAQDLITLLLRqNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDDTSYFDT 876
Cdd:cd05598    226 IPHeanlsPEAKDLILRLCC-DAEDRLGRNGADEIKAHPFFAGIDWEKLRKQKAPYIPTIRHPTDTSNFDP 295
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
571-876 3.61e-98

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: 318.75  E-value: 3.61e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05580      1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnly 730
Cdd:cd05580     81 EYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAK----------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 egHIEKDArefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDE 810
Cdd:cd05580    150 --RVKDRT-----YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFD 222
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  811 appPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYFDT 876
Cdd:cd05580    223 ---PDAKDLIKRLLVVDLTKRLGNlkNGVEDIKNHPWFAGIDWDALLQRKipAPYVPKVRGPGDTSNFDK 289
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
576-852 7.36e-95

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: 307.87  E-value: 7.36e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTF-AENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd05611      1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIqGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSmttnlyeghi 734
Cdd:cd05611     81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEK---------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 ekdaREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPE-KDEAPP 813
Cdd:cd05611    151 ----RH--NKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEeVKEFCS 224
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1988312908  814 PDAQDLITLLLRQNPLERLGTGGAYEVKQHRFFRSLDWN 852
Cdd:cd05611    225 PEAVDLINRLLCMDPAKRLGANGYQEIKSHPFFKSINWD 263
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
573-846 1.58e-93

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 303.68  E-value: 1.58e-93
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKI--KKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvgLMSMTTNLYEg 732
Cdd:smart00220   79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLAR--QLDPGEKLTT- 155
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   733 hiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD-TPEELFGQVISDEINWPEKDEA 811
Cdd:smart00220  156 -------------FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPEWD 222
                           250       260       270
                    ....*....|....*....|....*....|....*
gi 1988312908   812 PPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:smart00220  223 ISPEAKDLIRKLLVKDPEKRL---TAEEALQHPFF 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
571-870 2.60e-90

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: 297.23  E-value: 2.60e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05574      1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK-----VGLM 723
Cdd:cd05574     81 DYCPGGELFRLLQkqPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtPPPV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 SMTTN--LYEGHIEKDAREFLDKQV-------CGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:cd05574    161 RKSLRkgSRRSSVKSIEKETFVAEPsarsnsfVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDET 240
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  795 FGQVISDEINWPEKDEApPPDAQDLITLLLRQNPLERLGT-GGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDD 870
Cdd:cd05574    241 FSNILKKELTFPESPPV-SSEAKDLIRKLLVKDPSKRLGSkRGASEIKRHPFFRGVNWALIRNMTPPIIPRPDDPID 316
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
577-875 9.61e-90

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: 295.66  E-value: 9.61e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAEN-PFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05570      1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRhPFLTGLHACFQTEDRLYFVMEYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDcatLMKNM---GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtTNLYEG 732
Cdd:cd05570     81 GD---LMFHIqraRRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK-------EGIWGG 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hieKDAREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKdeaP 812
Cdd:cd05570    151 ---NTTSTF-----CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRW---L 219
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  813 PPDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05570    220 SREAVSILKGLLTKDPARRLGCGpkGEADIKAHPFFRNIDWDKLEKKEVEppFKPKVKSPRDTSNFD 286
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
568-878 4.92e-86

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: 286.39  E-value: 4.92e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd05610      1 PSIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGL----- 722
Cdd:cd05610     81 LVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLnreln 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 ---------MSMTTNLYE------------------------GHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDW 769
Cdd:cd05610    161 mmdilttpsMAKPKNDYSrtpgqvlslisslgfntptpyrtpKSVRRGAARVEGERILGTPDYLAPELLLGKPHGPAVDW 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  770 WAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPPPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFFRSL 849
Cdd:cd05610    241 WALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEELSVNAQNAIEILLTMDPTKR---AGLKELKQHPLFHGV 317
                          330       340
                   ....*....|....*....|....*....
gi 1988312908  850 DWNSLLRQKAEFIPQLESEDDTSYFDTRS 878
Cdd:cd05610    318 DWENLQNQTMPFIPQPDDETDTSYFEARN 346
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
571-879 3.54e-85

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: 281.25  E-value: 3.54e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05612      1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglmsmttnly 730
Cdd:cd05612     81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGF------------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiekdAREFLDK--QVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEK 808
Cdd:cd05612    148 -------AKKLRDRtwTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRH 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  809 DEappPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFDTRSE 879
Cdd:cd05612    221 LD---LYAKDLIKKLLVVDRTRRLGNmkNGADDVKNHRWFKSVDWDDVPQRKLKppIVPKVSHDGDTSNFDDYPE 292
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
567-880 5.41e-85

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: 283.50  E-value: 5.41e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  567 KPRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd05596     22 RMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglMSMt 726
Cdd:cd05596    102 YMVMDYMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTC----MKM- 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeghiEKDAREFLDKQVcGTPEYIAPEVILRQG----YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS-- 800
Cdd:cd05596    176 --------DKDGLVRSDTAV-GTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNhk 246
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  801 DEINWPEKDEApPPDAQDLIT--LLLRQNpleRLGTGGAYEVKQHRFFRSLDWN--SLLRQKAEFIPQLESEDDTSYFDT 876
Cdd:cd05596    247 NSLQFPDDVEI-SKDAKSLICafLTDREV---RLGRNGIEEIKAHPFFKNDQWTwdNIRETVPPVVPELSSDIDTSNFDD 322

                   ....
gi 1988312908  877 RSEK 880
Cdd:cd05596    323 IEED 326
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
563-875 1.39e-82

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: 277.68  E-value: 1.39e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  563 KLRRKPRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFET 642
Cdd:cd05600      3 KRRTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  643 RRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGL 722
Cdd:cd05600     83 PENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 -----MSMTTNL--------------YEGHIEKDAREFLDKQ---VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd05600    163 spkkiESMKIRLeevkntafleltakERRNIYRAMRKEDQNYansVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECL 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  781 VGCVPFFGDTPEELFGQVisdeINWPEKDEAP-----------PPDAQDLITLLLrQNPLERLgtGGAYEVKQHRFFRSL 849
Cdd:cd05600    243 VGFPPFSGSTPNETWANL----YHWKKTLQRPvytdpdlefnlSDEAWDLITKLI-TDPQDRL--QSPEQIKNHPFFKNI 315
                          330       340
                   ....*....|....*....|....*..
gi 1988312908  850 DWNSLLRQ-KAEFIPQLESEDDTSYFD 875
Cdd:cd05600    316 DWDRLREGsKPPFIPELESEIDTSYFD 342
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
571-883 2.78e-81

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 271.69  E-value: 2.78e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:PTZ00263    18 SDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnly 730
Cdd:PTZ00263    98 EFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAK----------- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiEKDAREFldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDE 810
Cdd:PTZ00263   167 ----KVPDRTF---TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFD 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  811 ApppDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQK-AEFIP-QLESEDDTSYFDTRSEKYHH 883
Cdd:PTZ00263   240 G---RARDLVKGLLQTDHTKRLGTlkGGVADVKNHPYFHGANWDKLYARYyPAPIPvRVKSPGDTSNFEKYPDSPVD 313
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
572-876 8.92e-80

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: 269.41  E-value: 8.92e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05629      2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS----KVGLMSMTT 727
Cdd:cd05629     82 FLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhKQHDSAYYQ 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NLYEGHIEKD----------------------------AREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEF 779
Cdd:cd05629    162 KLLQGKSNKNridnrnsvavdsinltmsskdqiatwkkNRRLMAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFEC 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  780 LVGCVPFFGDTPEELFGQVisdeINWPEKDEAP-----PPDAQDLITLLLrQNPLERLGTGGAYEVKQHRFFRSLDWNSL 854
Cdd:cd05629    242 LIGWPPFCSENSHETYRKI----INWRETLYFPddihlSVEAEDLIRRLI-TNAENRLGRGGAHEIKSHPFFRGVDWDTI 316
                          330       340
                   ....*....|....*....|..
gi 1988312908  855 LRQKAEFIPQLESEDDTSYFDT 876
Cdd:cd05629    317 RQIRAPFIPQLKSITDTSYFPT 338
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
577-875 1.50e-79

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: 266.53  E-value: 1.50e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd05571      1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlyeghiek 736
Cdd:cd05571     81 ELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATT-------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 darefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKdeaPPPDA 816
Cdd:cd05571    153 -------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPST---LSPEA 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  817 QDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05571    223 KSLLAGLLKKDPKKRLGGGprDAKEIMEHPFFASINWDDLYQKKIPppFKPQVTSETDTRYFD 285
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
571-846 1.95e-79

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: 264.46  E-value: 1.95e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05581      1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsMTTNLY 730
Cdd:cd05581     81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKV----LGPDSS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHIEKDAREFLDKQ------VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIN 804
Cdd:cd05581    157 PESTKGDADSQIAYNqaraasFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYE 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908  805 WPEKdeaPPPDAQDLITLLLRQNPLERLG---TGGAYEVKQHRFF 846
Cdd:cd05581    237 FPEN---FPPDAKDLIQKLLVLDPSKRLGvneNGGYDELKAHPFF 278
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
572-875 4.68e-78

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: 260.80  E-value: 4.68e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14209      2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK-VGLMSMTtnly 730
Cdd:cd14209     82 YVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKrVKGRTWT---- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDE 810
Cdd:cd14209    158 ---------------LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFS 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  811 appPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYFD 875
Cdd:cd14209    223 ---SDLKDLLRNLLQVDLTKRFGNlkNGVNDIKNHKWFATTDWIAIYQRKveAPFIPKLKGPGDTSNFD 288
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
576-877 1.13e-76

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: 258.10  E-value: 1.13e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESR---QRFAMKKINKQNlILRNQIQQAFV--ERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05584      1 LKVLGKGGYGKVFQVRKTTGSdkgKIFAMKVLKKAS-IVRNQKDTAHTkaERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnly 730
Cdd:cd05584     80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCK----------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eGHIEKDAREFldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINwpekde 810
Cdd:cd05584    149 -ESIHDGTVTH---TFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLN------ 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  811 APP---PDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFDTR 877
Cdd:cd05584    219 LPPyltNEARDLLKKLLKRNVSSRLGSGpgDAEEIKAHPFFRHINWDDLLAKKVEppFKPLLQSEEDVSQFDSK 292
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
579-852 1.76e-75

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: 252.15  E-value: 1.76e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd05572      1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttnlyeghIEKDA 738
Cdd:cd05572     81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-------------LGSGR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  739 REFldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD--TPEELFgQVISDEInwpEKDEAPP--- 813
Cdd:cd05572    148 KTW---TFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDdeDPMKIY-NIILKGI---DKIEFPKyid 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1988312908  814 PDAQDLITLLLRQNPLERLG--TGGAYEVKQHRFFRSLDWN 852
Cdd:cd05572    221 KNAKNLIKQLLRRNPEERLGylKGGIRDIKKHKWFEGFDWE 261
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
577-875 3.28e-74

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: 251.08  E-value: 3.28e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd05595      1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlyeghiek 736
Cdd:cd05595     81 ELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATM-------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 darefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdEAPPPDA 816
Cdd:cd05595    153 -------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFP---RTLSPEA 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  817 QDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYFD 875
Cdd:cd05595    223 KSLLAGLLKKDPKQRLGGGpsDAKEVMEHRFFLSINWQDVVQKKllPPFKPQVTSEVDTRYFD 285
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
571-881 1.61e-73

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: 249.15  E-value: 1.61e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05601      1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLM-KNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnl 729
Cdd:cd05601     81 EYHPGGDLLSLLsRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSA----------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 yeghiekdAREFLDKQV-----CGTPEYIAPEVIL------RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV 798
Cdd:cd05601    150 --------AKLSSDKTVtskmpVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNI 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  799 IS--DEINWPEkDEAPPPDAQDLITLLLrQNPLERLGtggaYE-VKQHRFFRSLDWNSLLRQKAEFIPQLESEDDTSYFD 875
Cdd:cd05601    222 MNfkKFLKFPE-DPKVSESAVDLIKGLL-TDAKERLG----YEgLCCHPFFSGIDWNNLRQTVPPFVPTLTSDDDTSNFD 295

                   ....*.
gi 1988312908  876 TRSEKY 881
Cdd:cd05601    296 EFEPKK 301
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
573-875 5.92e-73

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: 247.60  E-value: 5.92e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDIL---TFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd05589      1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFetvNSARHPFLVNLFACFQTPEHVCFV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDcatLM----KNMGPLPVdmARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLmsm 725
Cdd:cd05589     81 MEYAAGGD---LMmhihEDVFSEPR--AVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeGHIEKDArefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW 805
Cdd:cd05589    153 ------GFGDRTS------TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRY 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  806 PekdEAPPPDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05589    221 P---RFLSTEAISIMRRLLRKNPERRLGASerDAEDVKKQPFFRNIDWEALLARKIKppFVPTIKSPEDVSNFD 291
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
571-875 1.34e-72

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: 246.88  E-value: 1.34e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05597      1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGP-LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFG----LSKVGLMSM 725
Cdd:cd05597     81 DYYCGGDLLTLLSKFEDrLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGsclkLREDGTVQS 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TTNLyeghiekdarefldkqvcGTPEYIAPEvILR-----QG-YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd05597    161 SVAV------------------GTPDYISPE-ILQamedgKGrYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  800 SDE--INWPEKDEAPPPDAQDLITLLLrQNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDDTSYFD 875
Cdd:cd05597    222 NHKehFSFPDDEDDVSEEAKDLIRRLI-CSRERRLGQNGIDDFKKHPFFEGIDWDNIRDSTPPYIPEVTSPTDTSNFD 298
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
577-875 2.91e-72

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: 245.37  E-value: 2.91e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFA-ENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05592      1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALAsQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtTNLYEghiE 735
Cdd:cd05592     81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCK-------ENIYG---E 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  736 KDAREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEApppD 815
Cdd:cd05592    151 NKASTF-----CGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTK---E 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  816 AQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05592    223 AASCLSLLLERNPEKRLGVpeCPAGDIRDHPFFKTIDWDKLERREIDppFKPKVKSANDVSNFD 286
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
577-876 5.06e-71

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: 241.84  E-value: 5.06e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTfaEN---PFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd05575      1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLL--KNvkhPFLVGLHYSFQTKDKLYFVLDYV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTnlyegh 733
Cdd:cd05575     79 NGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDT------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdAREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKdeaPP 813
Cdd:cd05575    153 ----TSTF-----CGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTN---VS 220
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  814 PDAQDLITLLLRQNPLERLGTGGAY-EVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFDT 876
Cdd:cd05575    221 PSARDLLEGLLQKDRTKRLGSGNDFlEIKNHSFFRPINWDDLEAKKIPppFNPNVSGPLDLRNIDP 286
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
577-876 3.46e-70

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: 239.22  E-value: 3.46e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRH---KESRQRFAMKKINKQNLILRNQIQQAfVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd05582      1 KVLGQGSFGKVFLVRKitgPDAGTLYAMKVLKKATLKVRDRVRTK-MERDILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSmttnlyegh 733
Cdd:cd05582     80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDH--------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iEKDAREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdEAPP 813
Cdd:cd05582    151 -EKKAYSF-----CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMP---QFLS 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  814 PDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFDT 876
Cdd:cd05582    222 PEAQSLLRALFKRNPANRLGAGpdGVEEIKRHPFFATIDWNKLYRKEIKppFKPAVSRPDDTFYFDP 288
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
563-875 4.43e-70

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: 241.44  E-value: 4.43e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  563 KLRRKPResDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFET 642
Cdd:cd05621     46 ELQMKAE--DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQD 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  643 RRHLCMVMEYVEGGDCATLMKNMGpLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvgl 722
Cdd:cd05621    124 DKYLYMVMEYMPGGDLVNLMSNYD-VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTC---- 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 MSMTTNlyeGHIEKDArefldkqVCGTPEYIAPEVILRQG----YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV 798
Cdd:cd05621    199 MKMDET---GMVHCDT-------AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKI 268
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  799 I--SDEINWPEkDEAPPPDAQDLITLLLRQNPLeRLGTGGAYEVKQHRFFRSLDWN--SLLRQKAEFIPQLESEDDTSYF 874
Cdd:cd05621    269 MdhKNSLNFPD-DVEISKHAKNLICAFLTDREV-RLGRNGVEEIKQHPFFRNDQWNwdNIRETAAPVVPELSSDIDTSNF 346

                   .
gi 1988312908  875 D 875
Cdd:cd05621    347 D 347
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
571-880 5.69e-70

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: 241.07  E-value: 5.69e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05626      1 SMFVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLY 730
Cdd:cd05626     81 DYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFRWTHNSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 E--GHIEKDAREFLD------------------------KQVC------GTPEYIAPEVILRQGYGKPVDWWAMGIILYE 778
Cdd:cd05626    161 QkgSHIRQDSMEPSDlwddvsncrcgdrlktleqratkqHQRClahslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  779 FLVGCVPFFGDTPEELFGQVisdeINWPEKDEAPP-----PDAQDLITLLLRQNPlERLGTGGAYEVKQHRFFRSLDWNS 853
Cdd:cd05626    241 MLVGQPPFLAPTPTETQLKV----INWENTLHIPPqvklsPEAVDLITKLCCSAE-ERLGRNGADDIKAHPFFSEVDFSS 315
                          330       340
                   ....*....|....*....|....*...
gi 1988312908  854 LLR-QKAEFIPQLESEDDTSYFDTRSEK 880
Cdd:cd05626    316 DIRtQPAPYVPKISHPMDTSNFDPVEEE 343
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
572-845 1.06e-69

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: 235.10  E-value: 1.06e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQqafVER--DILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14003      1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEK---IKReiEIMKLLNHPNIIKLYEVIETENKIYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttNL 729
Cdd:cd14003     78 MEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLS---------NE 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 YEGHiekdarEFLdKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEK 808
Cdd:cd14003    149 FRGG------SLL-KTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSH 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  809 deaPPPDAQDLITLLLRQNPLERLGTGgayEVKQHRF 845
Cdd:cd14003    222 ---LSPDARDLIRRMLVVDPSKRITIE---EILNHPW 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
572-847 1.98e-69

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: 234.68  E-value: 1.98e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafVERDI--LTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14007      1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQ--LRREIeiQSHLRHPNILRLYGYFEDKKRIYLI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnl 729
Cdd:cd14007     79 LEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSV---------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 yegHIEKDARefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKd 809
Cdd:cd14007    149 ---HAPSNRR----KTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSS- 220
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1988312908  810 eaPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFR 847
Cdd:cd14007    221 --VSPEAKDLISKLLQKDPSKRL---SLEQVLNHPWIK 253
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
571-875 2.26e-69

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: 239.56  E-value: 2.26e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05625      1 SMFVKIKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLY 730
Cdd:cd05625     81 DYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHDSKYY 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EG--HIEKDAREF------------------------------LDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYE 778
Cdd:cd05625    161 QSgdHLRQDSMDFsnewgdpencrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  779 FLVGCVPFFGDTPEELFGQVisdeINWPEKDEAPP-----PDAQDLITLLLRqNPLERLGTGGAYEVKQHRFFRSLDWNS 853
Cdd:cd05625    241 MLVGQPPFLAQTPLETQMKV----INWQTSLHIPPqaklsPEASDLIIKLCR-GPEDRLGKNGADEIKAHPFFKTIDFSS 315
                          330       340
                   ....*....|....*....|...
gi 1988312908  854 LLRQK-AEFIPQLESEDDTSYFD 875
Cdd:cd05625    316 DLRQQsAPYIPKITHPTDTSNFD 338
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
571-875 1.52e-68

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: 235.20  E-value: 1.52e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFA-ENPFVVSMYCSFETRRHLCMV 649
Cdd:cd05619      5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAwEHPFLTHLFCTFQTKENLFFV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSmttnl 729
Cdd:cd05619     85 MEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLG----- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 yeghiekDAREfldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKD 809
Cdd:cd05619    160 -------DAKT---STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWL 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  810 EApppDAQDLITLLLRQNPLERLGTGGayEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05619    230 EK---EAKDILVKLFVREPERRLGVRG--DIRQHPFFREINWEALEEREIEppFKPKVKSPFDCSNFD 292
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
569-879 2.21e-68

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: 237.60  E-value: 2.21e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCM 648
Cdd:cd05622     71 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYM 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGpLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglMSMTTn 728
Cdd:cd05622    151 VMEYMPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC----MKMNK- 224
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyEGHIEKDArefldkqVCGTPEYIAPEVILRQG----YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS--DE 802
Cdd:cd05622    225 --EGMVRCDT-------AVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNhkNS 295
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  803 INWPEkDEAPPPDAQDLITLLLRQNPLeRLGTGGAYEVKQHRFFRS--LDWNSLLRQKAEFIPQLESEDDTSYFDTRSE 879
Cdd:cd05622    296 LTFPD-DNDISKEAKNLICAFLTDREV-RLGRNGVEEIKRHLFFKNdqWAWETLRDTVAPVVPDLSSDIDTSNFDDLEE 372
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
578-875 2.86e-67

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: 230.92  E-value: 2.86e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGD 657
Cdd:cd05585      1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLM-SMTTNLYeghiek 736
Cdd:cd05585     81 LFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKdDDKTNTF------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 darefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDeapPPDA 816
Cdd:cd05585    155 ----------CGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGF---DRDA 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  817 QDLITLLLRQNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05585    222 KDLLIGLLNRDPTKRLGYNGAQEIKNHPFFDQIDWKRLLMKKIQppFKPAVENAIDTSNFD 282
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
572-879 3.07e-67

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: 232.64  E-value: 3.07e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05627      3 DFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLY- 730
Cdd:cd05627     83 FLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYr 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 -------------------EGHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP 791
Cdd:cd05627    163 nlthnppsdfsfqnmnskrKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETP 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  792 EELFGQVisdeINWPEKDEAPP--PDAQDLITLLLR--QNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLES 867
Cdd:cd05627    243 QETYRKV----MNWKETLVFPPevPISEKAKDLILRfcTDAENRIGSNGVEEIKSHPFFEGVDWEHIRERPAAIPIEIKS 318
                          330
                   ....*....|..
gi 1988312908  868 EDDTSYFDTRSE 879
Cdd:cd05627    319 IDDTSNFDDFPE 330
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
572-845 3.11e-67

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: 228.51  E-value: 3.11e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLIlRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05117      1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLK-SEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDcatL---MKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM---GHIKLTDFGLSKvglmsm 725
Cdd:cd05117     80 LCTGGE---LfdrIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpdSPIKIIDFGLAK------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyegHIEKDarEFLdKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW 805
Cdd:cd05117    151 -------IFEEG--EKL-KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSF 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1988312908  806 PEKDEAP-PPDAQDLITLLLRQNPLERLgTggAYEVKQHRF 845
Cdd:cd05117    221 DSPEWKNvSEEAKDLIKRLLVVDPKKRL-T--AAEALNHPW 258
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
559-875 1.69e-66

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: 229.97  E-value: 1.69e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  559 NASLKLRRKPRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYC 638
Cdd:cd05593      3 DASTTHHKRKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  639 SFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS 718
Cdd:cd05593     83 SFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 KVGLMSMTTNlyeghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV 798
Cdd:cd05593    163 KEGITDAATM---------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELI 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  799 ISDEINWPEKDEApppDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYF 874
Cdd:cd05593    228 LMEDIKFPRTLSA---DAKSLLSGLLIKDPNKRLGGGpdDAKEIMRHSFFTGVNWQDVYDKKlvPPFKPQVTSETDTRYF 304

                   .
gi 1988312908  875 D 875
Cdd:cd05593    305 D 305
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
576-876 2.10e-66

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: 228.43  E-value: 2.10e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENP-FVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd05587      1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVMEYVN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlyeghi 734
Cdd:cd05587     81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTT------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 ekdaREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdEAPPP 814
Cdd:cd05587    155 ----RTF-----CGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP---KSLSK 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  815 DAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFDT 876
Cdd:cd05587    223 EAVSICKGLLTKHPAKRLGCGptGERDIKEHPFFRRIDWEKLERREIQppFKPKIKSPRDAENFDK 288
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
548-875 2.16e-66

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: 229.92  E-value: 2.16e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  548 TPETDESVSSSNASL-KLRRKPRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILT 626
Cdd:cd05594      1 SPSDNSGAEEMEVSLtKPKHKVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  627 FAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHN-YGIVHRDLKPDNLLVT 705
Cdd:cd05594     81 NSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  706 SMGHIKLTDFGLSKVGLMSMTTNlyeghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVP 785
Cdd:cd05594    161 KDGHIKITDFGLCKEGIKDGATM---------------KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLP 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  786 FFGDTPEELFGQVISDEINWPekdEAPPPDAQDLITLLLRQNPLERLGTGG--AYEVKQHRFFRSLDWNSLLRQK--AEF 861
Cdd:cd05594    226 FYNQDHEKLFELILMEEIRFP---RTLSPEAKSLLSGLLKKDPKQRLGGGPddAKEIMQHKFFAGIVWQDVYEKKlvPPF 302
                          330
                   ....*....|....
gi 1988312908  862 IPQLESEDDTSYFD 875
Cdd:cd05594    303 KPQVTSETDTRYFD 316
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
573-846 2.08e-64

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: 220.21  E-value: 2.08e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05578      2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLYEG 732
Cdd:cd05578     82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIA--------TKLTDG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HiekdarefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAP 812
Cdd:cd05578    154 T--------LATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAGW 225
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  813 PPDAQDLITLLLRQNPLERLGTggAYEVKQHRFF 846
Cdd:cd05578    226 SEEAIDLINKLLERDPQKRLGD--LSDLKNHPYF 257
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
577-875 7.11e-64

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: 221.32  E-value: 7.11e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAEN-PFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05590      1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNhPFLTQLYCCFQTPDRLFFVMEFVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMS-MTTNLYeghi 734
Cdd:cd05590     81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNgKTTSTF---- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 ekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAppp 814
Cdd:cd05590    157 ------------CGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQ--- 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  815 DAQDLITLLLRQNPLERLGT---GGAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05590    222 DAVDILKAFMTKNPTMRLGSltlGGEEAILRHPFFKELDWEKLNRRQIEppFRPRIKSREDVSNFD 287
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
572-875 1.04e-63

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: 222.99  E-value: 1.04e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05628      2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLY- 730
Cdd:cd05628     82 FLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYr 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 -------------------EGHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP 791
Cdd:cd05628    162 nlnhslpsdftfqnmnskrKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSETP 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  792 EELFGQVisdeINWPEKDEAPP--PDAQDLITLLLR--QNPLERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLES 867
Cdd:cd05628    242 QETYKKV----MNWKETLIFPPevPISEKAKDLILRfcCEWEHRIGAPGVEEIKTNPFFEGVDWEHIRERPAAIPIEIKS 317

                   ....*...
gi 1988312908  868 EDDTSYFD 875
Cdd:cd05628    318 IDDTSNFD 325
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
579-875 2.53e-63

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: 220.13  E-value: 2.53e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDIL---TFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05586      1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILvrtALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMS-MTTNLYeghi 734
Cdd:cd05586     81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDnKTTNTF---- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 ekdarefldkqvCGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEkdEAPP 813
Cdd:cd05586    157 ------------CGTTEYLAPEVLLDEkGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPK--DVLS 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  814 PDAQDLITLLLRQNPLERLG-TGGAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05586    223 DEGRSFVKGLLNRNPKHRLGaHDDAVELKEHPFFADIDWDLLSKKKITppFKPIVDSDTDVSNFD 287
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
577-875 8.74e-62

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: 215.19  E-value: 8.74e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFA-ENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05620      1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAwENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtTNLYEghiE 735
Cdd:cd05620     81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCK-------ENVFG---D 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  736 KDAREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdEAPPPD 815
Cdd:cd05620    151 NRASTF-----CGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYP---RWITKE 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  816 AQDLITLLLRQNPLERLGTGGayEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFD 875
Cdd:cd05620    223 SKDILEKLFERDPTRRLGVVG--NIRGHPFFKTINWTALEKRELDppFKPKVKSPSDYSNFD 282
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
572-874 1.70e-61

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: 214.78  E-value: 1.70e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRH---KESRQRFAMKKINKQNLILRNQIQQ-AFVERDILTFA-ENPFVVSMYCSFETRRHL 646
Cdd:cd05614      1 NFELLKVLGTGAYGKVFLVRKvsgHDANKLYAMKVLRKAALVQKAKTVEhTRTERNVLEHVrQSPFLVTLHYAFQTDAKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmt 726
Cdd:cd05614     81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSK------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyEGHIEKDAREFldkQVCGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVGCVPFF----GDTPEELFGQVISD 801
Cdd:cd05614    154 ----EFLTEEKERTY---SFCGTIEYMAPEIIRGKsGHGKAVDWWSLGILMFELLTGASPFTlegeKNTQSEVSRRILKC 226
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  802 EINWPEKdeaPPPDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYF 874
Cdd:cd05614    227 DPPFPSF---IGPVARDLLQKLLCKDPKKRLGAGpqGAQEIKEHPFFKGLDWEALALRKvnPPFRPSIRSELDVGNF 300
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
582-849 3.89e-61

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: 211.48  E-value: 3.89e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRH---KESRQRFAMKKINKQNLILRNQIQQ-AFVERDIL-TFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd05583      5 GAYGKVFLVRKvggHDAGKLYAMKVLKKATIVQKAKTAEhTMTERQVLeAVRQSPFLVTLHYAFQTDAKLHLILDYVNGG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMsmttnlyeghiEK 736
Cdd:cd05583     85 ELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLP-----------GE 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREFldkQVCGTPEYIAPEVILR--QGYGKPVDWWAMGIILYEFLVGCVPFfgdTPEElfGQVISDEINWPEKDEAPP- 813
Cdd:cd05583    154 NDRAY---SFCGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPF---TVDG--ERNSQSEISKRILKSHPPi 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1988312908  814 -----PDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSL 849
Cdd:cd05583    226 pktfsAEAKDFILKLLEKDPKKRLGAGprGAHEIKEHPFFKGL 268
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
572-875 5.29e-61

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: 216.03  E-value: 5.29e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05624     73 DFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVMD 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLM-KNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGlskvGLMSMTTnly 730
Cdd:cd05624    153 YYVGGDLLTLLsKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG----SCLKMND--- 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHIEKDArefldkqVCGTPEYIAPEVI--LRQG---YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE--I 803
Cdd:cd05624    226 DGTVQSSV-------AVGTPDYISPEILqaMEDGmgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerF 298
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  804 NWPEKDEAPPPDAQDLITLLLRQNPlERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDDTSYFD 875
Cdd:cd05624    299 QFPSHVTDVSEEAKDLIQRLICSRE-RRLGQNGIEDFKKHAFFEGLNWENIRNLEAPYIPDVSSPSDTSNFD 369
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
577-876 2.65e-60

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: 211.20  E-value: 2.65e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAEN-PFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05591      1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKhPFLTALHSCFQTKDRLFFVMEYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMS-MTTNLYeghi 734
Cdd:cd05591     81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNgKTTTTF---- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 ekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP---EKdea 811
Cdd:cd05591    157 ------------CGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPvwlSK--- 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  812 pppDAQDLITLLLRQNPLERLG----TGGAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDDTSYFDT 876
Cdd:cd05591    222 ---EAVSILKAFMTKNPAKRLGcvasQGGEDAIRQHPFFREIDWEALEQRKVKppFKPKIKTKRDANNFDQ 289
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
572-875 3.46e-60

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: 210.63  E-value: 3.46e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFA-ENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05616      1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSgKPPFLTQLHSCFQTMDRLYFVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtTNLY 730
Cdd:cd05616     81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK-------ENIW 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGhiekdareFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdE 810
Cdd:cd05616    154 DG--------VTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYP---K 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  811 APPPDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEdDTSYFD 875
Cdd:cd05616    223 SMSKEAVAICKGLMTKHPGKRLGCGpeGERDIKEHAFFRYIDWEKLERKEIQppYKPKACGR-NAENFD 290
PDZ_MAST4 cd23076
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ ...
1141-1235 7.48e-60

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 4 (MAST4); PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST4, and related domains. MAST4 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST4 is a component of the AICD-MAST4-FOXO1-RTKN2 neuroprotective pathway; MAST4 phosphorylation of forkhead box protein O1 (FOXO1) regulates rhotekin 2 (RTKN2) expression. As this pathway is repressed in Alzheimer's Disease (AD), MAST4 may play a role in preventing AD pathogenesis. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST4 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467289 [Multi-domain]  Cd Length: 95  Bit Score: 200.64  E-value: 7.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1141 PHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKS 1220
Cdd:cd23076      1 PHQPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKS 80
                           90
                   ....*....|....*
gi 1988312908 1221 GNKVSITTTPFENTS 1235
Cdd:cd23076     81 GNKVSITTTPFENTS 95
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
556-879 1.73e-59

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 209.45  E-value: 1.73e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  556 SSSNASLKLRRKPRESDFETIKLISNGAYGAVYFVRHK-ESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVV 634
Cdd:PTZ00426    15 SDSTKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKnEDFPPVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  635 SMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTD 714
Cdd:PTZ00426    95 NLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTD 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  715 FGLSKVglmsmttnlyeghieKDAREFldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:PTZ00426   175 FGFAKV---------------VDTRTY---TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLI 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  795 FGQVISDEINWPEKDEApppDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQKAE--FIPQLESEDD 870
Cdd:PTZ00426   237 YQKILEGIIYFPKFLDN---NCKHLMKKLLSHDLTKRYGNlkKGAQNVKEHPWFGNIDWVSLLHKNVEvpYKPKYKNVFD 313

                   ....*....
gi 1988312908  871 TSYFDTRSE 879
Cdd:PTZ00426   314 SSNFERVQE 322
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
576-932 3.40e-59

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: 207.89  E-value: 3.40e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDIL-TFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd05604      1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLyeghi 734
Cdd:cd05604     81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTT----- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 ekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPpp 814
Cdd:cd05604    156 ----------TFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLT-- 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  815 dAQDLITLLLRQNPLERLGTGGAY-EVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYFDtrsekyhhmeteeedd 891
Cdd:cd05604    224 -AWSILEELLEKDRQLRLGAKEDFlEIKNHPFFESINWTDLVQKKipPPFNPNVNGPDDISNFD---------------- 286
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1988312908  892 tndEDFNVEIRQFSSCshrfskvFSSIDRITQNSAEEKEDS 932
Cdd:cd05604    287 ---AEFTEEMVPYSVC-------VSSDYSIVNASVLEADDA 317
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
560-875 1.59e-58

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: 209.10  E-value: 1.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  560 ASLKLRRKPREsDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCS 639
Cdd:cd05623     62 SKVKQMRLHKE-DFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYA 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 FETRRHLCMVMEYVEGGDCATLM-KNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGlS 718
Cdd:cd05623    141 FQDDNNLYLVMDYYVGGDLLTLLsKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFG-S 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 KVGLMSmttnlyEGHIEKDArefldkqVCGTPEYIAPEVI--LRQG---YGKPVDWWAMGIILYEFLVGCVPFFGDTPEE 793
Cdd:cd05623    220 CLKLME------DGTVQSSV-------AVGTPDYISPEILqaMEDGkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVE 286
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  794 LFGQVIS--DEINWPEKDEAPPPDAQDLITLLLRQNPlERLGTGGAYEVKQHRFFRSLDWNSLLRQKAEFIPQLESEDDT 871
Cdd:cd05623    287 TYGKIMNhkERFQFPTQVTDVSENAKDLIRRLICSRE-HRLGQNGIEDFKNHPFFVGIDWDNIRNCEAPYIPEVSSPTDT 365

                   ....
gi 1988312908  872 SYFD 875
Cdd:cd05623    366 SNFD 369
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
572-831 2.85e-58

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: 202.69  E-value: 2.85e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd08215      1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKER-EEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNM----GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTT 727
Cdd:cd08215     80 YADGGDLAQKIKKQkkkgQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKV--LESTT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NLyeghiekdArefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEInwpe 807
Cdd:cd08215    158 DL--------A-----KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQY---- 220
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  808 kdeAPPPDA-----QDLITLLLRQNPLER 831
Cdd:cd08215    221 ---PPIPSQysselRDLVNSMLQKDPEKR 246
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
577-876 1.63e-57

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: 203.04  E-value: 1.63e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAEN-PFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05588      1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNhPFLVGLHSCFQTESRLFFVIEFVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSM-TTNLYeghi 734
Cdd:cd05588     81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGdTTSTF---- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 ekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF----FGDTPEE-----LFGQVISDEINW 805
Cdd:cd05588    157 ------------CGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgSSDNPDQntedyLFQVILEKPIRI 224
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  806 PEKDEApppDAQDLITLLLRQNPLERLG---TGGAYEVKQHRFFRSLDWNSLLRQKA--EFIPQLESEDDTSYFDT 876
Cdd:cd05588    225 PRSLSV---KAASVLKGFLNKNPAERLGchpQTGFADIQSHPFFRTIDWEQLEQKQVtpPYKPRIESERDLENFDP 297
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
579-863 7.40e-57

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: 199.29  E-value: 7.40e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd05577      1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGPLPVDMARMYF--AETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkVGLMSMTTNlyeghiek 736
Cdd:cd05577     81 KYHIYNVGTRGFSEARAIFyaAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLA-VEFKGGKKI-------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 darefldKQVCGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVGCVPFFGD----TPEELFGQVISDEINWPEKDEa 811
Cdd:cd05577    152 -------KGRVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYPDSFS- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  812 ppPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQKAE--FIP 863
Cdd:cd05577    224 --PEARSLCEGLLQKDPERRLGCrgGSADEVKEHPFFRSLNWQRLEAGMLEppFVP 277
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
572-846 9.09e-57

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: 198.20  E-value: 9.09e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd05122      1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILN---EIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKN-MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNly 730
Cdd:cd05122     78 FCSGGSLKDLLKNtNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRN-- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFGQVISDEINWPEKd 809
Cdd:cd05122    156 --------------TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPmKALFLIATNGPPGLRNP- 220
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  810 EAPPPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd05122    221 KKWSKEFKDFLKKCLQKDPEKR---PTAEQLLKHPFI 254
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
569-879 1.81e-56

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: 200.61  E-value: 1.81e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENP-FVVSMYCSFETRRHLC 647
Cdd:cd05615      8 RLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPpFLTQLHSCFQTVDRLY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTT 727
Cdd:cd05615     88 FVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVT 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NlyeghiekdaREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPe 807
Cdd:cd05615    168 T----------RTF-----CGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYP- 231
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  808 kdEAPPPDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQKAE--FIPQL--ESEDDTSYFDTRSE 879
Cdd:cd05615    232 --KSLSKEAVSICKGLMTKHPAKRLGCGpeGERDIREHAFFRRIDWDKLENREIQppFKPKVcgKGAENFDKFFTRGQ 307
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
572-877 3.11e-55

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: 197.55  E-value: 3.11e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAE-NPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05617     16 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFLVI 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNly 730
Cdd:cd05617     96 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTT-- 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF--FGDTP-----EELFGQVISDEI 803
Cdd:cd05617    174 -------------STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiITDNPdmnteDYLFQVILEKPI 240
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  804 NWPEKDEApppDAQDLITLLLRQNPLERLG---TGGAYEVKQHRFFRSLDWNSLLRQKA--EFIPQLESEDDTSYFDTR 877
Cdd:cd05617    241 RIPRFLSV---KASHVLKGFLNKDPKERLGcqpQTGFSDIKSHTFFRSIDWDLLEKKQVtpPFKPQITDDYGLENFDTQ 316
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
572-863 1.05e-54

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: 193.68  E-value: 1.05e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRH---KESRQRFAMKKINKQNLILRNQI-QQAFVERDILT-FAENPFVVSMYCSFETRRHL 646
Cdd:cd05613      1 NFELLKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLKKATIVQKAKTaEHTRTERQVLEhIRQSPFLVTLHYAFQTDTKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMT 726
Cdd:cd05613     81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 TNLYEghiekdarefldkqVCGTPEYIAPEVIL--RQGYGKPVDWWAMGIILYEFLVGCVPFFGD----TPEELFGQVIS 800
Cdd:cd05613    161 ERAYS--------------FCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVDgeknSQAEISRRILK 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  801 DEINWPEKdeaPPPDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSLLRQK--AEFIP 863
Cdd:cd05613    227 SEPPYPQE---MSALAKDIIQRLLMKDPKKRLGCGpnGADEIKKHPFFQKINWDDLAAKKvpAPFKP 290
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
582-846 2.03e-54

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: 192.00  E-value: 2.03e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLI-------LRNQIQQAF--VER--DILTFAENPFVVSMYcsfE-----TRRH 645
Cdd:cd14008      4 GSFGKVKLALDTETGQLYAIKIFNKSRLRkrregknDRGKIKNALddVRReiAIMKKLDHPNIVRLY---EviddpESDK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGdcaTLMK-----NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV 720
Cdd:cd14008     81 LYLVLEYCEGG---PVMEldsgdRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEM 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  721 glmsmttnlyeghIEKDAREFLDKQvcGTPEYIAPEV--ILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFgQ 797
Cdd:cd14008    158 -------------FEDGNDTLQKTA--GTPAFLAPELcdGDSKTYsGKAADIWALGVTLYCLVFGRLPFNGDNILELY-E 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908  798 VISDEINWPEKDEAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14008    222 AIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRI---TLKEIKEHPWV 267
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
579-843 3.70e-54

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 189.40  E-value: 3.70e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd00180      1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMK-NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyegHIEKD 737
Cdd:cd00180     79 KDLLKeNKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAK-------------DLDSD 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  738 AREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFlvgcvpffgdtpeelfgqvisdeinwpekdeappPDAQ 817
Cdd:cd00180    146 DSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL----------------------------------EELK 191
                          250       260
                   ....*....|....*....|....*.
gi 1988312908  818 DLITLLLRQNPLERLgtgGAYEVKQH 843
Cdd:cd00180    192 DLIRRMLQYDPKKRP---SAKELLEH 214
PDZ_MAST cd06705
PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family; PDZ ...
1143-1233 1.02e-53

PDZ domain of the microtubule-associated serine-threonine (MAST) protein kinase family; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinases, including MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. The PDZ domain gives the MAST family the capacity to scaffold its own kinase activity. These kinases are implicated in the inhibition of neurite outgrowth and regeneration in cultured cells. Their binding partners include microtubules, beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), and PTEN. This family also includes Caenorhabditis elegans KIN-4 MAST kinase, a key longevity factor acting through binding PTEN phosphatase, and Drosophila Drop out which regulates dynein-dependent transport during embryonic development. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467189 [Multi-domain]  Cd Length: 93  Bit Score: 182.83  E-value: 1.02e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1143 QPIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGN 1222
Cdd:cd06705      3 PPIVIKKGPRGFGFTLRAIRVYIGDSDVYTVHHLVTAVEEGSPAYEAGLRPGDLITHVNGEPVQGLLHTQVVQLILKGGN 82
                           90
                   ....*....|.
gi 1988312908 1223 KVSITTTPFEN 1233
Cdd:cd06705     83 KVSIRATPLEK 93
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
577-846 3.86e-53

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: 187.85  E-value: 3.86e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiqQAFVERDI--LTFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd14081      7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESV--LMKVEREIaiMKLIEHPNVLKLYDVYENKKYLYLVLEYVS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV---GLMSMTTnlye 731
Cdd:cd14081     85 GGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLqpeGSLLETS---- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekdarefldkqvCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKde 810
Cdd:cd14081    161 ---------------CGSPHYACPEVIKGEKYdGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHF-- 223
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  811 aPPPDAQDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14081    224 -ISPDAQDLLRRMLEVNPEKRITIE---EIKKHPWF 255
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
576-837 3.96e-53

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: 188.18  E-value: 3.96e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAE--NPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14014      5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELA--EDEEFRERFLREARALARlsHPNIVRVYDVGEDDGRPYIVMEYV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttnlyegh 733
Cdd:cd14014     83 EGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARA------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINwPEKDEAP- 812
Cdd:cd14014    150 -LGDSGLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPP-PPSPLNPd 227
                          250       260
                   ....*....|....*....|....*.
gi 1988312908  813 -PPDAQDLITLLLRQNPLERLGTGGA 837
Cdd:cd14014    228 vPPALDAIILRALAKDPEERPQSAAE 253
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
569-875 4.82e-52

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: 187.92  E-value: 4.82e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDIL-TFAENPFVVSMYCSFETRRHLC 647
Cdd:cd05602      5 KPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDKLY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTT 727
Cdd:cd05602     85 FVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGT 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NlyeghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW-P 806
Cdd:cd05602    165 T---------------STFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLkP 229
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  807 EKDEApppdAQDLITLLLRQNPLERLGTGGAY-EVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYFD 875
Cdd:cd05602    230 NITNS----ARHLLEGLLQKDRTKRLGAKDDFtEIKNHIFFSPINWDDLINKKitPPFNPNVSGPNDLRHFD 297
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
577-846 5.16e-52

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: 184.65  E-value: 5.16e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILR--NQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd06606      6 ELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEelEALER---EIRILSSLKHPNIVRYLGTERTENTLNIFLEYVP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyegHI 734
Cdd:cd06606     83 GGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAK-------------RL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 EKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF--FGDTPEELFGQVISDEInwPEKDEAP 812
Cdd:cd06606    150 AEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWseLGNPVAALFKIGSSGEP--PPIPEHL 227
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  813 PPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06606    228 SEEAKDFLRKCLQRDPKKR---PTADELLQHPFL 258
PDZ_MAST3 cd23075
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 3 (MAST3); PDZ ...
1144-1234 7.88e-52

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 3 (MAST3); PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST3, and related domains. MAST3 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST3 plays a critical role in regulating the immune response of inflammatory bowel disease (IBD), and is involved in the process of cytoskeleton organization, intracellular signal transduction and peptidyl-serine phosphorylation. MAST3 also promotes the proliferation and inflammation of fibroblast-like synoviocytes in rheumatoid arthritis. Binding partners of MAST3 include cAMP-regulated phosphoprotein (ARPP-16) and the tumor suppressor PTEN. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST3 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467288 [Multi-domain]  Cd Length: 94  Bit Score: 177.53  E-value: 7.88e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1144 PIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNK 1223
Cdd:cd23075      4 PIIIHSSGKKYGFTLRAIRVYMGDSDVYTVHHMVWSVEDGSPAQEAGLRAGDLITHINGESVLGLVHMDVVELLLKSGNK 83
                           90
                   ....*....|.
gi 1988312908 1224 VSITTTPFENT 1234
Cdd:cd23075     84 VSLRTTALENT 94
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
576-846 1.18e-51

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: 183.92  E-value: 1.18e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKES--RQRFAMKKINkqnlilRNQIQQAFVER------DILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd14080      5 GKTIGEGSYSKVKLAEYTKSglKEKVACKIID------KKKAPKDFLEKflprelEILRKLRHPNIIQVYSIFERGSKVF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtt 727
Cdd:cd14080     79 IFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFAR-------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyegHIEKDAREFLDKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP 806
Cdd:cd14080    151 -----LCPDDDGDVLSKTFCGSAAYAAPEILQGIPYdPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFP 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  807 EKDEAPPPDAQDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14080    226 SSVKKLSPECKDLIDQLLEPDPTKRATIE---EILNHPWL 262
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
572-877 4.73e-51

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: 185.62  E-value: 4.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAEN-PFVVSMYCSFETRRHLCMVM 650
Cdd:cd05618     21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNhPFLVGLHSCFQTESRLFFVI 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNly 730
Cdd:cd05618    101 EYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT-- 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF----FGDTPEE-----LFGQVISD 801
Cdd:cd05618    179 -------------STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgSSDNPDQntedyLFQVILEK 245
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  802 EINWPEKDEApppDAQDLITLLLRQNPLERLG---TGGAYEVKQHRFFRSLDWNsLLRQKA---EFIPQLESEDDTSYFD 875
Cdd:cd05618    246 QIRIPRSLSV---KAASVLKSFLNKDPKERLGchpQTGFADIQGHPFFRNVDWD-LMEQKQvvpPFKPNISGEFGLDNFD 321

                   ..
gi 1988312908  876 TR 877
Cdd:cd05618    322 SQ 323
PDZ_MAST1 cd23073
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 ...
1144-1235 7.96e-51

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 1; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST family kinase MAST1, and related domains. MAST1 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain; MAST family member MASTL is a shorter protein lacking the PDZ domain. MAST1 functions as a scaffold protein to link the dystrophin/utrophin network with microfilaments via syntrophin, and it has been identified as a main driver of cisplatin resistance in human cancers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST1 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467286 [Multi-domain]  Cd Length: 95  Bit Score: 174.83  E-value: 7.96e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1144 PIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNK 1223
Cdd:cd23073      4 PITIQRSGKKYGFTLRAIRVYMGDSDVYSVHHIVWHVEEGGPAQEAGLCAGDLITHVNGEPVHGMVHPEVVELILKSGNK 83
                           90
                   ....*....|..
gi 1988312908 1224 VSITTTPFENTS 1235
Cdd:cd23073     84 VAVTTTPFENTS 95
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
573-844 1.24e-50

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: 180.60  E-value: 1.24e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVErdILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14095      2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIENEVA--ILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLP-VDMARMyFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG----HIKLTDFGLSKVglmsMTT 727
Cdd:cd14095     80 VKGGDLFDAITSSTKFTeRDASRM-VTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATE----VKE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NLYeghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD--TPEELFGQVISDEInw 805
Cdd:cd14095    155 PLF--------------TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPdrDQEELFDLILAGEF-- 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1988312908  806 pekdEAPPP-------DAQDLITLLLRQNPLERLgtgGAYEVKQHR 844
Cdd:cd14095    219 ----EFLSPywdnisdSAKDLISRMLVVDPEKRY---SAGQVLDHP 257
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
577-875 1.53e-50

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: 182.86  E-value: 1.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDIL-TFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05603      1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlyeghie 735
Cdd:cd05603     81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETT------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  736 kdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP-EKDEAppp 814
Cdd:cd05603    154 --------STFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPgGKTVA--- 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  815 dAQDLITLLLRQNPLERLGTGGAY-EVKQHRFFRSLDWNSLLRQK--AEFIPQLESEDDTSYFD 875
Cdd:cd05603    223 -ACDLLQGLLHKDQRRRLGAKADFlEIKNHVFFSPINWDDLYHKRitPPYNPNVAGPADLRHFD 285
Pkinase pfam00069
Protein kinase domain;
573-846 7.54e-50

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 177.05  E-value: 7.54e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEK-IKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEylhnygivhrdlkpdnllvtsmGHIKLTDFglskvglmsmttnlyeg 732
Cdd:pfam00069   80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLE----------------------SGSSLTTF----------------- 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAP 812
Cdd:pfam00069  121 --------------VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNL 186
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  813 PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:pfam00069  187 SEEAKDLLKKLLKKDPSKRL---TATQALQHPWF 217
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
572-845 1.09e-49

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: 177.98  E-value: 1.09e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14663      1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGlmsmttnlye 731
Cdd:cd14663     81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALS---------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiEKDAREFLDKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdE 810
Cdd:cd14663    151 ---EQFRQDGLLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYP---R 224
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1988312908  811 APPPDAQDLITLLLRQNPLERLGTGgayEVKQHRF 845
Cdd:cd14663    225 WFSPGAKSLIKRILDPNPSTRITVE---QIMASPW 256
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
573-831 3.19e-49

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 184.06  E-value: 3.19e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:COG0515      9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVL-RPELAADPEARERFRrEARALARLNHPNIVRVYDVGEEDGRPYLVME 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlye 731
Cdd:COG0515     88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTQ--- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekdareflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:COG0515    165 -----------TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRP 233
                          250       260
                   ....*....|....*....|.
gi 1988312908  812 P-PPDAQDLITLLLRQNPLER 831
Cdd:COG0515    234 DlPPALDAIVLRALAKDPEER 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
579-833 4.01e-49

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: 176.26  E-value: 4.01e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLI--LRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14009      1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNkkLQENLES---EIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSKvglmsmttnlyegH 733
Cdd:cd14009     78 DLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFAR-------------S 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEKDArefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPP 813
Cdd:cd14009    145 LQPAS---MAETLCGSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQL 221
                          250       260
                   ....*....|....*....|.
gi 1988312908  814 -PDAQDLITLLLRQNPLERLG 833
Cdd:cd14009    222 sPDCKDLLRRLLRRDPAERIS 242
PDZ_MAST2 cd23074
PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 ...
1144-1233 8.42e-49

PDZ domain of microtubule-associated serine-threonine (MAST) protein kinase 2; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of MAST2 (also known as microtubule-associated serine/threonine kinase-205 kD, MAST205) , and related domains. MAST2 belongs to the MAST family kinases, which include MAST1-4. These MAST proteins contain a DUF1908 domain, a serine/threonine kinase domain, a AGC-kinase C-terminal domain, and a PDZ domain. MAST2 may function to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Binding partners of MAST2 include beta2-syntrophin, TNF receptor-associated factor 6 (TRAF6), cAMP-regulated phosphoprotein (ARPP-16), Na+/H+ exchanger NHE3 (SLC9A3) and PTEN. MAST2 is also associated with microtubules of the spermatid manchette. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAST2 family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467287 [Multi-domain]  Cd Length: 93  Bit Score: 169.04  E-value: 8.42e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1144 PIVIHSSGKNYGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNK 1223
Cdd:cd23074      4 PIIIHRAGKKYGFTLRAIRVYMGDSDVYTVHHMVWHVEDGGPASEAGLRQGDLITHVNGEPVHGLVHTEVVELILKSGNK 83
                           90
                   ....*....|
gi 1988312908 1224 VSITTTPFEN 1233
Cdd:cd23074     84 VSISTTPLEN 93
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
572-833 9.65e-49

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: 175.13  E-value: 9.65e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQN------LILRNQIqqafverDILTFAENPFVVSMYCSFETRRH 645
Cdd:cd14002      2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGksekelRNLRQEI-------EILRKLNHPNIIEMLDSFETKKE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGgDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSM 725
Cdd:cd14002     75 FVVVTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARA--MSC 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TTNLYeghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW 805
Cdd:cd14002    152 NTLVL-------------TSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKW 218
                          250       260
                   ....*....|....*....|....*...
gi 1988312908  806 PekdEAPPPDAQDLITLLLRQNPLERLG 833
Cdd:cd14002    219 P---SNMSPEFKSFLQGLLNKDPSKRLS 243
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
572-833 2.58e-47

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: 171.03  E-value: 2.58e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLIlRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd08530      1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSLS-QKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMG----PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsMTT 727
Cdd:cd08530     80 YAPFGDLSKLISKRKkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKV----LKK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NLYEGHIekdarefldkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDeinwpe 807
Cdd:cd08530    156 NLAKTQI-------------GTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRG------ 216
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  808 KDEAPPP----DAQDLITLLLRQNPLERLG 833
Cdd:cd08530    217 KFPPIPPvysqDLQQIIRSLLQVNPKKRPS 246
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
577-834 3.38e-47

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: 171.42  E-value: 3.38e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLiLRNQIQQAFVERDILTFAE------NPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14084     12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRKF-TIGSRREINKPRNIETEIEilkklsHPCIIKIEDFFDAEDDYYIVL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSKVglmsmtt 727
Cdd:cd14084     91 ELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKI------- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyeghIEKDArefLDKQVCGTPEYIAPEVIL---RQGYGKPVDWWAMGIILYEFLVGCVPFFGD-TPEELFGQVISDEI 803
Cdd:cd14084    164 ------LGETS---LMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEyTQMSLKEQILSGKY 234
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1988312908  804 NW-PEKDEAPPPDAQDLITLLLRQNPLERLGT 834
Cdd:cd14084    235 TFiPKAWKNVSEEAKDLVKKMLVVDPSRRPSI 266
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
573-863 7.55e-47

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: 171.00  E-value: 7.55e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05605      2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGP--LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnly 730
Cdd:cd05605     82 MNGGDLKFHIYNMGNpgFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLA------------ 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghIEKDAREFLDKQVcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP----EELFGQVISDEINWP 806
Cdd:cd05605    150 ---VEIPEGETIRGRV-GTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEkvkrEEVDRRVKEDQEEYS 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  807 EKdeaPPPDAQDLITLLLRQNPLERLG--TGGAYEVKQHRFFRSLDWNSL--LRQKAEFIP 863
Cdd:cd05605    226 EK---FSEEAKSICSQLLQKDPKTRLGcrGEGAEDVKSHPFFKSINFKRLeaGLLEPPFVP 283
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
573-854 3.14e-46

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: 169.31  E-value: 3.14e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05607      4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARM--YFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLY 730
Cdd:cd05607     84 MNGGDLKYHIYNVGERGIEMERVifYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLA--------VEVK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHIEkdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD----TPEELFGQVISDEINWP 806
Cdd:cd05607    156 EGKPI--------TQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEDEVKFE 227
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908  807 EKDEAPPpdAQDLITLLLRQNPLERLGTGGAY-EVKQHRFFRSLDWNSL 854
Cdd:cd05607    228 HQNFTEE--AKDICRLFLAKKPENRLGSRTNDdDPRKHEFFKSINFPRL 274
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
572-846 9.11e-46

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: 166.57  E-value: 9.11e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14099      2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmTTNLYE 731
Cdd:cd14099     82 LCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLA-------ARLEYD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 GhiEKdareflDKQVCGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDE 810
Cdd:cd14099    155 G--ER------KKTLCGTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLS 226
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  811 APPPdAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14099    227 ISDE-AKDLIRSMLQPDPTKRP---SLDEILSHPFF 258
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
572-831 1.05e-45

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: 166.88  E-value: 1.05e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14098      1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQrEINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG--HIKLTDFGLSKVglmsmttn 728
Cdd:cd14098     81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKV-------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghIEKDAreFLdKQVCGTPEYIAPEVIL------RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE 802
Cdd:cd14098    153 -----IHTGT--FL-VTFCGTMAYLAPEILMskeqnlQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGR 224
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  803 INW-PEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd14098    225 YTQpPLVDFNISEEAIDFILRLLDVDPEKR 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
571-850 8.12e-45

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: 164.30  E-value: 8.12e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKqnLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd06623      1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHV--DGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNY-GIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsMTTNL 729
Cdd:cd06623     79 EYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKV----LENTL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 YEghiekdAREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD---TPEELFGQVISDE-INW 805
Cdd:cd06623    155 DQ------CNTF-----VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPgqpSFFELMQAICDGPpPSL 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908  806 PekDEAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSLD 850
Cdd:cd06623    224 P--AEEFSPEFRDFISACLQKDPKKRP---SAAELLQHPFIKKAD 263
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
579-845 5.65e-44

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: 162.08  E-value: 5.65e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAF-VERDIltfaENPFVVSMYCSFETRRHLCMVMEYVEGGD 657
Cdd:cd14010      8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSK---RPEVLNEVrLTHEL----KHPNVLKFYEWYETSNHLWLVVEYCTGGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVgLMSMTTNLYEGHIEKD 737
Cdd:cd14010     81 LETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARR-EGEILKELFGQFSDEG 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  738 AREFLDKQ--VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP--EKDEAPP 813
Cdd:cd14010    160 NVNKVSKKqaKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPppKVSSKPS 239
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1988312908  814 PDAQDLITLLLRQNPLERLGTGgayEVKQHRF 845
Cdd:cd14010    240 PDFKSLLKGLLEKDPAKRLSWD---ELVKHPF 268
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
573-854 1.41e-43

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: 161.34  E-value: 1.41e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05630      2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMAR--MYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLY 730
Cdd:cd05630     82 MNGGDLKFHIYHMGQAGFPEARavFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA--------VHVP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHIEKDArefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFfgdtpEELFGQVISDEIN------ 804
Cdd:cd05630    154 EGQTIKGR--------VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPF-----QQRKKKIKREEVErlvkev 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  805 WPEKDEAPPPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSL 854
Cdd:cd05630    221 PEEYSEKFSPQARSLCSMLLCKDPAERLGCrgGGAREVKEHPLFKKLNFKRL 272
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
573-854 2.09e-43

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: 161.20  E-value: 2.09e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05608      3 FLDFRVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGP----LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttn 728
Cdd:cd05608     83 MNGGDLRYHIYNVDEenpgFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLA---------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF--FGDTPE--ELFGQVISDEIN 804
Cdd:cd05608    153 -----VELKDGQTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFraRGEKVEnkELKQRILNDSVT 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  805 WPEKDEappPDAQDLITLLLRQNPLERLG--TGGAYEVKQHRFFRSLDWNSL 854
Cdd:cd05608    228 YSEKFS---PASKSICEALLAKDPEKRLGfrDGNCDGLRTHPFFRDINWRKL 276
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
582-846 5.00e-43

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: 158.97  E-value: 5.00e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDI--LTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCA 659
Cdd:cd14079     13 GSFGKVKLAEHELTGHKVAVKILNRQKI--KSLDMEEKIRREIqiLKLFRHPHIIRLYEVIETPTDIFMVMEYVSGGELF 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  660 TLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnlyegHIEKDAr 739
Cdd:cd14079     91 DYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLS--------------NIMRDG- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  740 EFLdKQVCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEappPDAQD 818
Cdd:cd14079    156 EFL-KTSCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLS---PGARD 231
                          250       260
                   ....*....|....*....|....*...
gi 1988312908  819 LITLLLRQNPLERLGTggaYEVKQHRFF 846
Cdd:cd14079    232 LIKRMLVVDPLKRITI---PEIRQHPWF 256
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
579-843 1.83e-42

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: 157.91  E-value: 1.83e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLI--------------------LRNQIQQAFVERDILTFAENPFVVSMyc 638
Cdd:cd14118      2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLkqagffrrppprrkpgalgkPLDPLDRVYREIAILKKLDHPNVVKL-- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  639 sFET-----RRHLCMVMEYVEGGDCATLMKNmGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLT 713
Cdd:cd14118     80 -VEVlddpnEDNLYMVFELVDKGAVMEVPTD-NPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  714 DFGLSkvglmsmttNLYEGhieKDAreFLDKQVcGTPEYIAPEVIL--RQGY-GKPVDWWAMGIILYEFLVGCVPFFGDT 790
Cdd:cd14118    158 DFGVS---------NEFEG---DDA--LLSSTA-GTPAFMAPEALSesRKKFsGKALDIWAMGVTLYCFVFGRCPFEDDH 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  791 PEELFGQVISDEINWPEKDEApPPDAQDLITLLLRQNPLERLGTGgayEVKQH 843
Cdd:cd14118    223 ILGLHEKIKTDPVVFPDDPVV-SEQLKDLILRMLDKNPSERITLP---EIKEH 271
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
578-858 3.38e-42

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: 157.21  E-value: 3.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDIL----TFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd05606      1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLslvsTGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglmsmttnlyegh 733
Cdd:cd05606     81 NGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGL---------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdAREFLDKQ---VCGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGDTPE---ELFGQVISDEINWP 806
Cdd:cd05606    145 ----ACDFSKKKphaSVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKdkhEIDRMTLTMNVELP 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  807 EKDEappPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQK 858
Cdd:cd05606    221 DSFS---PELKSLLEGLLQRDVSKRLGClgRGATEVKEHPFFKGVDWQQVYLQK 271
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
573-854 2.29e-41

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: 155.15  E-value: 2.29e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05631      2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMAR--MYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLY 730
Cdd:cd05631     82 MNGGDLKFHIYNMGNPGFDEQRaiFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLA--------VQIP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGhiekdarEFLDKQVcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP----EELFGQVISDEINWP 806
Cdd:cd05631    154 EG-------ETVRGRV-GTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKErvkrEEVDRRVKEDQEEYS 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988312908  807 EKDEApppDAQDLITLLLRQNPLERLG-TG-GAYEVKQHRFFRSLDWNSL 854
Cdd:cd05631    226 EKFSE---DAKSICRMLLTKNPKERLGcRGnGAAGVKQHPIFKNINFKRL 272
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
571-846 8.74e-41

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: 152.50  E-value: 8.74e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQ-NLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd06605      1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEiDEALQKQILR---ELDVLHKCNSPYIVGFYGAFYSEGDISIC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVD-MARMYFAeTVLALEYLHN-YGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMtt 727
Cdd:cd06605     78 MEYMDGGSLDKILKEVGRIPERiLGKIAVA-VVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSL-- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyeghiekdAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF------FGDTPEELFGQVIsd 801
Cdd:cd06605    155 ----------AKTFV-----GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYpppnakPSMMIFELLSYIV-- 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  802 einwpekDEAPP--------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06605    218 -------DEPPPllpsgkfsPDFQDFVSQCLQKDPTER---PSYKELMEHPFI 260
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
571-846 1.04e-40

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: 152.10  E-value: 1.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQN--LILRNQIQQAFVERDILTfaeNPFVVSMYCSFETRRHLCM 648
Cdd:cd14069      1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRapGDCPENIKKEVCIQKMLS---HKNVVRFYGHRREGEFQYL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDcatLMKNMGP---LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsm 725
Cdd:cd14069     78 FLEYASGGE---LFDKIEPdvgMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATV----- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyegHIEKDAREFLDKQvCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFfgDTPEELfGQVISDEIN 804
Cdd:cd14069    150 -------FRYKGKERLLNKM-CGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGELPW--DQPSDS-CQEYSDWKE 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1988312908  805 WPEKDEAP----PPDAQDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14069    219 NKKTYLTPwkkiDTAALSLLRKILTENPNKRITIE---DIKKHPWY 261
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
579-831 3.72e-40

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: 150.00  E-value: 3.72e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKesRQRFAMKKINKQNLilRNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGD 657
Cdd:cd13999      1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDD--NDELLKEFRrEVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLM-KNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV---GLMSMTTnlyegh 733
Cdd:cd13999     77 LYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIknsTTEKMTG------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIsdeinwpEKDEAPP 813
Cdd:cd13999    151 ------------VVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVV-------QKGLRPP 211
                          250       260
                   ....*....|....*....|....
gi 1988312908  814 PDA---QDLITLLLR---QNPLER 831
Cdd:cd13999    212 IPPdcpPELSKLIKRcwnEDPEKR 235
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
579-832 9.53e-40

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: 148.96  E-value: 9.53e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQnLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd14006      1 LGRGRFGVVKRCIEKATGREFAAKFIPKR-DKKKEAVLR---EISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG--HIKLTDFGLSKvglmsmttnlyeghieK 736
Cdd:cd14006     77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLAR----------------K 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW-PEKDEAPPPD 815
Cdd:cd14006    141 LNPGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFsEEYFSSVSQE 220
                          250
                   ....*....|....*..
gi 1988312908  816 AQDLITLLLRQNPLERL 832
Cdd:cd14006    221 AKDFIRKLLVKEPRKRP 237
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
573-854 1.27e-39

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: 150.89  E-value: 1.27e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05632      4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVLTI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYF--AETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLY 730
Cdd:cd05632     84 MNGGDLKFHIYNMGNPGFEEERALFyaAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLA--------VKIP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGhiekdarEFLDKQVcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP----EELFGQVISDEINWP 806
Cdd:cd05632    156 EG-------ESIRGRV-GTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYS 227
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988312908  807 EKDEApppDAQDLITLLLRQNPLERLGTG--GAYEVKQHRFFRSLDWNSL 854
Cdd:cd05632    228 AKFSE---EAKSICKMLLTKDPKQRLGCQeeGAGEVKRHPFFRNMNFKRL 274
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
573-837 1.79e-39

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: 149.76  E-value: 1.79e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLI----LRNQIQqafverdILTFAENPFVVSMYCSFETRRHLCM 648
Cdd:cd14166      5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSrdssLENEIA-------VLKRIKHENIVTLEDIYESTTHYYL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS---MGHIKLTDFGLSKV---GL 722
Cdd:cd14166     78 VMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTpdeNSKIMITDFGLSKMeqnGI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 MSMTtnlyeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE 802
Cdd:cd14166    158 MSTA--------------------CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGY 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  803 INWpekdEAPPPD-----AQDLITLLLRQNPLERLGTGGA 837
Cdd:cd14166    218 YEF----ESPFWDdisesAKDFIRHLLEKNPSKRYTCEKA 253
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
573-837 1.91e-39

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: 148.45  E-value: 1.91e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKqnlilRNQIQQAF-VERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14087      3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET-----KCRGREVCeSELNVLRRVRHTNIIQLIEVFETKERVYMVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSkvglmsmttn 728
Cdd:cd14087     78 LATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLA---------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyegHIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIN---- 804
Cdd:cd14087    148 ----STRKKGPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSysge 223
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  805 -WPEKDEApppdAQDLITLLLRQNPLERLGTGGA 837
Cdd:cd14087    224 pWPSVSNL----AKDFIDRLLTVNPGERLSATQA 253
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
573-843 2.36e-39

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: 148.17  E-value: 2.36e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAfvERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14185      2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIES--EILIIKSLSHPNIVKLFEVYETEKEIYLILEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT----SMGHIKLTDFGLSKVGLMSMTTn 728
Cdd:cd14185     80 VRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQhnpdKSTTLKLADFGLAKYVTGPIFT- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD--TPEELFGQVISDEIN-- 804
Cdd:cd14185    159 -----------------VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEfl 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  805 ---WPEKDEApppdAQDLITLLLRQNPLERLgtgGAYEVKQH 843
Cdd:cd14185    222 ppyWDNISEA----AKDLISRLLVVDPEKRY---TAKQVLQH 256
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
573-831 5.26e-39

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: 147.13  E-value: 5.26e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL-----ILRNQIqqafverDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd14083      5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALkgkedSLENEI-------AVLRKIKHPNIVQLLDIYESKSHLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGG---------------DCATLMKnmgplpvdmarmyfaETVLALEYLHNYGIVHRDLKPDNLLVTSM---GH 709
Cdd:cd14083     78 LVMELVTGGelfdrivekgsytekDASHLIR---------------QVLEAVDYLHSLGIVHRDLKPENLLYYSPdedSK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  710 IKLTDFGLSKV---GLMSMTtnlyeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14083    143 IMISDFGLSKMedsGVMSTA--------------------CGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPF 202
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988312908  787 FGDTPEELFGQVISDEIN-----WPEKDEApppdAQDLITLLLRQNPLER 831
Cdd:cd14083    203 YDENDSKLFAQILKAEYEfdspyWDDISDS----AKDFIRHLMEKDPNKR 248
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
579-832 6.59e-39

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: 146.74  E-value: 6.59e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESR-QRFAMKKINKQNLILrnqiQQAFVERDILTFA----ENpfVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14120      1 IGHGAFAVVFKGRHRKKPdLPVAIKCITKKNLSK----SQNLLGKEIKILKelshEN--VVALLDCQETSSSVYLVMEYC 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---------HIKLTDFGLSKV---G 721
Cdd:cd14120     75 NGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARFlqdG 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 LMSMTtnlyeghiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISD 801
Cdd:cd14120    155 MMAAT-------------------LCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKN 215
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  802 EINWPEKDEAPPPDAQDLITLLLRQNPLERL 832
Cdd:cd14120    216 ANLRPNIPSGTSPALKDLLLGLLKRNPKDRI 246
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
573-846 3.20e-38

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: 145.05  E-value: 3.20e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnlILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd06614      2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMR----LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGdCATLMKNMGPLPVDMARMYF--AETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLY 730
Cdd:cd06614     78 MDGG-SLTDIITQNPVRMNESQIAYvcREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFA--------AQLT 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EghiEKDARefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE-LFgqVISDeiNWPEKD 809
Cdd:cd06614    149 K---EKSKR----NSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRaLF--LITT--KGIPPL 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  810 EAP---PPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06614    218 KNPekwSPEFKDFLNKCLVKDPEKR---PSAEELLQHPFL 254
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
573-831 6.05e-38

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: 144.07  E-value: 6.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL---ILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14073      3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIedeQDMVRIRR---EIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttNL 729
Cdd:cd14073     80 MEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS---------NL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 YeghiekDAREFLdKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEK 808
Cdd:cd14073    151 Y------SKDKLL-QTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQ 223
                          250       260
                   ....*....|....*....|...
gi 1988312908  809 deapPPDAQDLITLLLRQNPLER 831
Cdd:cd14073    224 ----PSDASGLIRWMLTVNPKRR 242
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
573-846 6.44e-38

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: 143.91  E-value: 6.44e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRnqiqQAFVERDIL----TFAENPFVVSMYCSFETR--RHL 646
Cdd:cd05118      1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPK----AALREIKLLkhlnDVEGHPNIVKLLDVFEHRggNHL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVeGGDCATLMK-NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIKLTDFGLSKVGlms 724
Cdd:cd05118     77 CLVFELM-GMNLYELIKdYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFGLARSF--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghiekdAREFLDKQVCgTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGcVPFF-GDTP-------EELF 795
Cdd:cd05118    153 -------------TSPPYTPYVA-TRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTG-RPLFpGDSEvdqlakiVRLL 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  796 GqvisdeinwpekdeapPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd05118    218 G----------------TPEALDLLSKMLKYDPAKRI---TASQALAHPYF 249
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
577-846 1.04e-37

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: 143.52  E-value: 1.04e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd06627      6 DLIGRGAFGSVYKGLNLNTGEFVAIKQI-SLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLyeghIEK 736
Cdd:cd06627     85 SLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVA--------TKL----NEV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREFLdkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFGQVisdeinwpeKDEAPP-- 813
Cdd:cd06627    153 EKDENS---VVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPmAALFRIV---------QDDHPPlp 220
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  814 ----PDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd06627    221 enisPELRDFLLQCFQKDPTLRP---SAKELLKHPWL 254
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
572-832 1.14e-37

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: 143.46  E-value: 1.14e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14186      2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmtTNLY 730
Cdd:cd14186     82 MCHNGEMSRYLKNRKkPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLA--------TQLK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHiEKDArefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDE 810
Cdd:cd14186    154 MPH-EKHF------TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLS 226
                          250       260
                   ....*....|....*....|..
gi 1988312908  811 ApppDAQDLITLLLRQNPLERL 832
Cdd:cd14186    227 R---EAQDLIHQLLRKNPADRL 245
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
573-846 3.40e-37

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: 141.76  E-value: 3.40e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNqIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14071      2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEEN-LKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttNLYEg 732
Cdd:cd14071     81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS---------NFFK- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hiekdAREFLdKQVCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:cd14071    151 -----PGELL-KTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMST 224
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1988312908  812 pppDAQDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14071    225 ---DCEHLIRRMLVLDPSKRLTIE---QIKKHKWM 253
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
573-831 4.87e-37

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: 141.63  E-value: 4.87e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQrFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14161      5 YEFLETLGKGTYGRVKKARDSSGRL-VAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttNLYEG 732
Cdd:cd14161     84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLS---------NLYNQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HiekdarEFLdKQVCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKdea 811
Cdd:cd14161    155 D------KFL-QTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTK--- 224
                          250       260
                   ....*....|....*....|
gi 1988312908  812 pPPDAQDLITLLLRQNPLER 831
Cdd:cd14161    225 -PSDACGLIRWLLMVNPERR 243
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
573-846 5.19e-37

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: 142.41  E-value: 5.19e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVeRDI-----LTFAENPFVVSMY-----CSFET 642
Cdd:cd07838      1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLS--EEGIPLSTI-REIallkqLESFEHPNVVRLLdvchgPRTDR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  643 RRHLCMVMEYVEGgDCATLMKNMGP--LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV 720
Cdd:cd07838     78 ELKLTLVFEHVDQ-DLATYLDKCPKpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  721 --GLMSMTTnlyeghiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEfLVGCVPFFGDTPE------ 792
Cdd:cd07838    157 ysFEMALTS------------------VVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAE-LFNRRPLFRGSSEadqlgk 217
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  793 --ELFGQVISDEinWPEKDEAPP-------------------PDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07838    218 ifDVIGLPSEEE--WPRNSALPRssfpsytprpfksfvpeidEEGLDLLKKMLTFNPHKRI---SAFEALQHPYF 287
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
572-831 6.25e-37

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: 141.39  E-value: 6.25e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd08529      1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMR-EEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMK-NMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNl 729
Cdd:cd08529     80 YAENGDLHSLIKsQRGrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKI--LSDTTN- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 yeghiekdarefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIsdeinwpeKD 809
Cdd:cd08529    157 ------------FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIV--------RG 216
                          250       260
                   ....*....|....*....|....*...
gi 1988312908  810 EAPP------PDAQDLITLLLRQNPLER 831
Cdd:cd08529    217 KYPPisasysQDLSQLIDSCLTKDYRQR 244
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
579-832 7.44e-37

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: 141.29  E-value: 7.44e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKE--SRQRFAMKKINKqnlILRNQIQQAFVER-----DILTFAENPFVVSMYCSFETR-RHLCMVM 650
Cdd:cd13994      1 IGKGATSVVRIVTKKNprSGVLYAVKEYRR---RDDESKRKDYVKRltseyIISSKLHHPNIVKVLDLCQDLhGKWCLVM 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttnlY 730
Cdd:cd13994     78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEV---------F 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHIEKDARefLDKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQviSDEINWPEKD 809
Cdd:cd13994    149 GMPAEKESP--MSAGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYK--AYEKSGDFTN 224
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  810 EAPPP-------DAQDLITLLLRQNPLERL 832
Cdd:cd13994    225 GPYEPienllpsECRRLIYRMLHPDPEKRI 254
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
579-832 8.05e-37

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: 140.94  E-value: 8.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLilrNQIQQAFVERDILTFAE--NPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14075     10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTKL---DQKTQRLLSREISSMEKlhHPNIIRLYEVVETLSKLHLVMEYASGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYeghiek 736
Cdd:cd14075     87 ELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTF------ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 darefldkqvCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKdeaPPPD 815
Cdd:cd14075    161 ----------CGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSY---VSEP 227
                          250
                   ....*....|....*..
gi 1988312908  816 AQDLITLLLRQNPLERL 832
Cdd:cd14075    228 CQELIRGILQPVPSDRY 244
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
582-832 1.07e-36

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: 140.50  E-value: 1.07e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHK-ESRQRFAMKKINKQNLIlRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCAT 660
Cdd:cd14121      6 GTYATVYKAYRKsGAREVVAVKCVSKSSLN-KASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDLSR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  661 LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG--HIKLTDFGLSKvglmsmttnlyegHIEKDA 738
Cdd:cd14121     85 FIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQ-------------HLKPND 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  739 REFldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELfgqviSDEINWPEKDEAPP----- 813
Cdd:cd14121    152 EAH---SLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEEL-----EEKIRSSKPIEIPTrpels 223
                          250
                   ....*....|....*....
gi 1988312908  814 PDAQDLITLLLRQNPLERL 832
Cdd:cd14121    224 ADCRDLLLRLLQRDPDRRI 242
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
566-832 2.38e-36

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: 139.79  E-value: 2.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  566 RKPRESDFETI--KLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDILTF---AENPFVVSMYCSF 640
Cdd:cd14106      1 STENINEVYTVesTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRR---RGQDCRNEILHEIAVLelcKDCPRVVNLHEVY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 ETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS---MGHIKLTDFGL 717
Cdd:cd14106     78 ETRSELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSefpLGDIKLCDFGI 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SKVglmsmttnLYEGhieKDAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQ 797
Cdd:cd14106    158 SRV--------IGEG---EEIREIL-----GTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLN 221
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  798 VISDEINWPEKD-EAPPPDAQDLITLLLRQNPLERL 832
Cdd:cd14106    222 ISQCNLDFPEELfKDVSPLAIDFIKRLLVKDPEKRL 257
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
573-846 2.94e-36

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: 139.92  E-value: 2.94e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLI-------LRnqiqqafvERDILTFAENPFVVSMYCSFETRRH 645
Cdd:cd07829      1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegipstaLR--------EISLLKELKHPNIVKLLDVIHTENK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGgDCATLMKNM-GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglms 724
Cdd:cd07829     73 LYLVFEYCDQ-DLKKYLDKRpGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGL------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghiekdAREFLDKQVCGTPE-----YIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGDTpE------ 792
Cdd:cd07829    145 -------------ARAFGIPLRTYTHEvvtlwYRAPEILLGsKHYSTAVDIWSVGCIFAELITGKPLFPGDS-Eidqlfk 210
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  793 --ELFGQviSDEINWPE------KDEAPP---------------PDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07829    211 ifQILGT--PTEESWPGvtklpdYKPTFPkwpkndlekvlprldPEGIDLLSKMLQYNPAKRI---SAKEALKHPYF 282
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
570-846 7.54e-36

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: 138.17  E-value: 7.54e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd06612      2 EEVFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVP-----VEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvGLMSMTTn 728
Cdd:cd06612     77 MEYCGAGSVSDIMKITNkTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVS--GQLTDTM- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghiekdareFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEelfgQVISDEINWPek 808
Cdd:cd06612    154 ------------AKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPM----RAIFMIPNKP-- 215
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1988312908  809 deaPP---------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06612    216 ---PPtlsdpekwsPEFNDFVKKCLVKDPEER---PSAIQLLQHPFI 256
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
572-839 9.13e-36

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: 137.78  E-value: 9.13e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKkinkqnLILRNQIQQAFVER------DILTFAENPFVVSMYCSFETRRH 645
Cdd:cd14116      6 DFEIGRPLGKGKFGNVYLAREKQSKFILALK------VLFKAQLEKAGVEHqlrrevEIQSHLRHPNILRLYGYFHDATR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSM 725
Cdd:cd14116     80 VYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TTNLyeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW 805
Cdd:cd14116    160 RTTL-----------------CGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTF 222
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  806 PekdEAPPPDAQDLITLLLRQNPLERLGTGGAYE 839
Cdd:cd14116    223 P---DFVTEGARDLISRLLKHNPSQRPMLREVLE 253
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
579-850 1.13e-35

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: 138.71  E-value: 1.13e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNqIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDc 658
Cdd:cd14086      9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARD-HQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGE- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 atLMKNMgplpvdMARMYFAET--------VL-ALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSkvglmsmt 726
Cdd:cd14086     87 --LFEDI------VAREFYSEAdashciqqILeSVNHCHQNGIVHRDLKPENLLLASKSKgaaVKLADFGLA-------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlYEGHIEKDAREFLdkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP 806
Cdd:cd14086    151 ---IEVQGDQQAWFGF----AGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYP 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908  807 EKD-EAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSLD 850
Cdd:cd14086    224 SPEwDTVTPEAKDLINQMLTVNPAKRI---TAAEALKHPWICQRD 265
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
572-832 4.21e-35

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: 136.29  E-value: 4.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQ-RFAMKKINKQNLilrnQIQQAFVERDILTFAE--NPFVVSMYCSFETRRHLCM 648
Cdd:cd14202      3 EFSRKDLIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNL----AKSQTLLGKEIKILKElkHENIVALYDFQEIANSVYL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---------HIKLTDFGLSK 719
Cdd:cd14202     79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFAR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 VglmsMTTNLyeghiekdarefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL---FG 796
Cdd:cd14202    159 Y----LQNNM------------MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLrlfYE 222
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  797 QVISDEINWPEKDEAPppdAQDLITLLLRQNPLERL 832
Cdd:cd14202    223 KNKSLSPNIPRETSSH---LRQLLLGLLQRNQKDRM 255
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
571-855 4.39e-35

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: 136.61  E-value: 4.39e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKIN----KQNLILrnqIQQafvERDILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd06609      1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDleeaEDEIED---IQQ---EIQFLSQCDSPYITKYYGSFLKGSKL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKnMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvGLMSMT 726
Cdd:cd06609     75 WIIMEYCGGGSVLDLLK-PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVS--GQLTST 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 TnlyeghieKDAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE-LFgqVISDeiNW 805
Cdd:cd06609    152 M--------SKRNTFV-----GTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRvLF--LIPK--NN 214
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  806 PEKDEAPP--PDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSLDWNSLL 855
Cdd:cd06609    215 PPSLEGNKfsKPFKDFVELCLNKDPKERP---SAKELLKHKFIKKAKKTSYL 263
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
573-831 5.48e-35

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: 135.93  E-value: 5.48e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilrnQIQQAFVERDI--LTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14167      5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKAL----EGKETSIENEIavLHKIKHPNIVALDDIYESGGHLYLIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM---GHIKLTDFGLSKV-GLMSMT 726
Cdd:cd14167     81 QLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLdedSKIMISDFGLSKIeGSGSVM 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 TNlyeghiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW- 805
Cdd:cd14167    161 ST-----------------ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFd 223
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  806 -PEKDEApPPDAQDLITLLLRQNPLER 831
Cdd:cd14167    224 sPYWDDI-SDSAKDFIQHLMEKDPEKR 249
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
582-846 7.04e-35

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: 135.08  E-value: 7.04e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNL-ILRNQIQQAFVERDILTFAENPFVVSMYCSF--ETRRHLCMVMEYVEGGdc 658
Cdd:cd14119      4 GSYGKVKEVLDTETLCRRAVKILKKRKLrRIPNGEANVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEYCVGG-- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGP---LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnlyeghie 735
Cdd:cd14119     82 LQEMLDSAPdkrLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVA----------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  736 kdarEFLDK----QVC----GTPEYIAPEVILRQGY--GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW 805
Cdd:cd14119    145 ----EALDLfaedDTCttsqGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTI 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1988312908  806 PEKdeaPPPDAQDLITLLLRQNPLERLGTggaYEVKQHRFF 846
Cdd:cd14119    221 PDD---VDPDLQDLLRGMLEKDPEKRFTI---EQIRQHPWF 255
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
582-832 7.20e-35

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: 136.17  E-value: 7.20e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLilrnQIQQAFVERDI--LTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCA 659
Cdd:cd14169     14 GAFSEVVLAQERGSQRLVALKCIPKKAL----RGKEAMVENEIavLRRINHENIVSLEDIYESPTHLYLAMELVTGGELF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  660 TLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM---GHIKLTDFGLSKV---GLMSMTtnlyegh 733
Cdd:cd14169     90 DRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfedSKIMISDFGLSKIeaqGMLSTA------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIN-----WPEK 808
Cdd:cd14169    163 -------------CGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEfdspyWDDI 229
                          250       260
                   ....*....|....*....|....
gi 1988312908  809 DEApppdAQDLITLLLRQNPLERL 832
Cdd:cd14169    230 SES----AKDFIRHLLERDPEKRF 249
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
572-832 7.85e-35

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: 135.52  E-value: 7.85e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIK--LISNGAYGAVYFVRH-KESRQRFAMKKINKQNLIlRNQIQQAfVERDILTFAENPFVVSMYCSFETRRHLCM 648
Cdd:cd14201      5 DFEYSRkdLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLS-KSQILLG-KEIKILKELQHENIVALYDVQEMPNSVFL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---------HIKLTDFGLSK 719
Cdd:cd14201     83 VMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFAR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 VglmsMTTNLyeghiekdarefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd14201    163 Y----LQSNM------------MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYE 226
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1988312908  800 SDEINWPEKDEAPPPDAQDLITLLLRQNPLERL 832
Cdd:cd14201    227 KNKNLQPSIPRETSPYLADLLLGLLQRNQKDRM 259
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
573-831 1.16e-34

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: 134.57  E-value: 1.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNqIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14072      2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSS-LQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttNLYEG 732
Cdd:cd14072     81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFS---------NEFTP 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HIEKDArefldkqVCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:cd14072    152 GNKLDT-------FCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMST 224
                          250       260
                   ....*....|....*....|
gi 1988312908  812 pppDAQDLITLLLRQNPLER 831
Cdd:cd14072    225 ---DCENLLKKFLVLNPSKR 241
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
571-858 1.60e-34

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: 137.12  E-value: 1.60e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAEN---PFVVSMYCSFETRRHLC 647
Cdd:cd05633      5 NDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMTYAFHTPDKLC 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglmsmtt 727
Cdd:cd05633     85 FILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGL---------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyeghiekdAREFLDKQ---VCGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGDTPE---ELFGQVIS 800
Cdd:cd05633    155 ----------ACDFSKKKphaSVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLT 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  801 DEINWPEKDEappPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQK 858
Cdd:cd05633    225 VNVELPDSFS---PELKSLLEGLLQRDVSKRLGChgRGAQEVKEHSFFKGIDWQQVYLQK 281
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
577-831 2.85e-34

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: 133.68  E-value: 2.85e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKIN--KQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd06632      6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyegHI 734
Cdd:cd06632     86 GGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAK-------------HV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 EKDArefLDKQVCGTPEYIAPEVILRQ--GYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFGQVISDEInwPEKDEA 811
Cdd:cd06632    153 EAFS---FAKSFKGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGvAAIFKIGNSGEL--PPIPDH 227
                          250       260
                   ....*....|....*....|
gi 1988312908  812 PPPDAQDLITLLLRQNPLER 831
Cdd:cd06632    228 LSPDAKDFIRLCLQRDPEDR 247
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
572-831 2.89e-34

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: 133.82  E-value: 2.89e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKIN--------KQNLIlrnqiqqafVERDILTFAENPFVVSMYCSF--E 641
Cdd:cd08217      1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDygkmsekeKQQLV---------SEVNILRELKHPNIVRYYDRIvdR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 TRRHLCMVMEYVEGGDCATLMKNM----GPLPVDMARMYFAETVLALEYLHN-----YGIVHRDLKPDNLLVTSMGHIKL 712
Cdd:cd08217     72 ANTTLYIVMEYCEGGDLAQLIKKCkkenQYIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANIFLDSDNNVKL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  713 TDFGLSKVglMSMTTNLyeghiekdAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPE 792
Cdd:cd08217    152 GDFGLARV--LSHDSSF--------AKTYV-----GTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQL 216
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  793 ELFGQVISDEIN-WPEKDEappPDAQDLITLLLRQNPLER 831
Cdd:cd08217    217 ELAKKIKEGKFPrIPSRYS---SELNEVIKSMLNVDPDKR 253
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
573-832 3.31e-34

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: 133.58  E-value: 3.31e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDI--LTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14162      2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKA--PEDYLQKFLPREIevIKGLKHPNLICFYEAIETTSRVYIIM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglMSMTTnly 730
Cdd:cd14162     80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR---GVMKT--- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghieKDAREFLDKQVCGTPEYIAPEvILRqgyGKP-----VDWWAMGIILYEFLVGCVPFFGDTPEELFGQViSDEINW 805
Cdd:cd14162    154 -----KDGKPKLSETYCGSYAYASPE-ILR---GIPydpflSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV-QRRVVF 223
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  806 PEKDEApPPDAQDLITLLLRQNPlERL 832
Cdd:cd14162    224 PKNPTV-SEECKDLILRMLSPVK-KRI 248
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
582-832 4.20e-34

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: 132.73  E-value: 4.20e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG----- 656
Cdd:cd14103      4 GKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRN---EIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGelfer 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 -----------DCATLMKnmgplpvdmarmyfaETVLALEYLHNYGIVHRDLKPDNLL-VTSMGH-IKLTDFGLskvglm 723
Cdd:cd14103     81 vvdddfelterDCILFMR---------------QICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGL------ 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttnlyeghiekdAREFLDKQV----CGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd14103    140 --------------ARKYDPDKKlkvlFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVT 205
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  800 SdeINWPEKDEA---PPPDAQDLITLLLRQNPLERL 832
Cdd:cd14103    206 R--AKWDFDDEAfddISDEAKDFISKLLVKDPRKRM 239
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
570-831 6.15e-34

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: 133.19  E-value: 6.15e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRN-QIQQAFVERDILTFA--ENPFVVSMYCSFETRRHL 646
Cdd:cd13996      5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIR-----LTEkSSASEKVLREVKALAklNHPNIVRYYTAWVEEPPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGG------DCATLMKNMGplpVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIKLTDFGLSK 719
Cdd:cd13996     80 YIQMELCEGGtlrdwiDRRNSSSKND---RKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLAT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 V--GLMSMTTNLYEGHIEKDAREfldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCvpffgDTPEELFgQ 797
Cdd:cd13996    157 SigNQKRELNNLNNNNNGNTSNN---SVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLHPF-----KTAMERS-T 227
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  798 VISD--EINWPEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd13996    228 ILTDlrNGILPESFKAKHPKEADLIQSLLSKNPEER 263
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
579-843 6.72e-34

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: 133.55  E-value: 6.72e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLIL-----------------------RNQIQQAFVERDILTFAENPFVVS 635
Cdd:cd14199     10 IGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRqagfprrppprgaraapegctqpRGPIERVYQEIAILKKLDHPNVVK 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  636 MYCSFE--TRRHLCMVMEYVEGGDCATLmKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLT 713
Cdd:cd14199     90 LVEVLDdpSEDHLYMVFELVKQGPVMEV-PTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  714 DFGLSkvglmsmttNLYEGhieKDAreFLDKQVcGTPEYIAPEVI--LRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDT 790
Cdd:cd14199    169 DFGVS---------NEFEG---SDA--LLTNTV-GTPAFMAPETLseTRKIFsGKALDVWAMGVTLYCFVFGQCPFMDER 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  791 PEELFGQVISDEINWPEKDEApPPDAQDLITLLLRQNPLERLGTGgayEVKQH 843
Cdd:cd14199    234 ILSLHSKIKTQPLEFPDQPDI-SDDLKDLLFRMLDKNPESRISVP---EIKLH 282
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
579-832 7.93e-34

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: 132.12  E-value: 7.93e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNL---ILRNQIqqafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd14078     11 IGSGGFAKVKLATHILTGEKVAIKIMDKKALgddLPRVKT-----EIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGL-SKvglmsmttnlyeghi 734
Cdd:cd14078     86 GELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAK--------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 EKDAREFLDKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEInwpEKDEAPP 813
Cdd:cd14078    151 PKGGMDHHLETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKY---EEPEWLS 227
                          250
                   ....*....|....*....
gi 1988312908  814 PDAQDLITLLLRQNPLERL 832
Cdd:cd14078    228 PSSKLLLDQMLQVDPKKRI 246
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
574-846 8.93e-34

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 132.29  E-value: 8.93e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  574 ETIKLIsNGAYGAVYFVRHKESRQRFAMKKINKQNLilrNQIQqaFVERDILtfAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:PHA03390    20 KKLKLI-DGKFGKVSVLKHKPTQKLFVQKIIKAKNF---NAIE--PMVHQLM--KDNPNFIKLYYSVTTLKGHVLIMDYI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIKLTDFGLSK-VGlmsmTTNLYE 731
Cdd:PHA03390    92 KDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCKiIG----TPSCYD 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekdarefldkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD-----TPEELFgQVISDEINWP 806
Cdd:PHA03390   168 ----------------GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDedeelDLESLL-KRQQKKLPFI 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  807 EKDeapPPDAQDLITLLLRQNPLERLGTGgaYEVKQHRFF 846
Cdd:PHA03390   231 KNV---SKNANDFVQSMLKYNINYRLTNY--NEIIKHPFL 265
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
568-847 9.58e-34

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: 132.18  E-value: 9.58e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PReSDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQA--FVERDILTFAENPFVVSMYCSFETRRH 645
Cdd:cd06648      5 PR-SDLDNFVKIGEGSTGIVCIATDKSTGRQVAVKKMD-----LRKQQRREllFNEVVIMRDYQHPNIVEMYSSYLVGDE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMgplpvdmaRM------YFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS 718
Cdd:cd06648     79 LWVVMEFLEGGALTDIVTHT--------RMneeqiaTVCRAVLkALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFC 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 kvglmsmttnlyeGHIEKDAREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV 798
Cdd:cd06648    151 -------------AQVSKEVPR--RKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRI 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  799 isdeinwpeKDEAPP---------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFFR 847
Cdd:cd06648    216 ---------RDNEPPklknlhkvsPRLRSFLDRMLVRDPAQR---ATAAELLNHPFLA 261
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
576-831 1.42e-33

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: 131.47  E-value: 1.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd08218      5 IKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKER-EESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GD-CATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLyegh 733
Cdd:cd08218     84 GDlYKRINAQRGvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARV--LNSTVEL---- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDeiNWPEKDEAPP 813
Cdd:cd08218    158 ----ARTCI-----GTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRG--SYPPVPSRYS 226
                          250
                   ....*....|....*...
gi 1988312908  814 PDAQDLITLLLRQNPLER 831
Cdd:cd08218    227 YDLRSLVSQLFKRNPRDR 244
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
570-837 2.20e-33

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: 132.26  E-value: 2.20e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLILRNQIqqafverDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd14085      2 EDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKtvDKKIVRTEI-------GVLLRLSHPNIIKLKEIFETPTEIS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSKVglms 724
Cdd:cd14085     75 LVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKI---- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghIEKDArefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD-TPEELFGQVISDEI 803
Cdd:cd14085    151 ---------VDQQV---TMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDErGDQYMFKRILNCDY 218
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  804 NW--PEKDEApPPDAQDLITLLLRQNPLERLGTGGA 837
Cdd:cd14085    219 DFvsPWWDDV-SLNAKDLVKKLIVLDPKKRLTTQQA 253
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
573-846 2.39e-33

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: 131.89  E-value: 2.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQ--------NLilrNQIQQafverdILTFAENPFVVSMYCSFETRR 644
Cdd:cd07830      1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKKfysweecmNL---REVKS------LRKLNEHPNIVKLKEVFREND 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGgDCATLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvgl 722
Cdd:cd07830     72 ELYFVFEYMEG-NLYQLMKdrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGL----- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttnlyeghiekdAREFLDKQV----CGTPEYIAPEVILRQG-YGKPVDWWAMGIILYEfLVGCVPFFGDTPE----- 792
Cdd:cd07830    146 ---------------AREIRSRPPytdyVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAE-LYTLRPLFPGSSEidqly 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  793 ---ELFGQVISDEinWPEKDE----------------------APPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07830    210 kicSVLGTPTKQD--WPEGYKlasklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRP---TASQALQHPYF 283
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
572-848 2.48e-33

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: 131.99  E-value: 2.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafverdILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14091      1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEI------LLRYGQHPNIITLRDVYDDGNSVYLVTE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDcatLMKNMgplpvdMARMYFAE--------TVL-ALEYLHNYGIVHRDLKPDNLLVTSMGH----IKLTDFGLS 718
Cdd:cd14091     75 LLRGGE---LLDRI------LRQKFFSEreasavmkTLTkTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFA 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 KV-----GLMsMTTnlyeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFF---GDT 790
Cdd:cd14091    146 KQlraenGLL-MTP-------------------CYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsgpNDT 205
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  791 PEELFGQVISDEI-----NWpekdEAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRS 848
Cdd:cd14091    206 PEVILARIGSGKIdlsggNW----DHVSDSAKDLVRKMLHVDPSQRP---TAAQVLQHPWIRN 261
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
572-858 3.39e-33

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: 132.48  E-value: 3.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAEN---PFVVSMYCSFETRRHLCM 648
Cdd:cd14223      1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLVSTgdcPFIVCMSYAFHTPDKLSF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglmsmttn 728
Cdd:cd14223     81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGL----------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghiekdAREFLDKQ---VCGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVGCVPFFGDTPE---ELFGQVISD 801
Cdd:cd14223    150 ---------ACDFSKKKphaSVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKdkhEIDRMTLTM 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  802 EINWPekdEAPPPDAQDLITLLLRQNPLERLGT--GGAYEVKQHRFFRSLDWNSLLRQK 858
Cdd:cd14223    221 AVELP---DSFSPELRSLLEGLLQRDVNRRLGCmgRGAQEVKEEPFFRGLDWQMVFLQK 276
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
573-842 4.42e-33

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: 131.40  E-value: 4.42e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRF-AMKKINKQNL----ILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd14096      3 YRLINKIGEGAFSNVYKAVPLRNTGKPvAIKVVRKADLssdnLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS--------------------- 706
Cdd:cd14096     83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkadddetkvd 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  707 ------------MGHIKLTDFGLSKVgLMSMTTnlyeghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGI 774
Cdd:cd14096    163 egefipgvggggIGIVKLADFGLSKQ-VWDSNT----------------KTPCGTVGYTAPEVVKDERYSKKVDMWALGC 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  775 ILYEFLVGCVPFFGDTPEELFGQVISDEINW--PEKDEApPPDAQDLITLLLRQNPLERlgtggaYEVKQ 842
Cdd:cd14096    226 VLYTLLCGFPPFYDESIETLTEKISRGDYTFlsPWWDEI-SKSAKDLISHLLTVDPAKR------YDIDE 288
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
569-831 5.53e-33

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: 130.64  E-value: 5.53e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKIN-KQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRR-HL 646
Cdd:cd06620      3 KNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHiDAKSSVRKQILR---ELQILHECHSPYIVSFYGAFLNENnNI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHN-YGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSM 725
Cdd:cd06620     80 IICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeghiekdAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPfFGDTPEELFGQVISDEI-- 803
Cdd:cd06620    160 ------------ADTFV-----GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFP-FAGSNDDDDGYNGPMGIld 221
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1988312908  804 ------NWPE----KDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd06620    222 llqrivNEPPprlpKDRIFPKDLRDFVDRCLLKDPRER 259
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
572-833 8.35e-33

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: 129.49  E-value: 8.35e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQ-NLILRNQIQ---QAFVERDILTFAE--------NPFVVSMYCS 639
Cdd:cd14077      2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRAsNAGLKKEREkrlEKEISRDIRTIREaalssllnHPHICRLRDF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 FETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSk 719
Cdd:cd14077     82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLS- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 vglmsmttNLYeghiekDAREFLdKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV 798
Cdd:cd14077    161 --------NLY------DPRRLL-RTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKI 225
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1988312908  799 ISDEINWPEKDEApppDAQDLITLLLRQNPLERLG 833
Cdd:cd14077    226 KKGKVEYPSYLSS---ECKSLISRMLVVDPKKRAT 257
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
582-832 1.26e-32

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: 129.21  E-value: 1.26e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVER--DILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCA 659
Cdd:cd14097     12 GSFGVVIEATHKETQTKWAIKKINREK---AGSSAVKLLERevDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELK 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  660 TLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG-------HIKLTDFGLSKVglmsmTTNLYEG 732
Cdd:cd14097     89 ELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSVQ-----KYGLGED 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HIEkdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIN-----WPE 807
Cdd:cd14097    164 MLQ---------ETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTftqsvWQS 234
                          250       260
                   ....*....|....*....|....*
gi 1988312908  808 KDEApppdAQDLITLLLRQNPLERL 832
Cdd:cd14097    235 VSDA----AKNVLQQLLKVDPAHRM 255
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
571-846 1.72e-32

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: 128.63  E-value: 1.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQnlilRNQIQQAFVERDILTFAEN--PFVVSMYCSFETRRHLCM 648
Cdd:cd06610      1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLE----KCQTSMDELRKEIQAMSQCnhPNVVSYYTSFVVGDELWL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMK---NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsm 725
Cdd:cd06610     77 VMPLLSGGSLLDIMKssyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVS------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 tTNLYE-GHIEKDARefldKQVCGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIsdei 803
Cdd:cd06610    150 -ASLATgGDRTRKVR----KTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTL---- 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  804 nwpekdEAPPPDAQ-------------DLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06610    221 ------QNDPPSLEtgadykkysksfrKMISLCLQKDPSKR---PTAEELLKHKFF 267
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
572-846 4.11e-32

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: 127.42  E-value: 4.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd06613      1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGDDFEIIQQ---EISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvGLMSMTtnlye 731
Cdd:cd06613     78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVS--AQLTAT----- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghIEKdaRefldKQVCGTPEYIAPEVIL---RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFgqVIsdeinwPE 807
Cdd:cd06613    151 --IAK--R----KSFIGTPYWMAPEVAAverKGGYDGKCDIWALGITAIELAELQPPMFDLHPmRALF--LI------PK 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1988312908  808 KDEAPP---------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06613    215 SNFDPPklkdkekwsPDFHDFIKKCLTKNPKKR---PTATKLLQHPFV 259
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
572-839 4.37e-32

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: 127.67  E-value: 4.37e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14117      7 DFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnlye 731
Cdd:cd14117     87 YAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWS------------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghieKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdEA 811
Cdd:cd14117    154 ----VHAPSLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFP---PF 226
                          250       260
                   ....*....|....*....|....*...
gi 1988312908  812 PPPDAQDLITLLLRQNPLERLGTGGAYE 839
Cdd:cd14117    227 LSDGSRDLISKLLRYHPSERLPLKGVME 254
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
592-846 4.59e-32

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: 127.86  E-value: 4.59e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  592 HKESRQRFAMKKI----NKQNLILRNQIQQAFV-ERDIL-TFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNM 665
Cdd:cd14093     24 EKETGQEFAVKIIditgEKSSENEAEELREATRrEIEILrQVSGHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  666 GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGlskvglmsMTTNLYEGhiekdarEFLdKQ 745
Cdd:cd14093    104 VTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFG--------FATRLDEG-------EKL-RE 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  746 VCGTPEYIAPEVILRQ------GYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW--PEKDEApPPDAQ 817
Cdd:cd14093    168 LCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFgsPEWDDI-SDTAK 246
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  818 DLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14093    247 DLISKLLVVDPKKRL---TAEEALEHPFF 272
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
577-845 4.77e-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: 4.77e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLiLRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd06626      6 NKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDN-DPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVgLMSMTTNLYEGHIEK 736
Cdd:cd06626     85 TLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVK-LKNNTTTMAPGEVNS 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DArefldkqvcGTPEYIAPEVILRQ---GYGKPVDWWAMGIILYEFLVGCVPffgdtpeelfgqvisdeinWPEKD---- 809
Cdd:cd06626    164 LV---------GTPAYMAPEVITGNkgeGHGRAADIWSLGCVVLEMATGKRP-------------------WSELDnewa 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  810 --------EAPP--------PDAQDLITLLLRQNPLERLgtgGAYEVKQHRF 845
Cdd:cd06626    216 imyhvgmgHKPPipdslqlsPEGKDFLSRCLESDPKKRP---TASELLDHPF 264
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
577-825 6.15e-32

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: 126.76  E-value: 6.15e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKqnliLR---NQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14082      9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDK----LRfptKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGdcatlMKNM------GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---HIKLTDFGLSKVglms 724
Cdd:cd14082     85 HGD-----MLEMilssekGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI---- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghI-EKDARefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDtpEELFGQVISDEI 803
Cdd:cd14082    156 ---------IgEKSFR----RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNED--EDINDQIQNAAF 220
                          250       260
                   ....*....|....*....|...
gi 1988312908  804 NWPEKDEAP-PPDAQDLITLLLR 825
Cdd:cd14082    221 MYPPNPWKEiSPDAIDLINNLLQ 243
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
570-832 1.03e-31

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: 126.45  E-value: 1.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL------ILRNQIQQafvERDILTFAENPFVVSMYCSFETR 643
Cdd:cd14105      4 EDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSkasrrgVSREDIER---EVSILRQVLHPNIITLHDVFENK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG----HIKLTDFGLSk 719
Cdd:cd14105     81 TDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLA- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 vglmsmttnlyegHIEKDAREFldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd14105    160 -------------HKIEDGNEF--KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANIT 224
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  800 SdeINWPEKDE---APPPDAQDLITLLLRQNPLERL 832
Cdd:cd14105    225 A--VNYDFDDEyfsNTSELAKDFIRQLLVKDPRKRM 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
573-845 2.11e-31

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: 125.48  E-value: 2.11e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNqiqqafVERDILTFA--ENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14665      2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDEN------VQREIINHRslRHPNIVRFKEVILTPTHLAIVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV--TSMGHIKLTDFGLSKVGLMsmttn 728
Cdd:cd14665     76 EYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVL----- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyegHIEKdarefldKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFfgDTPEE------LFGQVISD 801
Cdd:cd14665    151 ----HSQP-------KSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVMLVGAYPF--EDPEEprnfrkTIQRILSV 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1988312908  802 EINWPEkDEAPPPDAQDLITLLLRQNPLERLGTGgayEVKQHRF 845
Cdd:cd14665    218 QYSIPD-YVHISPECRHLISRIFVADPATRITIP---EIRNHEW 257
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
577-831 2.58e-31

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: 125.14  E-value: 2.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAfvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14184      7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIEN--EVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DC-ATLMKNMGPLPVDMARMYFaETVLALEYLHNYGIVHRDLKPDNLLVTSMGH----IKLTDFGLSKVglmsMTTNLYe 731
Cdd:cd14184     85 DLfDAITSSTKYTERDASAMVY-NLASALKYLHGLCIVHRDIKPENLLVCEYPDgtksLKLGDFGLATV----VEGPLY- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDT--PEELFGQVISDEINWPekd 809
Cdd:cd14184    159 -------------TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFP--- 222
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  810 eAPPPD-----AQDLITLLLRQNPLER 831
Cdd:cd14184    223 -SPYWDnitdsAKELISHMLQVNVEAR 248
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
572-843 5.03e-31

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: 124.06  E-value: 5.03e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFEtiKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL--ILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14074      6 DLE--ETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLddVSKAHLFQ---EVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDC-ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV-TSMGHIKLTDFGLSkvglmsmtt 727
Cdd:cd14074     81 LELGDGGDMyDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFS--------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NLYEghiekdAREFLDKQvCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP 806
Cdd:cd14074    152 NKFQ------PGEKLETS-CGSLAYSAPEILLGDEYDAPaVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVP 224
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  807 EKdeaPPPDAQDLITLLLRQNPLERLGTGgayEVKQH 843
Cdd:cd14074    225 AH---VSPECKDLIRRMLIRDPKKRASLE---EIENH 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
577-846 5.35e-31

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: 124.00  E-value: 5.35e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKIN--KQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd06625      6 KLLGQGAFGQVYLCYDADTGRELAVKQVEidPINTEASKEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK-VGLMSMTTNLyegh 733
Cdd:cd06625     86 GGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrLQTICSSTGM---- 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFGQVISdeinwPEKDEAP 812
Cdd:cd06625    162 ----------KSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPmAAIFKIATQ-----PTNPQLP 226
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  813 P---PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06625    227 PhvsEDARDFLSLIFVRNKKQR---PSAEELLSHSFV 260
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
573-849 6.13e-31

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: 124.99  E-value: 6.13e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL-ILRNQIQQ-AFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd07841      2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkEAKDGINFtALREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGgDCATLMKNMGPL--PVDMaRMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV-Glmsmtt 727
Cdd:cd07841     82 EFMET-DLEKVIKDKSIVltPADI-KSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSfG------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyeghiekDAREFLDKQVCgTPEYIAPEVIL--RQgYGKPVDWWAMGIILYEFLVGcVPFF-GDTPEELFGQVIS---- 800
Cdd:cd07841    154 ---------SPNRKMTHQVV-TRWYRAPELLFgaRH-YGVGVDMWSVGCIFAELLLR-VPFLpGDSDIDQLGKIFEalgt 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  801 -DEINWP---------EKDEAPPP-----------DAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSL 849
Cdd:cd07841    222 pTEENWPgvtslpdyvEFKPFPPTplkqifpaasdDALDLLQRLLTLNPNKRI---TARQALEHPYFSND 288
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
579-831 6.42e-31

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: 124.10  E-value: 6.42e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMK--KINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd13978      1 LGSGGFGTVSKARHVSWFGMVAIKclHSSPNCIEERKALLK---EAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMK-NMGPLPVDMARMYFAETVLALEYLHNY--GIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLyEGH 733
Cdd:cd13978     78 SLKSLLErEIQDVPWSLRFRIIHEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANR-RRG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEKDArefldkqvcGTPEYIAPEViLRQGYGKPV---DWWAMGIILYEFLVGCVPFFG--DTPEELFGQVISDEINWPEK 808
Cdd:cd13978    157 TENLG---------GTPIYMAPEA-FDDFNKKPTsksDVYSFAIVIWAVLTRKEPFENaiNPLLIMQIVSKGDRPSLDDI 226
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  809 DEA-PPPDAQDLITLLLR---QNPLER 831
Cdd:cd13978    227 GRLkQIENVQELISLMIRcwdGNPDAR 253
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
573-843 8.50e-31

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: 123.34  E-value: 8.50e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNqiqqafVERDILTFAE--NPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14662      2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDEN------VQREIINHRSlrHPNIIRFKEVVLTPTHLAIVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV--TSMGHIKLTDFGLSKVGLMsmttn 728
Cdd:cd14662     76 EYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSKSSVL----- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyegHIEKdarefldKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFfgDTPEE------LFGQVISD 801
Cdd:cd14662    151 ----HSQP-------KSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVMLVGAYPF--EDPDDpknfrkTIQRIMSV 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  802 EINWPEKDEApPPDAQDLITLLLRQNPLERLGTGgayEVKQH 843
Cdd:cd14662    218 QYKIPDYVRV-SQDCRHLLSRIFVANPAKRITIP---EIKNH 255
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
572-843 1.16e-30

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: 123.15  E-value: 1.16e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd08224      1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMG----PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVgLMSMTT 727
Cdd:cd08224     81 LADAGDLSRLIKHFKkqkrLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRF-FSSKTT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyEGHiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTpEELF--GQVIsdeinw 805
Cdd:cd08224    160 ---AAH-----------SLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEK-MNLYslCKKI------ 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908  806 pEKDEAPP-PDAQ------DLITLLLRQNPLERLGTGGAYEVKQH 843
Cdd:cd08224    219 -EKCEYPPlPADLysqelrDLVAACIQPDPEKRPDISYVLDVAKR 262
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
573-865 1.70e-30

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: 123.81  E-value: 1.70e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERD--ILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14094      5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTEDLKREasICHMLKHPHIVELLETYSSDGMLYMVF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGD-CATLMKNMGPLPV---DMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSKvglm 723
Cdd:cd14094     85 EFMDGADlCFEIVKRADAGFVyseAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAI---- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttNLYEGHIEKDARefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGdTPEELFGQVISDEI 803
Cdd:cd14094    161 ----QLGESGLVAGGR-------VGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG-TKERLFEGIIKGKY 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  804 N-----WPEKDEApppdAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSLDWNSLLRQKAEFIPQL 865
Cdd:cd14094    229 KmnprqWSHISES----AKDLVRRMLMLDPAERI---TVYEALNHPWIKERDRYAYRIHLPETVEQL 288
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
573-849 2.22e-30

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: 124.56  E-value: 2.22e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNL-----ILRnqiqqafvERDILTFAENPFVVSMY-----CSF 640
Cdd:cd07834      2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfDDLidakrILR--------EIKILRHLKHENIIGLLdilrpPSP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 ETRRHLCMVMEYVEGgDCATLMKNMGPLPVDMARmYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK 719
Cdd:cd07834     74 EEFNDVYIVTELMET-DLHKVIKSPQPLTDDHIQ-YFLYQILrGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLAR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 VGlmsmttnlyeghIEKDAREFLDKQVCgTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCvPFF----------- 787
Cdd:cd07834    152 GV------------DPDEDKGFLTEYVV-TRWYRAPELLLSsKKYTKAIDIWSVGCIFAELLTRK-PLFpgrdyidqlnl 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  788 -----GDTPEELFGQVISDE-------------INWPEKDEAPPPDAQDLITLLLRQNPLERLgTggAYEVKQHRFFRSL 849
Cdd:cd07834    218 ivevlGTPSEEDLKFISSEKarnylkslpkkpkKPLSEVFPGASPEAIDLLEKMLVFNPKKRI-T--ADEALAHPYLAQL 294
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
579-846 2.32e-30

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: 122.58  E-value: 2.32e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNlilrnqIQQAFVER------DILTFAENPFVVSMYCSFETRR-HLCMVME 651
Cdd:cd14165      9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKK------APDDFVEKflprelEILARLNHKSIIKTYEIFETSDgKVYIVME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlye 731
Cdd:cd14165     83 LGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSK------------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 gHIEKDA--REFLDKQVCGTPEYIAPEVILRQGYGKPV-DWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPeK 808
Cdd:cd14165    151 -RCLRDEngRIVLSKTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFP-R 228
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1988312908  809 DEAPPPDAQDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14165    229 SKNLTSECKDLIYRLLQPDVSQRLCID---EVLSHPWL 263
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
579-846 3.05e-30

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: 123.17  E-value: 3.05e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQA--FVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd06659     29 IGEGSTGVVCIAREKHSGRQVAVKMMD-----LRKQQRREllFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGG 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNmgplpVDMARMYFA---ETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnlyeG 732
Cdd:cd06659    104 ALTDIVSQ-----TRLNEEQIAtvcEAVLqALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFC-------------A 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HIEKDAREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVisdeinwpeKDEAP 812
Cdd:cd06659    166 QISKDVPK--RKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRL---------RDSPP 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1988312908  813 P---------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06659    235 PklknshkasPVLRDFLERMLVRDPQER---ATAQELLDHPFL 274
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
571-848 4.59e-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: 122.20  E-value: 4.59e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilrNQIQQAFVERDI-----LTFAENPFVVSMYCSFETRRH 645
Cdd:cd06917      1 SLYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDT----DDDDVSDIQKEVallsqLKLGQPKNIIKYYGSYLKGPS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKnMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvGLMSM 725
Cdd:cd06917     77 LWIIMDYCEGGSIRTLMR-AGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVA--ASLNQ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TTNLYEGHIekdarefldkqvcGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGdtpEELFGQVISDEIN 804
Cdd:cd06917    154 NSSKRSTFV-------------GTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSD---VDALRAVMLIPKS 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1988312908  805 WPEK--DEAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRS 848
Cdd:cd06917    218 KPPRleGNGYSPLLKEFVAACLDEEPKDRL---SADELLKSKWIKQ 260
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
572-845 6.38e-30

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: 121.55  E-value: 6.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRhKESRQRFAMKKINKQNLilRNQIQQAFV-ERDIL-TFAENPFVVSMYCS--FETRRHLC 647
Cdd:cd14131      2 PYEILKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGA--DEQTLQSYKnEIELLkKLKGSDRIIQLYDYevTDEDDYLY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGgDCATLMKNMGPLPVDMA--RMYFAETVLALEYLHNYGIVHRDLKPDN-LLVTsmGHIKLTDFGLSKVgLMS 724
Cdd:cd14131     79 MVMECGEI-DLATILKKKRPKPIDPNfiRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLVK--GRLKLIDFGIAKA-IQN 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTTNlyeghIEKDARefldkqvCGTPEYIAPEVILRQGY----------GKPVDWWAMGIILYEFLVGCVPF--FGDTPE 792
Cdd:cd14131    155 DTTS-----IVRDSQ-------VGTLNYMSPEAIKDTSAsgegkpkskiGRPSDVWSLGCILYQMVYGKTPFqhITNPIA 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  793 ELfgQVISD---EINWPEKdeaPPPDAQDLITLLLRQNPLERLGTGgayEVKQHRF 845
Cdd:cd14131    223 KL--QAIIDpnhEIEFPDI---PNPDLIDVMKRCLQRDPKKRPSIP---ELLNHPF 270
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
578-846 7.93e-30

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: 121.62  E-value: 7.93e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKESRQRFAMK--KINKQNLILRnQIQQ----AFVERDILTFAEN-PFVVSMYCSFETRRHLCMVM 650
Cdd:cd14181     17 VIGRGVSSVVRRCVHRHTGQEFAVKiiEVTAERLSPE-QLEEvrssTLKEIHILRQVSGhPSIITLIDSYESSTFIFLVF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnly 730
Cdd:cd14181     96 DLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFS------------ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eGHIEKDAREfldKQVCGTPEYIAPEVI------LRQGYGKPVDWWAMGIILYEFLVGCVPFFgDTPEELFGQVISD--- 801
Cdd:cd14181    164 -CHLEPGEKL---RELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFW-HRRQMLMLRMIMEgry 238
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908  802 EINWPEKDEApPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14181    239 QFSSPEWDDR-SSTVKDLISRLLVVDPEIRL---TAEQALQHPFF 279
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
573-831 9.50e-30

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: 120.92  E-value: 9.50e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILR----NQIQQAFVERDILTFA-ENPFVVSMYCSFETRRHLC 647
Cdd:cd13993      2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKdgndFQKLPQLREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVD--MARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIKLTDFGLSkvglms 724
Cdd:cd13993     82 IVLEYCPNGDLFEAITENRIYVGKteLIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGLA------ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mTTnlyeghiEKDAREFldkqVCGTPEYIAPEVI-----LRQGYG-KPVDWWAMGIILYEFLVGCVPFFGDTPEE----- 793
Cdd:cd13993    156 -TT-------EKISMDF----GVGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPWKIASESDpifyd 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1988312908  794 --LFGQVISDEInwpekdeapPPDAQDLITLL---LRQNPLER 831
Cdd:cd13993    224 yyLNSPNLFDVI---------LPMSDDFYNLLrqiFTVNPNNR 257
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
568-849 1.71e-29

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 120.69  E-value: 1.71e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQiqqafvERDILTFAENPFVVSMYCSFETR---- 643
Cdd:cd14137      1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKV-LQDKRYKNR------ELQIMRRLKHPNIVKLKYFFYSSgekk 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 --RHLCMVMEYVEGgdcaTL-------MKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM-GHIKLT 713
Cdd:cd14137     74 deVYLNLVMEYMPE----TLyrvirhySKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLC 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  714 DFGLSKVglmsMTTNlyeghiekdareflDKQVCgtpeYI------APEVILR-QGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14137    150 DFGSAKR----LVPG--------------EPNVS----YIcsryyrAPELIFGaTDYTTAIDIWSAGCVLAELLLGQPLF 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  787 FGDTPEELFGQVIS-------DEI---NwPEKDE-----------------APPPDAQDLITLLLRQNPLERLgtgGAYE 839
Cdd:cd14137    208 PGESSVDQLVEIIKvlgtptrEQIkamN-PNYTEfkfpqikphpwekvfpkRTPPDAIDLLSKILVYNPSKRL---TALE 283
                          330
                   ....*....|
gi 1988312908  840 VKQHRFFRSL 849
Cdd:cd14137    284 ALAHPFFDEL 293
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
570-843 1.76e-29

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: 120.17  E-value: 1.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnlILRNQIQQAFVERDILTFA--ENPFVVSMYCSFETRRHLC 647
Cdd:cd14046      5 LTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIK----LRSESKNNSRILREVMLLSrlNHQHVVRYYQAWIERANLY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVG-LMSMT 726
Cdd:cd14046     81 IQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNkLNVEL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 TNLYEGHIEKDAREFLDKQV--CGTPEYIAPEVILRQG--YGKPVDWWAMGIILYEFlvgCVPFfgDTPEELF---GQVI 799
Cdd:cd14046    161 ATQDINKSTSAALGSSGDLTgnVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEM---CYPF--STGMERVqilTALR 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908  800 SDEINWPEK-DEAPPPDAQDLITLLLRQNPLERlgtGGAYEVKQH 843
Cdd:cd14046    236 SVSIEFPPDfDDNKHSKQAKLIRWLLNHDPAKR---PSAQELLKS 277
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
572-831 1.85e-29

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: 119.69  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQnlILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd08219      1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLP--KSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNM-GPL-PVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFG----LSKVGLMSM 725
Cdd:cd08219     79 YCDGGDLMQKIKLQrGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlLTSPGAYAC 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TtnlyeghiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINw 805
Cdd:cd08219    159 T-------------------YVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYK- 218
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  806 pekdeaPPP-----DAQDLITLLLRQNPLER 831
Cdd:cd08219    219 ------PLPshysyELRSLIKQMFKRNPRSR 243
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
572-846 2.14e-29

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: 120.51  E-value: 2.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKInkQNLILRNQIQQAFVeRDILTFAE---NPFVVSMYCSFETRRHLCM 648
Cdd:cd07832      1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKV--ALRKLEGGIPNQAL-REIKALQAcqgHPYVVKLRDVFPHGTGFVL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVeGGDCATLMKNM-GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSmtt 727
Cdd:cd07832     78 VFEYM-LSSLSEVLRDEeRPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARL--FS--- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyeghiEKDAREFLDKqvCGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGcVPFF-GDTPEELFGQVIS----- 800
Cdd:cd07832    152 -------EEDPRLYSHQ--VATRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNG-SPLFpGENDIEQLAIVLRtlgtp 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  801 DEINWPEKDEAP----------------------PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07832    222 NEKTWPELTSLPdynkitfpeskgirleeifpdcSPEAIDLLKGLLVYNPKKRL---SAEEALRHPYF 286
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
572-831 2.37e-29

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: 119.46  E-value: 2.37e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETRR-HLCMVM 650
Cdd:cd08223      1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRER-KAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARM--YFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV--GLMSMT 726
Cdd:cd08223     80 GFCEGGDLYTRLKEQKGVLLEERQVveWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVleSSSDMA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 TNLyeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEInwP 806
Cdd:cd08223    160 TTL-----------------IGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKL--P 220
                          250       260
                   ....*....|....*....|....*
gi 1988312908  807 EKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd08223    221 PMPKQYSPELGELIKAMLHQDPEKR 245
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
579-843 3.01e-29

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: 120.05  E-value: 3.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILR-----------------------NQIQQAFVERDILTFAENPFVVS 635
Cdd:cd14200      8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplAPLERVYQEIAILKKLDHVNIVK 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  636 MYCSFE--TRRHLCMVMEYVEGGDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLT 713
Cdd:cd14200     88 LIEVLDdpAEDNLYMVFDLLRKGPVMEVPSDK-PFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  714 DFGLSkvglmsmttNLYEGHiekDArefLDKQVCGTPEYIAPEVIL--RQGY-GKPVDWWAMGIILYEFLVGCVPFFGDT 790
Cdd:cd14200    167 DFGVS---------NQFEGN---DA---LLSSTAGTPAFMAPETLSdsGQSFsGKALDVWAMGVTLYCFVYGKCPFIDEF 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  791 PEELFGQVISDEINWPEKDEApPPDAQDLITLLLRQNPLERLGTGgayEVKQH 843
Cdd:cd14200    232 ILALHNKIKNKPVEFPEEPEI-SEELKDLILKMLDKNPETRITVP---EIKVH 280
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
570-832 3.03e-29

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: 119.29  E-value: 3.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINK-QNLILRNQIQQAFVER--DILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd14196      4 EDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrQSRASRRGVSREEIERevSILRQVLHPNIITLHDVYENRTDV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV----TSMGHIKLTDFGLSkvgl 722
Cdd:cd14196     84 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLldknIPIPHIKLIDFGLA---- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttnlyegHIEKDAREFldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE 802
Cdd:cd14196    160 ----------HEIEDGVEF--KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVS 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  803 INWPEKDEAPPPD-AQDLITLLLRQNPLERL 832
Cdd:cd14196    228 YDFDEEFFSHTSElAKDFIRKLLVKETRKRL 258
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
573-847 4.83e-29

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: 118.86  E-value: 4.83e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMK--KINKQNLILRNQIQQ----AFVERDIL-TFAENPFVVSMYCSFETRRH 645
Cdd:cd14182      5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKiiDITGGGSFSPEEVQElreaTLKEIDILrKVSGHPNIIQLKDTYETNTF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsm 725
Cdd:cd14182     85 FFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFS------- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 tTNLYEGhiEKdareflDKQVCGTPEYIAPEVIL------RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd14182    158 -CQLDPG--EK------LREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIM 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988312908  800 SDEINW--PEKDEApPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFR 847
Cdd:cd14182    229 SGNYQFgsPEWDDR-SDTVKDLISRFLVVQPQKRY---TAEEALAHPFFQ 274
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
573-846 5.78e-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. 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: 118.96  E-value: 5.78e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMK--KINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd07833      3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKkfKESEDDEDVKKTALR---EVKVLRQLRHENIVNLKEAFRRKGRLYLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNLY 730
Cdd:cd07833     80 EYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFAR--------ALT 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGhiekdAREFLDKQVcGTPEYIAPEVILRQG-YGKPVDWWAMGIILYEFLVGcVPFF-GD----------------TPE 792
Cdd:cd07833    152 AR-----PASPLTDYV-ATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDG-EPLFpGDsdidqlyliqkclgplPPS 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  793 --ELFGQ------VISDEINWPEKDEAPPPD-----AQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07833    225 hqELFSSnprfagVAFPEPSQPESLERRYPGkvsspALDFLKACLRMDPKERL---TCDELLQHPYF 288
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
610-791 5.94e-29

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 124.91  E-value: 5.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  610 ILRNQIQ--QAFVERdiltF-------AE--NPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMArMYFA 678
Cdd:NF033483    39 VLRPDLArdPEFVAR----FrreaqsaASlsHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEA-VEIM 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  679 ETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK-VGLMSMT-TNlyeghiekdarefldkQVCGTPEYIAP 755
Cdd:NF033483   114 IQILsALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARaLSSTTMTqTN----------------SVLGTVHYLSP 177
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1988312908  756 EvilrQGYGKPV----DWWAMGIILYEFLVGCVPFFGDTP 791
Cdd:NF033483   178 E----QARGGTVdarsDIYSLGIVLYEMLTGRPPFDGDSP 213
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
575-835 7.58e-29

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: 118.10  E-value: 7.58e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  575 TIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd14190      8 SKEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQN---SKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDC-ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDN-LLVTSMGH-IKLTDFGLSKvglmsmttnlye 731
Cdd:cd14190     85 GGELfERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENiLCVNRTGHqVKIIDFGLAR------------ 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiEKDAREFLdKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDeiNW---PEK 808
Cdd:cd14190    153 ---RYNPREKL-KVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMG--NWyfdEET 226
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  809 DEAPPPDAQDLITLLLRQNPLERLGTG 835
Cdd:cd14190    227 FEHVSDEAKDFVSNLIIKERSARMSAT 253
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
579-862 7.76e-29

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: 118.98  E-value: 7.76e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafverdILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDc 658
Cdd:cd14175      9 IGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEI------LLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGE- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 atLMKNMgplpvdMARMYFAE----TVL-----ALEYLHNYGIVHRDLKPDNLL-VTSMGH---IKLTDFGLSKvglmsm 725
Cdd:cd14175     82 --LLDKI------LRQKFFSEreasSVLhtickTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAK------ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeghiEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF---FGDTPEELFGQVISDE 802
Cdd:cd14175    148 ---------QLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFangPSDTPEEILTRIGSGK 218
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  803 I-----NWPEKDEApppdAQDLITLLLRQNPLERLgtgGAYEVKQHRFFR---SLDWNSLLRQKAEFI 862
Cdd:cd14175    219 FtlsggNWNTVSDA----AKDLVSKMLHVDPHQRL---TAKQVLQHPWITqkdKLPQSQLNHQDVQLV 279
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
577-831 7.90e-29

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: 118.11  E-value: 7.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14187     13 RFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRR 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyegHIEK 736
Cdd:cd14187     93 SLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLAT-------------KVEY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEappPDA 816
Cdd:cd14187    160 DGER--KKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHIN---PVA 234
                          250
                   ....*....|....*
gi 1988312908  817 QDLITLLLRQNPLER 831
Cdd:cd14187    235 ASLIQKMLQTDPTAR 249
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
571-846 8.90e-29

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: 117.68  E-value: 8.90e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQ-QAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14107      2 SVYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIP-----LRSSTRaRAFQERDILARLSHRRLTCLLDQFETRKTLILI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH--IKLTDFGLSKvglmsmtt 727
Cdd:cd14107     77 LELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQ-------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyeghiEKDAREFLDKQVcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPE 807
Cdd:cd14107    149 -------EITPSEHQFSKY-GSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDT 220
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  808 KDEAP-PPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd14107    221 PEITHlSEDAKDFIKRVLQPDPEKR---PSASECLSHEWF 257
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
577-843 1.26e-28

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: 117.79  E-value: 1.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAfvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14183     12 RTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQN--EVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV----TSMGHIKLTDFGLSKVglmsMTTNLYeg 732
Cdd:cd14183     90 DLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATV----VDGPLY-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG--DTPEELFGQVISDEINWPEKDE 810
Cdd:cd14183    164 ------------TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQVDFPSPYW 231
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  811 APPPD-AQDLITLLLRQNPLERLgtgGAYEVKQH 843
Cdd:cd14183    232 DNVSDsAKELITMMLQVDVDQRY---SALQVLEH 262
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
573-846 1.27e-28

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: 118.14  E-value: 1.27e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKI----NKQNLILRNQIQQAFVERdiLTFAENPFVVSMY---CSFETRRH 645
Cdd:cd07863      2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVrvqtNEDGLPLSTVREVALLKR--LEAFDHPNIVRLMdvcATSRTDRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 --LCMVMEYVEGgDCATLMKNMGP--LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVg 721
Cdd:cd07863     80 tkVTLVFEHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARI- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttnlYEGHIEKDArefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQvISD 801
Cdd:cd07863    158 --------YSCQMALTP-------VVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGK-IFD 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  802 EINWPEKDEAP----------PPDAQ---------------DLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07863    222 LIGLPPEDDWPrdvtlprgafSPRGPrpvqsvvpeieesgaQLLLEMLTFNPHKRI---SAFRALQHPFF 288
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
572-831 2.09e-28

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: 116.83  E-value: 2.09e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRF-AMKKINKQNLILRNQIQ---QAFveRDILTFAE-------NPFVVSMYCSF 640
Cdd:cd08528      1 EYAVLELLGSGAFGCVYKVRKKSNGQTLlALKEINMTNPAFGRTEQerdKSV--GDIISEVNiikeqlrHPNIVRYYKTF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 ETRRHLCMVMEYVEGGDCATLMKNM----GPLPVDMARMYFAETVLALEYLHN-YGIVHRDLKPDNLLVTSMGHIKLTDF 715
Cdd:cd08528     79 LENDRLYIVMELIEGAPLGEHFSSLkeknEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  716 GLSKvglmsmttnlyeghiEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELF 795
Cdd:cd08528    159 GLAK---------------QKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLA 223
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  796 GQVISDEINwPEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd08528    224 TKIVEAEYE-PLPEGMYSDDITFVIRSCLTPDPEAR 258
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
573-796 3.02e-28

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: 117.65  E-value: 3.02e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVR-HKESRQRfAMKkinkqnlILRNQI---QQAFVERDILTF------AENPFVVSMYCSFET 642
Cdd:cd14210     15 YEVLSVLGKGSFGQVVKCLdHKTGQLV-AIK-------IIRNKKrfhQQALVEVKILKHlndndpDDKHNIVRYKDSFIF 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  643 RRHLCMVMEyVEGGDCATLMKNMG--PLPVDMARMyFAETVL-ALEYLHNYGIVHRDLKPDNLLVT--SMGHIKLTDFGL 717
Cdd:cd14210     87 RGHLCIVFE-LLSINLYELLKSNNfqGLSLSLIRK-FAKQILqALQFLHKLNIIHCDLKPENILLKqpSKSSIKVIDFGS 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SkvglmsmttnLYEGHIekdarefldkqvcgTPEYI------APEVILRQGYGKPVDWWAMGIILYEFLVGcVPFF-GDT 790
Cdd:cd14210    165 S----------CFEGEK--------------VYTYIqsrfyrAPEVILGLPYDTAIDMWSLGCILAELYTG-YPLFpGEN 219

                   ....*.
gi 1988312908  791 PEELFG 796
Cdd:cd14210    220 EEEQLA 225
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
570-832 3.21e-28

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: 116.27  E-value: 3.21e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL-ILRNQIQQAFVERD--ILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd14194      4 DDYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTkSSRRGVSREDIEREvsILKEIQHPNVITLHEVYENKTDV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG----HIKLTDFGLSkvgl 722
Cdd:cd14194     84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLA---- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttnlyegHIEKDAREFldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE 802
Cdd:cd14194    160 ----------HKIDFGNEF--KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVN 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  803 INWPEKD-EAPPPDAQDLITLLLRQNPLERL 832
Cdd:cd14194    228 YEFEDEYfSNTSALAKDFIRRLLVKDPKKRM 258
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
582-832 3.59e-28

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: 116.23  E-value: 3.59e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKkinkqnlILRNqIQQAFVERDILTFAEN-PFVVSMYCSFET----RRHLCMVMEYVEGG 656
Cdd:cd14089     12 GINGKVLECFHKKTGEKFALK-------VLRD-NPKARREVELHWRASGcPHIVRIIDVYENtyqgRKCLLVVMECMEGG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 D-----------------CATLMKNMGplpvdmarmyfaetvLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFG 716
Cdd:cd14089     84 ElfsriqeradsaftereAAEIMRQIG---------------SAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  717 LSK--VGLMSMTTNlyeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTpeel 794
Cdd:cd14089    149 FAKetTTKKSLQTP------------------CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNH---- 206
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  795 fGQVIS---------------DEiNWPEKDEapppDAQDLITLLLRQNPLERL 832
Cdd:cd14089    207 -GLAISpgmkkrirngqyefpNP-EWSNVSE----EAKDLIRGLLKTDPSERL 253
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
573-831 9.36e-28

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: 115.92  E-value: 9.36e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilrnQIQQAFVERDI--LTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14168     12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKAL----KGKESSIENEIavLRKIKHENIVALEDIYESPNHLYLVM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM---GHIKLTDFGLSKVglmsmtt 727
Cdd:cd14168     88 QLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQdeeSKIMISDFGLSKM------- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyeghiekDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISD--EINW 805
Cdd:cd14168    161 ---------EGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyEFDS 231
                          250       260
                   ....*....|....*....|....*.
gi 1988312908  806 PEKDEApPPDAQDLITLLLRQNPLER 831
Cdd:cd14168    232 PYWDDI-SDSAKDFIRNLMEKDPNKR 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
570-831 9.53e-28

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: 115.07  E-value: 9.53e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQnLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14113      6 DSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKK-LMKRDQVTH---ELGVLQSLQHPQLVGLLDTFETPTSYILV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV---TSMGHIKLTDFGLSkvglMSMT 726
Cdd:cd14113     82 LEMADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVdqsLSKPTIKLADFGDA----VQLN 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 TNLYEghiekdarefldKQVCGTPEYIAPEVILrqgyGKPV----DWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE 802
Cdd:cd14113    158 TTYYI------------HQLLGSPEFAAPEIIL----GNPVsltsDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLD 221
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  803 INWPEKD-EAPPPDAQDLITLLLRQNPLER 831
Cdd:cd14113    222 FSFPDDYfKGVSQKAKDFVCFLLQMDPAKR 251
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
570-832 1.27e-27

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: 114.72  E-value: 1.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL------ILRNQIQQafvERDILTFAENPFVVSMYCSFETR 643
Cdd:cd14195      4 EDHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLsssrrgVSREEIER---EVNILREIQHPNIITLHDIFENK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG----HIKLTDFGLSk 719
Cdd:cd14195     81 TDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIA- 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 vglmsmttnlyegHIEKDAREFldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd14195    160 -------------HKIEAGNEF--KNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNIS 224
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  800 SDEINWPEKDEAPPPD-AQDLITLLLRQNPLERL 832
Cdd:cd14195    225 AVNYDFDEEYFSNTSElAKDFIRRLLVKDPKKRM 258
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
572-778 1.70e-27

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: 114.06  E-value: 1.70e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLIlRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd08220      1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMT-KEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARM--YFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHI-KLTDFGLSKVglMSMTTN 728
Cdd:cd08220     80 YAPGGTLFEYIQQRKGSLLSEEEIlhFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKI--LSSKSK 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 LYeghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYE 778
Cdd:cd08220    158 AY--------------TVVGTPCYISPELCEGKPYNQKSDIWALGCVLYE 193
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
577-845 1.71e-27

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 114.40  E-value: 1.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKK--INKQNLILRNQIQQAFV-----ERDILTFAENPFVVSmYCSFE-TRRHLCM 648
Cdd:cd06629      7 ELIGKGTYGRVYLAMNATTGEMLAVKQveLPKTSSDRADSRQKTVVdalksEIDTLKDLDHPNIVQ-YLGFEeTEDYFSI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsMTTN 728
Cdd:cd06629     86 FLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISK-----KSDD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 LYEGHIEKDARefldkqvcGTPEYIAPEVI--LRQGYGKPVDWWAMGIILYEFLVGCVPFfgdTPEELFGQVIsdEINwp 806
Cdd:cd06629    161 IYGNNGATSMQ--------GSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMF--KLG-- 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1988312908  807 EKDEAPP--------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRF 845
Cdd:cd06629    226 NKRSAPPvpedvnlsPEALDFLNACFAIDPRDR---PTAAELLSHPF 269
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
577-832 1.76e-27

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: 114.35  E-value: 1.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14088      7 QVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDG--RKVRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFLELATGR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLL-VTSMGHIKL--TDFGLSKVglmsmttnlyegh 733
Cdd:cd14088     85 EVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyYNRLKNSKIviSDFHLAKL------------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdaREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE--------LFGQVISD--EI 803
Cdd:cd14088    152 -----ENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDdyenhdknLFRKILAGdyEF 226
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  804 NWPEKDEAPPPdAQDLITLLLRQNPLERL 832
Cdd:cd14088    227 DSPYWDDISQA-AKDLVTRLMEVEQDQRI 254
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
573-862 1.92e-27

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: 114.73  E-value: 1.92e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafverdILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14178      5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEI------LLRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLL-VTSMGH---IKLTDFGLSKvglmsmttn 728
Cdd:cd14178     79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAK--------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghiEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG---DTPEELFGQVISDEI-- 803
Cdd:cd14178    150 ------QLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpdDTPEEILARIGSGKYal 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  804 ---NWPEKDEApppdAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSLDW---NSLLRQKAEFI 862
Cdd:cd14178    224 sggNWDSISDA----AKDIVSKMLHVDPHQRL---TAPQVLRHPWIVNREYlsqNQLSRQDVHLV 281
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
574-843 2.80e-27

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: 114.43  E-value: 2.80e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  574 ETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIqqaFVERDILTFAEN-PFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14090      5 LTGELLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSRV---FREVETLHQCQGhPNILQLIEYFEDDERFYLVFEK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGdcaTLMKNMgplpvdMARMYFAE---------TVLALEYLHNYGIVHRDLKPDNLLVTSMGHI---KLTDFGL-SK 719
Cdd:cd14090     82 MRGG---PLLSHI------EKRVHFTEqeaslvvrdIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLgSG 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 VGLMSMTTNlyeghiEKDAREFLDKqvCGTPEYIAPEVI---LRQG--YGKPVDWWAMGIILYEFLVGCVPFFG------ 788
Cdd:cd14090    153 IKLSSTSMT------PVTTPELLTP--VGSAEYMAPEVVdafVGEAlsYDKRCDLWSLGVILYIMLCGYPPFYGrcgedc 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  789 ---------DTPEELFGQVISDEINWPEKD-EAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQH 843
Cdd:cd14090    225 gwdrgeacqDCQELLFHSIQEGEYEFPEKEwSHISAEAKDLISHLLVRDASQRY---TAEQVLQH 286
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
582-785 3.62e-27

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: 113.19  E-value: 3.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQqafvERDI-LTFAENPFVVSMY-CSFETRRHLCMVMEYVEGGDca 659
Cdd:cd13987      4 GTYGKVLLAVHKGSGTKMALKFVPKPSTKLKDFLR----EYNIsLELSVHPHIIKTYdVAFETEDYYVFAQEYAPYGD-- 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  660 tLMKNMGP---LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV--TSMGHIKLTDFGLS-KVGLmsmttnlyegh 733
Cdd:cd13987     78 -LFSIIPPqvgLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTrRVGS----------- 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  734 iekdarefLDKQVCGTPEYIAPEV---ILRQGY--GKPVDWWAMGIILYEFLVGCVP 785
Cdd:cd13987    146 --------TVKRVSGTIPYTAPEVceaKKNEGFvvDPSIDVWAFGVLLFCCLTGNFP 194
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
573-831 4.48e-27

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: 112.90  E-value: 4.48e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFV---RHKESRQRFAMKKINKQNLiLRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd08222      2 YRVVRKLGSGNFGTVYLVsdlKATADEELKVLKEISVGEL-QPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCA----TLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSmGHIKLTDFGLSKVgLMSm 725
Cdd:cd08222     81 TEYCEGGDLDdkisEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGISRI-LMG- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TTNLyeghiekdAREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEInw 805
Cdd:cd08222    158 TSDL--------ATTF-----TGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGET-- 222
                          250       260
                   ....*....|....*....|....*.
gi 1988312908  806 PEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd08222    223 PSLPDKYSKELNAIYSRMLNKDPALR 248
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
573-832 4.87e-27

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: 112.72  E-value: 4.87e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQI---QQAFVERDILTFAEN---PFVVSMYCSFETRRHL 646
Cdd:cd14005      2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMIngpVPVPLEIALLLKASKpgvPGVIRLLDWYERPDGF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGgdCATL---MKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIKLTDFGlskvgl 722
Cdd:cd14005     82 LLIMERPEP--CQDLfdfITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFG------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttnlyEGHIEKDA--REFldkqvCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGD----TPEELF 795
Cdd:cd14005    154 --------CGALLKDSvyTDF-----DGTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLCGDIPFENDeqilRGNVLF 220
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  796 GQVISDEinwpekdeapppdAQDLITLLLRQNPLERL 832
Cdd:cd14005    221 RPRLSKE-------------CCDLISRCLQFDPSKRP 244
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
577-846 6.14e-27

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: 112.33  E-value: 6.14e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14189      7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyeghiEK 736
Cdd:cd14189     87 SLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAA---------------RL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPppdA 816
Cdd:cd14189    152 EPPEQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLP---A 228
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  817 QDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14189    229 RHLLAGILKRNPGDRLTLD---QILEHEFF 255
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
572-778 6.99e-27

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: 112.90  E-value: 6.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHK-ESRQRFAMKKINKQNLILRNQIQQaFVERDIL---TFAENPFVVSMYCSFETRRHLC 647
Cdd:cd14052      1 RFANVELIGSGEFSQVYKVSERvPTGKVYAVKKLKPNYAGAKDRLRR-LEEVSILrelTLDGHDNIVQLIDSWEYHGHLY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPV-DMARMY--FAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMS 724
Cdd:cd14052     80 IQTELCENGSLDVFLSELGLLGRlDEFRVWkiLVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  725 MttnlyeghiekdareflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYE 778
Cdd:cd14052    160 R-----------------GIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
575-831 1.28e-26

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: 111.66  E-value: 1.28e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  575 TIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilrNQIQQAFVERDILT-FAENPFVVSMYCSFETRRH----LCMV 649
Cdd:cd13985      4 VTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDE---EQLRVAIKEIEIMKrLCGHPNIVQYYDSAILSSEgrkeVLLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVeGGDCATLMKNM--GPLPVDMARMYFAETVLALEYLH--NYGIVHRDLKPDNLLVTSMGHIKLTDFGlskvglmSM 725
Cdd:cd13985     81 MEYC-PGSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHsqSPPIIHRDIKIENILFSNTGRFKLCDFG-------SA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TTNLYEGHIEKD---AREFLDKQVcgTPEYIAPEVI---LRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEelfgQVI 799
Cdd:cd13985    153 TTEHYPLERAEEvniIEEEIQKNT--TPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKL----AIV 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1988312908  800 SDEINWPEKDEApPPDAQDLITLLLRQNPLER 831
Cdd:cd13985    227 AGKYSIPEQPRY-SPELHDLIRHMLTPDPAER 257
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
579-831 1.43e-26

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: 111.10  E-value: 1.43e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERD--ILTFAENPFVVSMYCSFE-TRRHLCMVMEYVEG 655
Cdd:cd14164      8 IGEGSFSKVKLATSQKYCCKVAIKIVDRRRA--SPDFVQKFLPRElsILRRVNHPNIVQMFECIEvANGRLYIVMEAAAT 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 gDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG-HIKLTDFGLSKvglmsmttnLYEGHI 734
Cdd:cd14164     86 -DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFAR---------FVEDYP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  735 EkdarefLDKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQviSDEINWPEKDEAPP 813
Cdd:cd14164    156 E------LSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQ--QRGVLYPSGVALEE 227
                          250
                   ....*....|....*...
gi 1988312908  814 PdAQDLITLLLRQNPLER 831
Cdd:cd14164    228 P-CRALIRTLLQFNPSTR 244
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
573-846 1.61e-26

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: 112.27  E-value: 1.61e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNL-------ILRN-QIQQAFVERDILTFAEnpfVVSMYCSFETRR 644
Cdd:cd07840      1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEkegfpitAIREiKLLQKLDHPNVVRLKE---IVTSKGSAKYKG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGgDCATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglm 723
Cdd:cd07840     78 SIYMVFEYMDH-DLTGLLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR---- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttnlyegHIEKD-AREFLDKQVcgTPEYIAPEVILrqG---YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd07840    153 ---------PYTKEnNADYTNRVI--TLWYRPPELLL--GatrYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIF 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  800 S-----DEINWPEKDEAP-----------------------PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07840    220 ElcgspTEENWPGVSDLPwfenlkpkkpykrrlrevfknviDPSALDLLDKLLTLDPKKRI---SADQALQHEYF 291
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
573-831 1.64e-26

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: 111.20  E-value: 1.64e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd08225      2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEK-EASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDcatLMKNM----GPL-PVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHI-KLTDFGLSKVglmsmt 726
Cdd:cd08225     81 CDGGD---LMKRInrqrGVLfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQ------ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeghiEKDAREFldKQVC-GTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEInw 805
Cdd:cd08225    152 --------LNDSMEL--AYTCvGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYF-- 219
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  806 pekdeAP-PP----DAQDLITLLLRQNPLER 831
Cdd:cd08225    220 -----APiSPnfsrDLRSLISQLFKVSPRDR 245
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
576-831 2.03e-26

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: 110.98  E-value: 2.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd08221      5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKER-RDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCAT-LMKNMGPL-PVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttnlyegh 733
Cdd:cd08221     84 GNLHDkIAQQKNQLfPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKV------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 ieKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDeiNWPEKDEAPP 813
Cdd:cd08221    151 --LDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQG--EYEDIDEQYS 226
                          250
                   ....*....|....*...
gi 1988312908  814 PDAQDLITLLLRQNPLER 831
Cdd:cd08221    227 EEIIQLVHDCLHQDPEDR 244
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
549-834 2.06e-26

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 115.88  E-value: 2.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  549 PETDESVSSSNaslklrrkPRESDFETIKLISNGAYGAVYFVrhkeSRQRFAMKKINKQNLILRNQIQQAFVERDI--LT 626
Cdd:PTZ00267    53 PEGEEVPESNN--------PREHMYVLTTLVGRNPTTAAFVA----TRGSDPKEKVVAKFVMLNDERQAAYARSELhcLA 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  627 FAENPFVVSMYCSFETRRHLCMVMEYVEGGD----CATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNL 702
Cdd:PTZ00267   121 ACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDlnkqIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANI 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  703 LVTSMGHIKLTDFGLSKvglmsmttnLYEGHIEKDarefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVG 782
Cdd:PTZ00267   201 FLMPTGIIKLGDFGFSK---------QYSDSVSLD----VASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTL 267
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  783 CVPFFGDTPEELFGQVIsdeinWPEKDEAPPP---DAQDLITLLLRQNPLERLGT 834
Cdd:PTZ00267   268 HRPFKGPSQREIMQQVL-----YGKYDPFPCPvssGMKALLDPLLSKNPALRPTT 317
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
573-856 2.49e-26

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: 111.37  E-value: 2.49e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd06611      7 WEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIES---EEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGlmsmttnlye 731
Cdd:cd06611     84 CDGGALDSIMLELErGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKN---------- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghieKDAREFLDKQVcGTPEYIAPEVIL-----RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEinwP 806
Cdd:cd06611    154 ----KSTLQKRDTFI-GTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSE---P 225
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  807 EKDEAP---PPDAQDLITLLLRQNPLERLGTGgayEVKQHRFFRSLDWNSLLR 856
Cdd:cd06611    226 PTLDQPskwSSSFNDFLKSCLVKDPDDRPTAA---ELLKHPFVSDQSDNKAIK 275
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
578-786 2.75e-26

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 110.70  E-value: 2.75e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFV------ERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd06628      7 LIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKKSMldalqrEIALLRELQHENIVQYLGSSSDANHLNIFLE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK---VGLMSMTTN 728
Cdd:cd06628     87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKkleANSLSTKNN 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  729 lyeghiekDAREFLDkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd06628    167 --------GARPSLQ----GSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF 212
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
577-834 2.79e-26

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: 110.68  E-value: 2.79e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKqnlilRNQIQQAFVERD------ILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd14070      8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDK-----KKAKKDSYVTKNlrregrIQQMIRHPNITQLLDILETENSYYLVM 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttnly 730
Cdd:cd14070     83 ELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNC---------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eGHIEKDAREFLDKqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD--TPEELFGQVISDEINwpek 808
Cdd:cd14070    153 -AGILGYSDPFSTQ--CGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMN---- 225
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  809 dEAPP---PDAQDLITLLLRQNPLERLGT 834
Cdd:cd14070    226 -PLPTdlsPGAISFLRSLLEPDPLKRPNI 253
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
565-843 3.69e-26

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: 110.41  E-value: 3.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  565 RRKPRESDFETI--KLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLILRNQIQQafvERDILTFAE-NPFVVSMYCS 639
Cdd:cd14197      1 RSEPFQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKrrKGQDCRMEIIH---EIAVLELAQaNPWVINLHEV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 FETRRHLCMVMEYVEGG---DCATLMKNMGPLPVDMARMyFAETVLALEYLHNYGIVHRDLKPDNLLVTS---MGHIKLT 713
Cdd:cd14197     78 YETASEMILVLEYAAGGeifNQCVADREEAFKEKDVKRL-MKQILEGVSFLHNNNVVHLDLKPQNILLTSespLGDIKIV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  714 DFGLSKvglmsmttnlyeghIEKDAREFldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE 793
Cdd:cd14197    157 DFGLSR--------------ILKNSEEL--REIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQE 220
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  794 LFGQVISDEINWPEKD-EAPPPDAQDLITLLLRQNPLERlgtGGAYEVKQH 843
Cdd:cd14197    221 TFLNISQMNVSYSEEEfEHLSESAIDFIKTLLIKKPENR---ATAEDCLKH 268
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
570-857 4.73e-26

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: 110.50  E-value: 4.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd06643      4 EDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKS---EEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttn 728
Cdd:cd06643     81 IEFCAGGAVDAVMLELErPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSA--------- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghieKDAREFLDK-QVCGTPEYIAPEVIL-----RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDE 802
Cdd:cd06643    152 -------KNTRTLQRRdSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSE 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  803 inwPEKDEAP---PPDAQDLITLLLRQNPLERLGTGgayEVKQHRFFRSLDWNSLLRQ 857
Cdd:cd06643    225 ---PPTLAQPsrwSPEFKDFLRKCLEKNVDARWTTS---QLLQHPFVSVLVSNKPLRE 276
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
573-830 5.01e-26

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: 110.59  E-value: 5.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQ-NLILRNQIqqaFVERDILTFAENPFVVSMYCSF--ETRRHLCMV 649
Cdd:cd06621      3 IVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDpNPDVQKQI---LRELEINKSCASPYIVKYYGAFldEQDSSIGIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNM-------GPLPVDMarmyFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvg 721
Cdd:cd06621     80 MEYCEGGSLDSIYKKVkkkggriGEKVLGK----IAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVS--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttnlyeghieKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFfgdtpeelfgqvisd 801
Cdd:cd06621    153 --------------GELVNSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF--------------- 203
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  802 einwpEKDEAPPPDAQDLITLLLRQNPLE 830
Cdd:cd06621    204 -----PPEGEPPLGPIELLSYIVNMPNPE 227
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
571-850 9.23e-26

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: 110.22  E-value: 9.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKIN---KQNLilRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd06615      1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHleiKPAI--RNQIIR---ELKVLHECNSPYIVGFYGAFYSDGEIS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVD-MARMYFAeTVLALEYLH-NYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSM 725
Cdd:cd06615     76 ICMEHMDGGSLDQVLKKAGRIPENiLGKISIA-VLRGLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeghiekdAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVP-----------FFGDTPEEL 794
Cdd:cd06615    155 ------------ANSFV-----GTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeleaMFGRPVSEG 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  795 FGQVISDEINWPEKDEAPP------------------------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFFRSLD 850
Cdd:cd06615    218 EAKESHRPVSGHPPDSPRPmaifelldyivnepppklpsgafsDEFQDFVDKCLKKNPKER---ADLKELTKHPFIKRAE 294
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
579-847 1.07e-25

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: 108.86  E-value: 1.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQAFVERDILTFAEN--PFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd06647     15 IGQGASGTVYTAIDVATGQEVAIKQMN-----LQQQPKKELIINEILVMRENknPNIVNYLDSYLVGDELWVVMEYLAGG 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMyFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmSMTTnlyeghiEK 736
Cdd:cd06647     90 SLTDVVTETCMDEGQIAAV-CRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA----QITP-------EQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DARefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISD---EINWPEKDEapp 813
Cdd:cd06647    158 SKR----STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtpELQNPEKLS--- 230
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  814 PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFFR 847
Cdd:cd06647    231 AIFRDFLNRCLEMDVEKR---GSAKELLQHPFLK 261
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
573-846 2.01e-25

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: 108.53  E-value: 2.01e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKInkqnlilrnQIQQ--------AFVERDILTFAENPFVVSMYCSFETRR 644
Cdd:cd07835      1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKI---------RLETedegvpstAIREISLLKELNHPNIVRLLDVVHSEN 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEggdcATLMKNMGPLPVD-----MARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLsk 719
Cdd:cd07835     72 KLYLVFEFLD----LDLKKYMDSSPLTgldppLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGL-- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 vglmsmttnlyeghiekdAREFldkqvcGTP------E-----YIAPEVIL--RQgYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd07835    146 ------------------ARAF------GVPvrtythEvvtlwYRAPEILLgsKH-YSTPVDIWSVGCIFAEMVTRRPLF 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  787 FGDTP-EELFG--QVIS--DEINWPEKDEAP------P---------------PDAQDLITLLLRQNPLERLgtgGAYEV 840
Cdd:cd07835    201 PGDSEiDQLFRifRTLGtpDEDVWPGVTSLPdykptfPkwarqdlskvvpsldEDGLDLLSQMLVYDPAKRI---SAKAA 277

                   ....*.
gi 1988312908  841 KQHRFF 846
Cdd:cd07835    278 LQHPYF 283
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
577-836 2.36e-25

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: 107.74  E-value: 2.36e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14192     10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKN---EINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVL-ALEYLHNYGIVHRDLKPDNLL-VTSMGH-IKLTDFGLSKvglmsmttnlyegh 733
Cdd:cd14192     87 ELFDRITDESYQLTELDAILFTRQICeGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLAR-------------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iEKDAREFLdKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISdeINW---PEKDE 810
Cdd:cd14192    153 -RYKPREKL-KVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVN--CKWdfdAEAFE 228
                          250       260
                   ....*....|....*....|....*.
gi 1988312908  811 APPPDAQDLITLLLRQNPLERLGTGG 836
Cdd:cd14192    229 NLSEEAKDFISRLLVKEKSCRMSATQ 254
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
577-831 2.56e-25

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: 108.09  E-value: 2.56e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDI--LTFAE-NPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14198     14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKRR---RGQDCRAEILHEIavLELAKsNPRVVNLHEVYETTSEIILILEYA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGD----CATLMKNMGPlPVDMARMyFAETVLALEYLHNYGIVHRDLKPDNLLVTS---MGHIKLTDFGLS-KVGlmsm 725
Cdd:cd14198     91 AGGEifnlCVPDLAEMVS-ENDIIRL-IRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDIKIVDFGMSrKIG---- 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeghiekDAREFldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINW 805
Cdd:cd14198    165 -----------HACEL--REIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDY 231
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  806 PEKDEAPPPD-AQDLITLLLRQNPLER 831
Cdd:cd14198    232 SEETFSSVSQlATDFIQKLLVKNPEKR 258
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
571-789 2.75e-25

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: 107.81  E-value: 2.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd08228      2 ANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGP----LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVgLMSMT 726
Cdd:cd08228     82 ELADAGDLSQMIKYFKKqkrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRF-FSSKT 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  727 TNLYeghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD 789
Cdd:cd08228    161 TAAH--------------SLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
572-831 2.92e-25

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: 107.58  E-value: 2.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnLILRNqiqqafVERDILTFA--ENPFVVSMYCSFE-------- 641
Cdd:cd14047      7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVK---LNNEK------AEREVKALAklDHPNIVRYNGCWDgfdydpet 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 --------TRRHLCMVMEYVEGGDCATLMKNMGPLPVD--MARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIK 711
Cdd:cd14047     78 sssnssrsKTKCLFIQMEFCEKGTLESWIEKRNGEKLDkvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVK 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  712 LTDFGLskvgLMSMTtnlyeGHIEKDAREfldkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP 791
Cdd:cd14047    158 IGDFGL----VTSLK-----NDGKRTKSK-------GTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSK 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  792 E--ELFGQVISDEINWPEKDEAPppdaqdLITLLLRQNPLER 831
Cdd:cd14047    222 FwtDLRNGILPDIFDKRYKIEKT------IIKKMLSKKPEDR 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
572-845 3.33e-25

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: 107.77  E-value: 3.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnlILRNQIQQAFVERDILT-FAENPFVVSMYCSFETRRHLCM-- 648
Cdd:cd06608      7 IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD----IIEDEEEEIKLEINILRkFSNHPNIATFYGAFIKKDPPGGdd 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 ----VMEYVEGGDCATLMKNM----GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkv 720
Cdd:cd06608     83 qlwlVMEYCGGGSVTDLVKGLrkkgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS-- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  721 glmSMTTnlyeghiekdaREFLDKQVC-GTPEYIAPEVI-----LRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:cd06608    161 ---AQLD-----------STLGRRNTFiGTPYWMAPEVIacdqqPDASYDARCDVWSLGITAIELADGKPPLCDMHPMRA 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  795 FGQVISDeinwpekdeaPPP----------DAQDLITLLLRQNPLERLGTGgayEVKQHRF 845
Cdd:cd06608    227 LFKIPRN----------PPPtlkspekwskEFNDFISECLIKNYEQRPFTE---ELLEHPF 274
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
570-849 5.62e-25

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: 108.61  E-value: 5.62e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETR------ 643
Cdd:cd07855      4 GDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTA-KRTLRELKILRHFKHDNIIAIRDILRPKvpyadf 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGgDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvGLM 723
Cdd:cd07855     83 KDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMAR-GLC 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 SMttnlyeghiEKDAREFLDKQVcGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEfLVGCVPFF--------------- 787
Cdd:cd07855    161 TS---------PEEHKYFMTEYV-ATRWYRAPELMLSlPEYTQAIDMWSVGCIFAE-MLGRRQLFpgknyvhqlqliltv 229
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  788 -GDTPEELFGQVISDEI-----NWPEKDEAP--------PPDAQDLITLLLRQNPLERLGTGGAYevkQHRFFRSL 849
Cdd:cd07855    230 lGTPSQAVINAIGADRVrryiqNLPNKQPVPwetlypkaDQQALDLLSQMLRFDPSERITVAEAL---QHPFLAKY 302
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
577-797 5.84e-25

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: 106.61  E-value: 5.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERD--ILTFAENPFVVSMYCSFE-TRRHLCMVMEYV 653
Cdd:cd14163      6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGG--PEEFIQRFLPRElqIVERLDHKNIIHVYEMLEsADGKIYLVMELA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMgHIKLTDFGLSKVglmsmttnlyegh 733
Cdd:cd14163     84 EDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQ------------- 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  734 IEKDAREfLDKQVCGTPEYIAPEVIlrQGY---GKPVDWWAMGIILYEFLVGCVPFFG-DTPEELFGQ 797
Cdd:cd14163    150 LPKGGRE-LSQTFCGSTAYAAPEVL--QGVphdSRKGDIWSMGVVLYVMLCAQLPFDDtDIPKMLCQQ 214
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
571-832 7.61e-25

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: 106.24  E-value: 7.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIK-LISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14191      1 SDFYDIEeRLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQ---EISIMNCLHHPKLVQCVDAFEEKANIVMV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDC-ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLL-VTSMG-HIKLTDFGLSKvglmsmt 726
Cdd:cd14191     78 LEMVSGGELfERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLAR------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyegHIEKDAREfldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISdeINWP 806
Cdd:cd14191    151 ------RLENAGSL---KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTS--ATWD 219
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  807 EKDEA---PPPDAQDLITLLLRQNPLERL 832
Cdd:cd14191    220 FDDEAfdeISDDAKDFISNLLKKDMKARL 248
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
577-847 8.31e-25

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: 106.36  E-value: 8.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQ---IQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd06630      6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEQeevVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG-HIKLTDFGlSKVGLMSMTTNlyeg 732
Cdd:cd06630     86 AGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFG-AAARLASKGTG---- 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hiekdAREFlDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV--ISDEINWPEKDE 810
Cdd:cd06630    161 -----AGEF-QGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIfkIASATTPPPIPE 234
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  811 APPPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFFR 847
Cdd:cd06630    235 HLSPGLRDVTLRCLELQPEDR---PPARELLKHPVFT 268
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
571-831 1.03e-24

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: 106.86  E-value: 1.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQnlILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd06622      1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLE--LDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLM---KNMGPLPVDMARMYFAETVLALEYL---HNygIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglms 724
Cdd:cd06622     79 EYMDAGSLDKLYaggVATEGIPEDVLRRITYAVVKGLKFLkeeHN--IIHRDVKPTNVLVNGNGQVKLCDFGVS------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeGHIEKDarefLDKQVCGTPEYIAPEVILRQG------YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV 798
Cdd:cd06622    151 -------GNLVAS----LAKTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYPPETYANIFAQL 219
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1988312908  799 --ISDeinwpekdeAPPP--------DAQDLITLLLRQNPLER 831
Cdd:cd06622    220 saIVD---------GDPPtlpsgysdDAQDFVAKCLNKIPNRR 253
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
577-846 1.19e-24

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: 105.48  E-value: 1.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14188      7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyeghiEK 736
Cdd:cd14188     87 SMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAA---------------RL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPppdA 816
Cdd:cd14188    152 EPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAP---A 228
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  817 QDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14188    229 KHLIASMLSKNPEDRPSLD---EIIRHDFF 255
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
573-812 1.22e-24

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: 106.66  E-value: 1.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRF-AMKKINKQNL---ILRNQIQQAFVERDILTFaENPFVVSMY--CSF-ETRRH 645
Cdd:cd07862      3 YECVAEIGEGAYGKVFKARDLKNGGRFvALKRVRVQTGeegMPLSTIREVAVLRHLETF-EHPNVVRLFdvCTVsRTDRE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 --LCMVMEYVEGGDCATLMKNMGP-LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGL 722
Cdd:cd07862     82 tkLTLVFEHVDQDLTTYLDKVPEPgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIYS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 MSMTTNLyeghiekdarefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIsDE 802
Cdd:cd07862    162 FQMALTS----------------VVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKIL-DV 224
                          250
                   ....*....|
gi 1988312908  803 INWPEKDEAP 812
Cdd:cd07862    225 IGLPGEEDWP 234
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
582-832 1.24e-24

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: 105.84  E-value: 1.24e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKkinkqnLILRNQIQQAFVERDILTfAENPFVVSMYCSFET----RRHLCMVMEYVEGGD 657
Cdd:cd14172     15 GVNGKVLECFHRRTGQKCALK------LLYDSPKARREVEHHWRA-SGGPHIVHILDVYENmhhgKRCLLIIMECMEGGE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLMKNMG--PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM---GHIKLTDFGLSKvglmsmttnlyeg 732
Cdd:cd14172     88 LFSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAK------------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hiEKDAREFLdKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTpeelfGQVISDEIN-------- 804
Cdd:cd14172    155 --ETTVQNAL-QTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNT-----GQAISPGMKrrirmgqy 226
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  805 ------WPEKDEapppDAQDLITLLLRQNPLERL 832
Cdd:cd14172    227 gfpnpeWAEVSE----EAKQLIRHLLKTDPTERM 256
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
572-831 1.38e-24

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: 105.16  E-value: 1.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQnLILRNQIQQAFVERDIL-TFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd13997      1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKP-FRGPKERARALREVEAHaALGQHPNIVRYYSSWEEGGHLYIQM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGP---LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsMTT 727
Cdd:cd13997     80 ELCENGSLQDALEELSPiskLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATR----LET 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NLyeghiekDAREfldkqvcGTPEYIAPEVI-LRQGYGKPVDWWAMGIILYEFLVGCV-PFFGDTPEEL--------FGQ 797
Cdd:cd13997    156 SG-------DVEE-------GDSRYLAPELLnENYTHLPKADIFSLGVTVYEAATGEPlPRNGQQWQQLrqgklplpPGL 221
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  798 VISDEInwpekdeapppdaQDLITLLLRQNPLER 831
Cdd:cd13997    222 VLSQEL-------------TRLLKVMLDPDPTRR 242
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
579-832 1.41e-24

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: 106.03  E-value: 1.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQ-----RFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14076      9 LGEGEFGKVKLGWPLPKANhrsgvQVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttNLYeGH 733
Cdd:cd14076     89 SGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFA---------NTF-DH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEKDarefLDKQVCGTPEYIAPE-VILRQGY-GKPVDWWAMGIILYEFLVGCVPF-------FGDTPEELFGQVISDEIN 804
Cdd:cd14076    159 FNGD----LMSTSCGSPCYAAPElVVSDSMYaGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLI 234
                          250       260
                   ....*....|....*....|....*...
gi 1988312908  805 WPEKDEappPDAQDLITLLLRQNPLERL 832
Cdd:cd14076    235 FPEYVT---PKARDLLRRILVPNPRKRI 259
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
567-847 1.82e-24

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: 106.35  E-value: 1.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  567 KPRESDFETIkliSNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQAFVERDILTFAEN--PFVVSMYCSFETRR 644
Cdd:cd06654     19 KKKYTRFEKI---GQGASGTVYTAMDVATGQEVAIRQMN-----LQQQPKKELIINEILVMRENknPNIVNYLDSYLVGD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGDCATLMKNMGPLPVDMARMyFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmS 724
Cdd:cd06654     91 ELWVVMEYLAGGSLTDVVTETCMDEGQIAAV-CRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA----Q 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTTnlyeghiEKDAREfldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISD--- 801
Cdd:cd06654    166 ITP-------EQSKRS----TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNgtp 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1988312908  802 EINWPEKDEAPppdAQDLITLLLRQNPLERlgtGGAYEVKQHRFFR 847
Cdd:cd06654    235 ELQNPEKLSAI---FRDFLNRCLEMDVEKR---GSAKELLQHQFLK 274
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
573-795 3.38e-24

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: 105.08  E-value: 3.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKI--NKQNLILRnqiQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd07848      3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFkdSEENEEVK---ETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNLY 730
Cdd:cd07848     80 EYVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFAR--------NLS 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  731 EGHiEKDAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELF 795
Cdd:cd07848    152 EGS-NANYTEYV-----ATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEiDQLF 211
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
582-787 3.41e-24

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: 104.80  E-value: 3.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLilrNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATL 661
Cdd:cd06624     19 GTFGVVYAARDLSTQVRIAIKEIPERDS---REVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSAL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  662 MKNM-GPLPVDMARM-YFAETVL-ALEYLHNYGIVHRDLKPDNLLV-TSMGHIKLTDFGLSK--VGLMSMTTNLyeghie 735
Cdd:cd06624     96 LRSKwGPLKDNENTIgYYTKQILeGLKYLHDNKIVHRDIKGDNVLVnTYSGVVKISDFGTSKrlAGINPCTETF------ 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  736 kdarefldkqvCGTPEYIAPEVILR--QGYGKPVDWWAMGIILYEFLVGCVPFF 787
Cdd:cd06624    170 -----------TGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFI 212
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
579-847 3.47e-24

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: 105.58  E-value: 3.47e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQAFVERDILTFAE--NPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd06655     27 IGQGASGTVFTAIDVATGQEVAIKQIN-----LQKQPKKELIINEILVMKElkNPNIVNFLDSFLVGDELFVVMEYLAGG 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMyFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmSMTTnlyeghiEK 736
Cdd:cd06655    102 SLTDVVTETCMDEAQIAAV-CRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCA----QITP-------EQ 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREfldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPPPDA 816
Cdd:cd06655    170 SKRS----TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIF 245
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  817 QDLITLLLRQNPLERlgtGGAYEVKQHRFFR 847
Cdd:cd06655    246 RDFLNRCLEMDVEKR---GSAKELLQHPFLK 273
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
568-847 3.86e-24

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: 105.12  E-value: 3.86e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESDFETIKlISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQA--FVERDILTFAENPFVVSMYCSFETRRH 645
Cdd:cd06658     20 PREYLDSFIK-IGEGSTGIVCIATEKHTGKQVAVKKMD-----LRKQQRREllFNEVVIMRDYHHENVVDMYNSYLVGDE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAeTVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsm 725
Cdd:cd06658     94 LWVVMEFLEGGALTDIVTHTRMNEEQIATVCLS-VLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFC------- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeGHIEKDAREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQvISDEInw 805
Cdd:cd06658    166 ------AQVSKEVPK--RKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRR-IRDNL-- 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  806 pekdeapPPDAQDL----------ITLLLRQNPLERlgtGGAYEVKQHRFFR 847
Cdd:cd06658    235 -------PPRVKDShkvssvlrgfLDLMLVREPSQR---ATAQELLQHPFLK 276
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
574-824 4.28e-24

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: 104.23  E-value: 4.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  574 ETIKLISNGAYGAVYFVRHKESRQRFAMKKIN----KQNLILRNQIQqafverdILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14193      7 NKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKarsqKEKEEVKNEIE-------VMNQLNHANLIQLYDAFESRNDIVLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTS--MGHIKLTDFGLSKvglmsmt 726
Cdd:cd14193     80 MEYVDGGELFDRIIDENYNLTELDTILFIKQICeGIQYMHQMYILHLDLKPENILCVSreANQVKIIDFGLAR------- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeghiEKDAREFLdKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISdeINWP 806
Cdd:cd14193    153 --------RYKPREKL-RVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILA--CQWD 221
                          250       260
                   ....*....|....*....|.
gi 1988312908  807 EKDEA---PPPDAQDLITLLL 824
Cdd:cd14193    222 FEDEEfadISEEAKDFISKLL 242
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
577-846 5.05e-24

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 103.75  E-value: 5.05e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRnqiqqafvERDILTFAENPFVVSMYCSFET-RRHLCMVMEYVEG 655
Cdd:cd14109     10 EDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMR--------EVDIHNSLDHPNIVQMHDAYDDeKLAVTVIDNLAST 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDcatLMKNMGPLPVDM-----ARMYFAETVLALEYLHNYGIVHRDLKPDNLLVtSMGHIKLTDFGLSKvglmsmttnly 730
Cdd:cd14109     82 IE---LVRDNLLPGKDYyterqVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSR----------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 egHIEKDAREFLDKqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVisDEINWPEKDE 810
Cdd:cd14109    147 --RLLRGKLTTLIY---GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNV--RSGKWSFDSS 219
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1988312908  811 APPP---DAQDLITLLLRQNPLERLGTGgayEVKQHRFF 846
Cdd:cd14109    220 PLGNisdDARDFIKKLLVYIPESRLTVD---EALNHPWF 255
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
577-831 6.24e-24

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 108.42  E-value: 6.24e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNL----ILRNQIQ----------------QAFVERDiltfAENPFVVSM 636
Cdd:PTZ00283    38 RVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMseadKNRAQAEvccllncdffsivkchEDFAKKD----PRNPENVLM 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  637 ycsfetrrhLCMVMEYVEGGDCATLMKNMG----PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKL 712
Cdd:PTZ00283   114 ---------IALVLDYANAGDLRQEIKSRAktnrTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKL 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  713 TDFGLSKvglmsmttnLYEGHIEKDarefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPE 792
Cdd:PTZ00283   185 GDFGFSK---------MYAATVSDD----VGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENME 251
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  793 ELFGQVISDEInwpekDEAPP---PDAQDLITLLLRQNPLER 831
Cdd:PTZ00283   252 EVMHKTLAGRY-----DPLPPsisPEMQEIVTALLSSDPKRR 288
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
573-832 8.01e-24

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: 103.43  E-value: 8.01e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14114      4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRK---EIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT--SMGHIKLTDFGLskvglmsmTTNL 729
Cdd:cd14114     81 LSGGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGL--------ATHL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 yeghiekDAREFLdKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISdeINWPEKD 809
Cdd:cd14114    153 -------DPKESV-KVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKS--CDWNFDD 222
                          250       260
                   ....*....|....*....|....*.
gi 1988312908  810 EA---PPPDAQDLITLLLRQNPLERL 832
Cdd:cd14114    223 SAfsgISEEAKDFIRKLLLADPNKRM 248
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
573-860 1.03e-23

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: 103.96  E-value: 1.03e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd06644     14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKS---EEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEF 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGG--DCATLMKNMGpLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTtnly 730
Cdd:cd06644     91 CPGGavDAIMLELDRG-LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQ---- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiEKDAreFLdkqvcGTPEYIAPEVILRQG-----YGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEinw 805
Cdd:cd06644    166 ----RRDS--FI-----GTPYWMAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSE--- 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  806 PEKDEAP---PPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFFRSLDWNSLLRQ-----KAE 860
Cdd:cd06644    232 PPTLSQPskwSMEFRDFLKTALDKHPETR---PSAAQLLEHPFVSSVTSNRPLRElvaeaKAE 291
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
573-832 1.26e-23

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: 104.72  E-value: 1.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVerdILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd14176     21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLL-VTSMGH---IKLTDFGLSKvglmsmttn 728
Cdd:cd14176     95 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK--------- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghiEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG---DTPEELFGQVISDEIN- 804
Cdd:cd14176    166 ------QLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSl 239
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1988312908  805 ----WPEKDEapppDAQDLITLLLRQNPLERL 832
Cdd:cd14176    240 sggyWNSVSD----TAKDLVSKMLHVDPHQRL 267
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
576-831 1.34e-23

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: 102.63  E-value: 1.34e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   576 IKLISNGAYGAVYF----VRHKESRQRFAMKKINKQnlILRNQIQQAFVERDILTFAENPFVVSMY--CSfeTRRHLCMV 649
Cdd:smart00221    4 GKKLGEGAFGEVYKgtlkGKGDGKEVEVAVKTLKED--ASEQQIEEFLREARIMRKLDHPNIVKLLgvCT--EEEPLMIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   650 MEYVEGGDCATLMKNMGPLPVDMARM-YFAETV-LALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtt 727
Cdd:smart00221   80 MEYMPGGDLLDYLRKNRPKELSLSDLlSFALQIaRGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSR-------- 151
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   728 NLYEGHIEKDAREFLdkqvcgtP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLVGC-VPFFGDTPEELFGQVISDEINW 805
Cdd:smart00221  152 DLYDDDYYKVKGGKL-------PiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGeEPYPGMSNAEVLEYLKKGYRLP 224
                           250       260
                    ....*....|....*....|....*....
gi 1988312908   806 PekdeaPPPDAQDLITLLLR---QNPLER 831
Cdd:smart00221  225 K-----PPNCPPELYKLMLQcwaEDPEDR 248
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
612-831 1.35e-23

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 103.17  E-value: 1.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  612 RNQIQQAFVERDILTFAENPFVVSMYCSFETRRH-LCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNY 690
Cdd:cd13990     45 QNYIKHALREYEIHKSLDHPRIVKLYDVFEIDTDsFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEI 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  691 --GIVHRDLKPDNLLVTSM---GHIKLTDFGLSKVglmsMTTNLY-EGHIEkdarefLDKQVCGTPEYIAPEVILRqGYG 764
Cdd:cd13990    125 kpPIIHYDLKPGNILLHSGnvsGEIKITDFGLSKI----MDDESYnSDGME------LTSQGAGTYWYLPPECFVV-GKT 193
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  765 KP-----VDWWAMGIILYEFLVGCVPFFGDTPEE--LFGQVI--SDEINWPEKDeAPPPDAQDLITLLLRQNPLER 831
Cdd:cd13990    194 PPkisskVDVWSVGVIFYQMLYGRKPFGHNQSQEaiLEENTIlkATEVEFPSKP-VVSSEAKDFIRRCLTYRKEDR 268
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
650-845 1.80e-23

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: 102.51  E-value: 1.80e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvGLMSMTTNL 729
Cdd:cd06631     82 MEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAK-RLCINLSSG 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 YEGHIEKDARefldkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKD 809
Cdd:cd06631    161 SQSQLLKSMR--------GTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLP 232
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1988312908  810 EAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRF 845
Cdd:cd06631    233 DKFSPEARDFVHACLTRDQDERP---SAEQLLKHPF 265
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
579-865 1.86e-23

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: 103.17  E-value: 1.86e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafverdILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDc 658
Cdd:cd14177     12 IGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEI------LMRYGQHPNIITLKDVYDDGRYVYLVTELMKGGE- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 atLMKNMgplpvdMARMYFAE----TVL-----ALEYLHNYGIVHRDLKPDNLLV----TSMGHIKLTDFGLSKvglmsm 725
Cdd:cd14177     85 --LLDRI------LRQKFFSEreasAVLytitkTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAK------ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyegHIEKDAREFLDKqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFF---GDTPEELFGQVISDE 802
Cdd:cd14177    151 -------QLRGENGLLLTP--CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGK 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  803 I-----NWPEKDEApppdAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSLDWNSLLRQKAEFIPQL 865
Cdd:cd14177    222 FslsggNWDTVSDA----AKDLLSHMLHVDPHQRY---TAEQVLKHSWIACRDQLPHYQLNRQDAPHL 282
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
573-846 1.92e-23

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: 102.35  E-value: 1.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRnqiqQAFVERDILTF------AENPFVVSMYCSFETRRHL 646
Cdd:cd14133      1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLD----QSLDEIRLLELlnkkdkADKYHIVRLKDVFYFKNHL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVeGGDCATLMKNMGPLPVDMARM-YFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMG--HIKLTDFGLSkvgl 722
Cdd:cd14133     77 CIVFELL-SQNLYEFLKQNKFQYLSLPRIrKIAQQILeALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGSS---- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttnLYEGhiekdarefldkQVCGTpeYI------APEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFG 796
Cdd:cd14133    152 ------CFLT------------QRLYS--YIqsryyrAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLA 211
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  797 QVISDEINWPEK--DEAPPPDAQ--DLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14133    212 RIIGTIGIPPAHmlDQGKADDELfvDFLKKLLEIDPKERP---TASQALSHPWL 262
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
573-846 2.00e-23

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: 102.97  E-value: 2.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd07860      2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKI-RLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGgDCATLMKNMGP--LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLY 730
Cdd:cd07860     81 LHQ-DLKKFMDASALtgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTH 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EghiekdarefldkqvCGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELFgQVIS-----DEI 803
Cdd:cd07860    160 E---------------VVTLWYRAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEiDQLF-RIFRtlgtpDEV 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  804 NWPEKDEAP------------------PP---DAQDLITLLLRQNPLERLGTGGAYevkQHRFF 846
Cdd:cd07860    224 VWPGVTSMPdykpsfpkwarqdfskvvPPldeDGRDLLSQMLHYDPNKRISAKAAL---AHPFF 284
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
577-836 3.17e-23

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: 102.81  E-value: 3.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQnlilrnqiQQAFVERDI--LTFAE-NPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14179     13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKR--------MEANTQREIaaLKLCEgHPNIVKLHEVYHDQLHTFLVMELL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---HIKLTDFGLSKVglmsmttnly 730
Cdd:cd14179     85 KGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFARL---------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghieKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF-------FGDTPEELFGQVISDEI 803
Cdd:cd14179    155 -----KPPDNQPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFqchdkslTCTSAEEIMKKIKQGDF 229
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  804 NWP-EKDEAPPPDAQDLITLLLRQNPLERLGTGG 836
Cdd:cd14179    230 SFEgEAWKNVSQEAKDLIQGLLTVDPNKRIKMSG 263
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
573-783 4.07e-23

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 102.06  E-value: 4.07e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKI--NKQNLILRnqiQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd07847      3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFveSEDDPVIK---KIALREIRMLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvgLMSMTTNLY 730
Cdd:cd07847     80 EYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR--ILTGPGDDY 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  731 EGHIekdarefldkqvcGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGC 783
Cdd:cd07847    158 TDYV-------------ATRWYRAPELLVgDTQYGPPVDVWAIGCVFAELLTGQ 198
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
572-787 4.13e-23

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: 101.31  E-value: 4.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQ-----QAFVERDILTFAE---NPFVVSMYCSFETR 643
Cdd:cd14004      1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRdrklgTVPLEIHILDTLNkrsHPNIVKLLDFFEDD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVME-YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvgl 722
Cdd:cd14004     81 EFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA---- 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  723 msmtTNLYEGHIEkdarefldkQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFF 787
Cdd:cd14004    157 ----AYIKSGPFD---------TFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVFKENPFY 209
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
575-832 4.16e-23

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: 102.76  E-value: 4.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  575 TIKLISNGAYGAVYFVRHKESRQRFAMKKINKqnlilRNQIQQafvERDILTFAEN-PFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14092     10 REEALGDGSFSVCRKCVHKKTGQEFAVKIVSR-----RLDTSR---EVQLLRLCQGhPNIVKLHEVFQDELHTYLVMELL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---HIKLTDFGLS--KVGLMSMTTN 728
Cdd:cd14092     82 RGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDddaEIKIVDFGFArlKPENQPLKTP 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 lyeghiekdarefldkqvCGTPEYIAPEVILR----QGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI----S 800
Cdd:cd14092    162 ------------------CFTLPYAAPEVLKQalstQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMkrikS 223
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  801 DEIN-----WpekdEAPPPDAQDLITLLLRQNPLERL 832
Cdd:cd14092    224 GDFSfdgeeW----KNVSSEAKSLIQGLLTVDPSKRL 256
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
567-847 5.22e-23

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: 102.11  E-value: 5.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  567 KPRESDFETIkliSNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQAFVERDILTFAEN--PFVVSMYCSFETRR 644
Cdd:cd06656     18 KKKYTRFEKI---GQGASGTVYTAIDIATGQEVAIKQMN-----LQQQPKKELIINEILVMRENknPNIVNYLDSYLVGD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGDCATLMKNMGPLPVDMARMyFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmS 724
Cdd:cd06656     90 ELWVVMEYLAGGSLTDVVTETCMDEGQIAAV-CRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCA----Q 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTTnlyeghiEKDAREfldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISD--- 801
Cdd:cd06656    165 ITP-------EQSKRS----TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNgtp 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1988312908  802 EINWPEKDEAPppdAQDLITLLLRQNPLERlgtGGAYEVKQHRFFR 847
Cdd:cd06656    234 ELQNPERLSAV---FRDFLNRCLEMDVDRR---GSAKELLQHPFLK 273
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
565-831 8.45e-23

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: 100.89  E-value: 8.45e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  565 RRKPREsDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVerdILTFAENPFVVSMYCSFETRR 644
Cdd:cd06645      6 RRNPQE-DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEII---MMKDCKHSNIVAYFGSYLRRD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmS 724
Cdd:cd06645     82 KLWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSA----Q 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTTNLYEghiekdareflDKQVCGTPEYIAPEVIL---RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISD 801
Cdd:cd06645    158 ITATIAK-----------RKSFIGTPYWMAPEVAAverKGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKS 226
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1988312908  802 EINWPE-KDEAPPPDA-QDLITLLLRQNPLER 831
Cdd:cd06645    227 NFQPPKlKDKMKWSNSfHHFVKMALTKNPKKR 258
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
569-813 8.90e-23

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: 102.06  E-value: 8.90e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQ-NLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd06650      3 KDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEiKPAIRNQIIR---ELQVLHECNSPYIVGFYGAFYSDGEIS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYL-HNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMt 726
Cdd:cd06650     80 ICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeghiekdAREFLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL---FGQVISDEI 803
Cdd:cd06650    159 -----------ANSFV-----GTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELelmFGCQVEGDA 222
                          250
                   ....*....|
gi 1988312908  804 NWPEKDEAPP 813
Cdd:cd06650    223 AETPPRPRTP 232
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
572-846 1.21e-22

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: 99.60  E-value: 1.21e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKES-------RQRFAMKKINKQNLILRNQIQQAFVERdiLTFAENpfVVSMYCSFETRR 644
Cdd:cd14019      2 KYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSSPSRILNELECLER--LGGSNN--VSGLITAFRNED 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGDCATLMKNMGPLpvDMaRMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS-MGHIKLTDFGLSKvglm 723
Cdd:cd14019     78 QVVAVLPYIEHDDFRDFYRKMSLT--DI-RIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNReTGKGVLVDFGLAQ---- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttNLYEGHIEKDAREfldkqvcGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE--------L 794
Cdd:cd14019    151 ----REEDRPEQRAPRA-------GTRGFRAPEVLFKcPHQTTAIDIWSAGVILLSILSGRFPFFFSSDDIdalaeiatI 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  795 FGQvisdeinwpekdeappPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14019    220 FGS----------------DEAYDLLDKLLELDPSKRI---TAEEALKHPFF 252
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
554-845 1.36e-22

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 102.21  E-value: 1.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  554 SVSSSNASLKLRRKPRESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKI--NKQNLIlRNQIQQafvERDILTFAENP 631
Cdd:PLN00034    57 SSSSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygNHEDTV-RRQICR---EIEILRDVNHP 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  632 FVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARmyfaETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIK 711
Cdd:PLN00034   133 NVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAKNVK 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  712 LTDFGLSKVGLMSMttnlyeghiekdarEFLDKQVcGTPEYIAPEVI---LRQGY--GKPVDWWAMGIILYEFLVGCVPF 786
Cdd:PLN00034   209 IADFGVSRILAQTM--------------DPCNSSV-GTIAYMSPERIntdLNHGAydGYAGDIWSLGVSILEFYLGRFPF 273
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  787 F----GDTPEELFGQVISDEinwPEKDEAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRF 845
Cdd:PLN00034   274 GvgrqGDWASLMCAICMSQP---PEAPATASREFRHFISCCLQREPAKRW---SAMQLLQHPF 330
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
573-846 1.64e-22

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: 101.49  E-value: 1.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKkinkqnlILRNQ---IQQAFVERDIL-TFAEN-----PFVVSMYCSFETR 643
Cdd:cd14134     14 YKILRLLGEGTFGKVLECWDRKRKRYVAVK-------IIRNVekyREAAKIEIDVLeTLAEKdpngkSHCVQLRDWFDYR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVME------YveggdcaTLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS--------- 706
Cdd:cd14134     87 GHMCIVFEllgpslY-------DFLKknNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynp 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  707 ----------MGHIKLTDFGlskvglmSMTtnlYEghiekdaREFlDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIIL 776
Cdd:cd14134    160 kkkrqirvpkSTDIKLIDFG-------SAT---FD-------DEY-HSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCIL 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  777 YEFLVGCVPF---------------FGDTPEELFGQVISD---------EINWPEK------------------DEAPPP 814
Cdd:cd14134    222 VELYTGELLFqthdnlehlammeriLGPLPKRMIRRAKKGakyfyfyhgRLDWPEGsssgrsikrvckplkrlmLLVDPE 301
                          330       340       350
                   ....*....|....*....|....*....|....
gi 1988312908  815 DAQ--DLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14134    302 HRLlfDLIRKMLEYDPSKRI---TAKEALKHPFF 332
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
575-843 1.73e-22

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: 100.10  E-value: 1.73e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  575 TIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiqqafVERDILTFAE---NPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14174      6 TDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSR-----VFREVETLYQcqgNKNILELIEFFEDDTRFYLVFE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS---MGHIKLTDFGL-SKVGLMSMTT 727
Cdd:cd14174     81 KLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESpdkVSPVKICDFDLgSGVKLNSACT 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 NLYEGHIEKDarefldkqvCGTPEYIAPEVI-----LRQGYGKPVDWWAMGIILYEFLVGCVPFFG--------DTPE-- 792
Cdd:cd14174    161 PITTPELTTP---------CGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGhcgtdcgwDRGEvc 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  793 -----ELFGQVISDEINWPEKDEAP-PPDAQDLITLLLRQNPLERLgtgGAYEVKQH 843
Cdd:cd14174    232 rvcqnKLFESIQEGKYEFPDKDWSHiSSEAKDLISKLLVRDAKERL---SAAQVLQH 285
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
573-790 2.32e-22

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: 99.80  E-value: 2.32e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKK-INKQNLILRNQIqqAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd07846      3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKfLESEDDKMVKKI--AMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLYE 731
Cdd:cd07846     81 FVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART--LAAPGEVYT 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 GHIekdarefldkqvcGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVGCVPFFGDT 790
Cdd:cd07846    159 DYV-------------ATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTGEPLFPGDS 205
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
673-832 2.57e-22

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: 99.79  E-value: 2.57e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  673 ARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH-IKLTDFGLSKvGLMSMTTNLyeghieKDARefldkqvcGTPE 751
Cdd:cd13974    134 ALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGK-HLVSEDDLL------KDQR--------GSPA 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  752 YIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEkDEAPPPDAQDLITLLLRQNPLE 830
Cdd:cd13974    199 YISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPE-DGRVSENTVCLIRKLLVLNPQK 277

                   ..
gi 1988312908  831 RL 832
Cdd:cd13974    278 RL 279
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
577-831 4.93e-22

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 97.99  E-value: 4.93e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVY---FVRHKESRQRFAMKKINKqnlILRNQIQQAFV-ERDILTFAENPFVVSMY--CSfeTRRHLCMVM 650
Cdd:cd00192      1 KKLGEGAFGEVYkgkLKGGDGKTVDVAVKTLKE---DASESERKDFLkEARVMKKLGHPNVVRLLgvCT--EEEPLYLVM 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGPLPVDMARMYFAETVL---------ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvg 721
Cdd:cd00192     76 EYMEGGDLLDFLRKSRPVFPSPEPSTLSLKDLlsfaiqiakGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSR-- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttNLYEGHIEKDARefldkqvcGTPEYI---APEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELFGQ 797
Cdd:cd00192    154 ------DIYDDDYYRKKT--------GGKLPIrwmAPESLKDGIFTSKSDVWSFGVLLWEiFTLGATPYPGLSNEEVLEY 219
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  798 VISDEInwPEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd00192    220 LRKGYR--LPKPENCPDELYELMLSCWQLDPEDR 251
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
572-850 5.07e-22

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: 98.99  E-value: 5.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKI----NKQNL--ILRNQiqqafveRDILTFAENPFVVSMYCSFETRRH 645
Cdd:cd06618     16 DLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMrrsgNKEENkrILMDL-------DVVLKSHDCPYIVKCYGYFITDSD 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYL-HNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvGLMs 724
Cdd:cd06618     89 VFICMELMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGIS--GRL- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghIEKDAReflDKQVcGTPEYIAPEVILRQGYGK---PVDWWAMGIILYEFLVGCVPFFGDTPE-ELFGQVIS 800
Cdd:cd06618    166 ---------VDSKAK---TRSA-GCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILN 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  801 DEINWPEKDEAPPPDAQDLITLLLRQNPLERlgtgGAY-EVKQHRFFRSLD 850
Cdd:cd06618    233 EEPPSLPPNEGFSPDFCSFVDLCLTKDHRYR----PKYrELLQHPFIRRYE 279
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
576-831 5.42e-22

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 97.99  E-value: 5.42e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   576 IKLISNGAYGAVYF----VRHKESRQRFAMKKINKQnlILRNQIQQAFVERDILTFAENPFVVSMY--CSFETRrhLCMV 649
Cdd:smart00219    4 GKKLGEGAFGEVYKgklkGKGGKKKVEVAVKTLKED--ASEQQIEEFLREARIMRKLDHPNVVKLLgvCTEEEP--LYIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   650 MEYVEGGDCAT-LMKNMGPLPVDMaRMYFAETV-LALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtt 727
Cdd:smart00219   80 MEYMEGGDLLSyLRKNRPKLSLSD-LLSFALQIaRGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSR-------- 150
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908   728 NLYEGhiekdarEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLVGC-VPFFGDTPEELFGQVISDEINW 805
Cdd:smart00219  151 DLYDD-------DYYRKRGGKLPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGeQPYPGMSNEEVLEYLKNGYRLP 223
                           250       260
                    ....*....|....*....|....*....
gi 1988312908   806 PekdeaPPPDAQDLITLLLR---QNPLER 831
Cdd:smart00219  224 Q-----PPNCPPELYDLMLQcwaEDPEDR 247
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
572-850 5.70e-22

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: 98.41  E-value: 5.70e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnLILRNQIQ-QAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd06619      2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIP---LDITVELQkQIMSELEILYKCDSPYIIGFYGAFFVENRISICT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNmgPLPVdMARMYFAeTVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTtnly 730
Cdd:cd06619     79 EFMDGGSLDVYRKI--PEHV-LGRIAVA-VVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIA---- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 eghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVP---FFGD----TPEELFGQVIsdei 803
Cdd:cd06619    151 -------------KTYVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPypqIQKNqgslMPLQLLQCIV---- 213
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  804 nwpekDEAPP--PDAQ------DLITLLLRQNPLERLGTGgayEVKQHRFFRSLD 850
Cdd:cd06619    214 -----DEDPPvlPVGQfsekfvHFITQCMRKQPKERPAPE---NLMDHPFIVQYN 260
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
577-848 6.47e-22

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 99.84  E-value: 6.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKK-----INKQNLILRNQIQQA---FV---ERDILTFAENPFVVSMYCSFETRRH 645
Cdd:PTZ00024    15 AHLGEGTYGKVEKAYDTLTGKIVAIKKvkiieISNDVTKDRQLVGMCgihFTtlrELKIMNEIKHENIMGLVDVYVEGDF 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGgDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSM 725
Cdd:PTZ00024    95 INLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPP 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 TTNLYEGHIEKDAREFLDKQVCgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS---- 800
Cdd:PTZ00024   174 YSDTLSKDETMQRREEMTSKVV-TLWYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFEllgt 252
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  801 -DEINWPEKDEAP--------------------PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRS 848
Cdd:PTZ00024   253 pNEDNWPQAKKLPlyteftprkpkdlktifpnaSDDAIDLLQSLLKLNPLERI---SAKEALKHEYFKS 318
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
571-789 1.17e-21

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: 97.79  E-value: 1.17e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd08229     24 ANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMKNMGP----LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVgLMSMT 726
Cdd:cd08229    104 ELADAGDLSRMIKHFKKqkrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRF-FSSKT 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  727 TNLYeghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD 789
Cdd:cd08229    183 TAAH--------------SLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
582-786 1.57e-21

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: 97.52  E-value: 1.57e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVS-------MYCSFETRRHLcMVMEYVE 654
Cdd:cd13989      4 GGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSardvppeLEKLSPNDLPL-LAMEYCS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLM---KN---MGPLPVdmaRMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSKVglmsm 725
Cdd:cd13989     83 GGDLRKVLnqpENccgLKESEV---RTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKE----- 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  726 ttnlyeghiekdarefLDKQ-VC----GTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd13989    155 ----------------LDQGsLCtsfvGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
564-831 1.69e-21

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: 97.02  E-value: 1.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  564 LRRKPREsDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQAFVERDILTFAE--NPFVVSMYCSFE 641
Cdd:cd06646      3 LRRNPQH-DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIK-----LEPGDDFSLIQQEIFMVKEckHCNIVAYFGSYL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 TRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVG 721
Cdd:cd06646     77 SREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 LMSMTTNlyeghiekdarefldKQVCGTPEYIAPEVILRQ---GYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQV 798
Cdd:cd06646    157 TATIAKR---------------KSFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLM 221
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1988312908  799 ISDEINWPE-KDEAP-PPDAQDLITLLLRQNPLER 831
Cdd:cd06646    222 SKSNFQPPKlKDKTKwSSTFHNFVKISLTKNPKKR 256
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
577-786 2.61e-21

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: 96.27  E-value: 2.61e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKI--NKQNLILRNQIQQAFVERDILTFAENPFVVSMY-CSFETR-RHLCMVMEY 652
Cdd:cd06652      8 KLLGQGAFGRVYLCYDADTGRELAVKQVqfDPESPETSKEVNALECEIQLLKNLLHERIVQYYgCLRDPQeRTLSIFMEY 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmSMTTNLYEG 732
Cdd:cd06652     88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASK----RLQTICLSG 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  733 HIEkdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd06652    164 TGM--------KSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
577-843 3.04e-21

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: 96.63  E-value: 3.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIqqaFVERDILTFAE-NPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd14173      8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSRV---FREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS---MGHIKLTDFGL-SKVGLMSMTTNLye 731
Cdd:cd14173     85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHpnqVSPVKICDFDLgSGIKLNSDCSPI-- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekDAREFLDKqvCGTPEYIAPEVILRQG-----YGKPVDWWAMGIILYEFLVGCVPFFG--------DTPEE----- 793
Cdd:cd14173    163 -----STPELLTP--CGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGrcgsdcgwDRGEAcpacq 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  794 --LFGQVISDEINWPEKDEAP-PPDAQDLITLLLRQNPLERLgtgGAYEVKQH 843
Cdd:cd14173    236 nmLFESIQEGKYEFPEKDWAHiSCAAKDLISKLLVRDAKQRL---SAAQVLQH 285
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
573-831 3.35e-21

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: 95.45  E-value: 3.35e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKI---NKQNLILRNQIQQAfveRDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14050      3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSrsrFRGEKDRKRKLEEV---ERHEKLGEHPNCVRFIKAWEEKGILYIQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYveggdCATLMKN----MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsm 725
Cdd:cd14050     80 TEL-----CDTSLQQyceeTHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLV------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeghIEKDAREFLDKQVcGTPEYIAPEVIlrQG-YGKPVDWWAMGIILYEflVGC---VPFFGDTPEELFGQVISD 801
Cdd:cd14050    148 --------VELDKEDIHDAQE-GDPRYMAPELL--QGsFTKAADIFSLGITILE--LACnleLPSGGDGWHQLRQGYLPE 214
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  802 EINwpekdEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd14050    215 EFT-----AGLSPELRSIIKLMMDPDPERR 239
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
579-831 3.67e-21

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: 95.41  E-value: 3.67e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQnlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd14115      1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK----MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT---SMGHIKLTDFGLSkvglMSMTTNLYEGHIe 735
Cdd:cd14115     77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDA----VQISGHRHVHHL- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  736 kdarefldkqvCGTPEYIAPEVIlrqgYGKPV----DWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP-EKDE 810
Cdd:cd14115    152 -----------LGNPEFAAPEVI----QGTPVslatDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPdEYFG 216
                          250       260
                   ....*....|....*....|.
gi 1988312908  811 APPPDAQDLITLLLRQNPLER 831
Cdd:cd14115    217 DVSQAARDFINVILQEDPRRR 237
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
571-798 5.36e-21

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: 95.89  E-value: 5.36e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQiQQAFVERDILTFAEN-PFVVSMYCSFETRRHLCMV 649
Cdd:cd06616      6 EDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRI-RSTVDEKEQ-KRLLMDLDVVMRSSDcPYIVKFYGALFREGDCWIC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEggdcaTLMKNMGPLPVDMARMYFAE---------TVLALEYLHN-YGIVHRDLKPDNLLVTSMGHIKLTDFGLSk 719
Cdd:cd06616     84 MELMD-----ISLDKFYKYVYEVLDSVIPEeilgkiavaTVKALNYLKEeLKIIHRDVKPSNILLDRNGNIKLCDFGIS- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 vglmsmttnlyeGHIE------KDArefldkqvcGTPEYIAPEVIL----RQGYGKPVDWWAMGIILYEFLVGCVPFfgD 789
Cdd:cd06616    158 ------------GQLVdsiaktRDA---------GCRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPY--P 214

                   ....*....
gi 1988312908  790 TPEELFGQV 798
Cdd:cd06616    215 KWNSVFDQL 223
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
573-832 5.59e-21

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: 96.86  E-value: 5.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQnliLRNQI--QQAFveRDIL---TFAENPFVVSMYCSF--ETRRH 645
Cdd:cd07852      9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDA---FRNATdaQRTF--REIMflqELNDHPNIIKLLNVIraENDKD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNmgpLPVDMARMYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglms 724
Cdd:cd07852     84 IYLVFEYMETDLHAVIRAN---ILEDIHKQYIMYQLLkALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLAR----- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTTNLYEGHIEKDAREFLdkqvcGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGD-------------- 789
Cdd:cd07852    156 SLSQLEEDDENPVLTDYV-----ATRWYRAPEILLgSTRYTKGVDMWSVGCILGEMLLGKPLFPGTstlnqlekiievig 230
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  790 --TPEEL------FGQVISDEINWPEK---DEAPP---PDAQDLITLLLRQNPLERL 832
Cdd:cd07852    231 rpSAEDIesiqspFAATMLESLPPSRPkslDELFPkasPDALDLLKKLLVFNPNKRL 287
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
577-780 1.03e-20

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: 94.32  E-value: 1.03e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKI---------NKQNLILRNQIQqafverdILTFAENPFVVSMYCSFE--TRRH 645
Cdd:cd06653      8 KLLGRGAFGEVYLCYDADTGRELAVKQVpfdpdsqetSKEVNALECEIQ-------LLKNLRHDRIVQYYGCLRdpEEKK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK-VGLMS 724
Cdd:cd06653     81 LSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrIQTIC 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  725 MT-TNLyeghiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd06653    161 MSgTGI--------------KSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEML 203
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
571-787 1.26e-20

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: 95.83  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKI---NKQNLILRnqiqqAFVERDILTFAENPFVVSMY-----CSFET 642
Cdd:cd07849      5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIspfEHQTYCLR-----TLREIKILLRFKHENIIGILdiqrpPTFES 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  643 RRHLCMVMEYVEGgDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVgl 722
Cdd:cd07849     80 FKDVYIVQELMET-DLYKLIKTQ-HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARI-- 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  723 msmTTNlyeghiEKDAREFLDKQVcGTPEYIAPEVILRQ-GYGKPVDWWAMGIILYEFLVgCVPFF 787
Cdd:cd07849    156 ---ADP------EHDHTGFLTEYV-ATRWYRAPEIMLNSkGYTKAIDIWSVGCILAEMLS-NRPLF 210
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
571-812 1.45e-20

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: 95.13  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilrnqiqqafvERD-----------ILTFAENPFVVSMYcS 639
Cdd:cd07845      7 TEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN------------ERDgipisslreitLLLNLRHPNIVELK-E 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 FETRRHL---CMVMEYVEGgDCATLMKNM-GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDF 715
Cdd:cd07845     74 VVVGKHLdsiFLVMEYCEQ-DLASLLDNMpTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADF 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  716 GLSKVglmsmttnlyeghIEKDAREFLDKQVcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:cd07845    153 GLART-------------YGLPAKPMTPKVV--TLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQ 217
                          250       260
                   ....*....|....*....|....
gi 1988312908  795 FGQVI------SDEInWPEKDEAP 812
Cdd:cd07845    218 LDLIIqllgtpNESI-WPGFSDLP 240
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
572-846 1.92e-20

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: 94.21  E-value: 1.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLI-------LRN-QIQQAFVERDILTFAEnpFVVSmycsfETR 643
Cdd:cd07843      6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKegfpitsLREiNILLKLQHPNIVTVKE--VVVG-----SNL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGgDCATLMKNM-GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvgl 722
Cdd:cd07843     79 DKIYMVMEYVEH-DLKSLMETMkQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGL----- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttnlyeghiekdAREF---LDK--QVCGTPEYIAPEVILRQG-YGKPVDWWAMGIILYEFLVGCVPFFG----DTPE 792
Cdd:cd07843    153 ---------------AREYgspLKPytQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGkseiDQLN 217
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  793 ELFGQVIS-DEINWPEKDEAP---------PPDAQ---------------DLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07843    218 KIFKLLGTpTEKIWPGFSELPgakkktftkYPYNQlrkkfpalslsdngfDLLNRLLTYDPAKRI---SAEDALKHPYF 293
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
573-839 2.98e-20

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: 94.78  E-value: 2.98e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQ--RFAMKKINK--QNLILrnqIQQAFVERDILT-FAENPFVVSMY----CSFETR 643
Cdd:cd07857      2 YELIKELGQGAYGIVCSARNAETSEeeTVAIKKITNvfSKKIL---AKRALRELKLLRhFRGHKNITCLYdmdiVFPGNF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGgDCATLMKNMGPLpVDMARMYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvgl 722
Cdd:cd07857     79 NELYLYEELMEA-DLHQIIRSGQPL-TDAHFQSFIYQILcGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLAR--- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttNLYEGHIEKDarEFLDKQVcGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLvGCVPFF-------------- 787
Cdd:cd07857    154 -----GFSENPGENA--GFMTEYV-ATRWYRAPEIMLSfQSYTKAIDVWSVGCILAELL-GRKPVFkgkdyvdqlnqilq 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  788 --GDTPEELFGQVISDEI--------NWPEKD-----EAPPPDAQDLITLLLRQNPLERLGTGGAYE 839
Cdd:cd07857    225 vlGTPDEETLSRIGSPKAqnyirslpNIPKKPfesifPNANPLALDLLEKLLAFDPTKRISVEEALE 291
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
573-778 3.30e-20

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: 92.90  E-value: 3.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKIN---KQNlilRNQIQQAFVERDILTFAENPFVVSMYCSFeTRRHLC-M 648
Cdd:cd06607      3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSysgKQS---TEKWQDIIKEVKFLRQLRHPNTIEYKGCY-LREHTAwL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGlskvglmsmttn 728
Cdd:cd06607     79 VMEYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG------------ 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  729 lyEGHIEKDAREFLdkqvcGTPEYIAPEVILR--QG-YGKPVDWWAMGIILYE 778
Cdd:cd06607    147 --SASLVCPANSFV-----GTPYWMAPEVILAmdEGqYDGKVDVWSLGITCIE 192
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
577-846 5.01e-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: 92.34  E-value: 5.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRqRFAMKKInkqnliLRNQIQQAFVERDILTFA-ENPFVVSMYCSFETRRHLCMVME---- 651
Cdd:cd13982      7 KVLGYGSEGTIVFRGTFDGR-PVAVKRL------LPEFFDFADREVQLLRESdEHPNVIRYFCTEKDRQFLYIALElcaa 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 ----YVEGGDCATLMKNMGPLPVDMARmyfaETVLALEYLHNYGIVHRDLKPDNLLV---TSMGHIK--LTDFGLSKvGL 722
Cdd:cd13982     80 slqdLVESPRESKLFLRPGLEPVRLLR----QIASGLAHLHSLNIVHRDLKPQNILIstpNAHGNVRamISDFGLCK-KL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 MSMTTNLyeghiekdareFLDKQVCGTPEYIAPEVILRQGYGKP---VDWWAMGIILYEFLVGCVPFFGDTPEELfGQVI 799
Cdd:cd13982    155 DVGRSSF-----------SRRSGVAGTSGWIAPEMLSGSTKRRQtraVDIFSLGCVFYYVLSGGSHPFGDKLERE-ANIL 222
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908  800 SDEINWPE--KDEAPPPDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd13982    223 KGKYSLDKllSLGEHGPEAQDLIERMIDFDPEKR---PSAEEVLNHPFF 268
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
572-846 5.82e-20

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: 92.49  E-value: 5.82e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQiQQAFVERDI-LTFAENPFVVSMYCSF--ETRRHLCM 648
Cdd:cd06617      2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQEQ-KRLLMDLDIsMRSVDCPYTVTFYGALfrEGDVWICM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 -VME------YVEggdcaTLMKNMG-PLPVdMARMYFAeTVLALEYLH-NYGIVHRDLKPDNLLVTSMGHIKLTDFGLSk 719
Cdd:cd06617     80 eVMDtsldkfYKK-----VYDKGLTiPEDI-LGKIAVS-IVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFGIS- 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 vglmsmttnlyeGHIEKDAREFLDkqvCGTPEYIAPEVI----LRQGYGKPVDWWAMGIILYEFLVGCVPFFG-DTPEEL 794
Cdd:cd06617    152 ------------GYLVDSVAKTID---AGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYDSwKTPFQQ 216
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  795 FGQVIsdeinwpekdEAPPP---------DAQDLITLLLRQNPLERlgtgGAY-EVKQHRFF 846
Cdd:cd06617    217 LKQVV----------EEPSPqlpaekfspEFQDFVNKCLKKNYKER----PNYpELLQHPFF 264
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
559-847 7.80e-20

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: 93.18  E-value: 7.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  559 NASLKLRRKPRESdFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYC 638
Cdd:cd06633     10 IADLFYKDDPEEI-FVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  639 SFETRRHLCMVMEYVEGGDCATLMKNMGPL-PVDMARMYFAeTVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGl 717
Cdd:cd06633     89 CYLKDHTAWLVMEYCLGSASDLLEVHKKPLqEVEIAAITHG-ALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 skvglmsmttnlyEGHIEKDAREFLdkqvcGTPEYIAPEVILRQGYGK---PVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:cd06633    167 -------------SASIASPANSFV-----GTPYWMAPEVILAMDEGQydgKVDIWSLGITCIELAERKPPLFNMNAMSA 228
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  795 FGQVISDEINWPEKDEAPPPdAQDLITLLLRQNPLERLGTGgayEVKQHRFFR 847
Cdd:cd06633    229 LYHIAQNDSPTLQSNEWTDS-FRGFVDYCLQKIPQERPSSA---ELLRHDFVR 277
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
578-831 8.61e-20

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: 91.45  E-value: 8.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKESRQRFAMKKINkqnlilRNQIQQAFVERDILTF-------------AENPFVVSMYCSFETRR 644
Cdd:cd14101      7 LLGKGGFGTVYAGHRISDGLQVAIKQIS------RNRVQQWSKLPGVNPVpnevallqsvgggPGHRGVIRLLDWFEIPE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVE-GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV-TSMGHIKLTDFGLSKVGL 722
Cdd:cd14101     81 GFLLVLERPQhCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVdLRTGDIKLIDFGSGATLK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 MSMTTNLYeghiekdarefldkqvcGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDTpeelfgQVISD 801
Cdd:cd14101    161 DSMYTDFD-----------------GTRVYSPPEWILYHQYhALPATVWSLGILLYDMVCGDIPFERDT------DILKA 217
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  802 EINWPEKdeaPPPDAQDLITLLLRQNPLER 831
Cdd:cd14101    218 KPSFNKR---VSNDCRSLIRSCLAYNPSDR 244
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
569-825 1.13e-19

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: 92.80  E-value: 1.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQ-NLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd06649      3 KDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEiKPAIRNQIIR---ELQVLHECNSPYIVGFYGAFYSDGEIS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYL-HNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMT 726
Cdd:cd06649     80 ICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 TNLyeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFfgdtpeelfgqvisdeinwp 806
Cdd:cd06649    160 NSF-----------------VGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPI-------------------- 202
                          250
                   ....*....|....*....
gi 1988312908  807 ekdeaPPPDAQDLITLLLR 825
Cdd:cd06649    203 -----PPPDAKELEAIFGR 216
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
563-832 1.22e-19

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: 91.22  E-value: 1.22e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  563 KLRRKPRESDFetiklISNGAYGAVYFVRHKESRQRFAMKkinkqnLILRNQIQQAFVERDILTFAENpfVVSMYCSFET 642
Cdd:cd13995      1 KLTYRNIGSDF-----IPRGAFGKVYLAQDTKTKKRMACK------LIPVEQFKPSDVEIQACFRHEN--IAELYGALLW 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  643 RRHLCMVMEYVEGGDCATLMKNMGPLPvDMARMYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIkLTDFGLSkvg 721
Cdd:cd13995     68 EETVHLFMEAGEGGSVLEKLESCGPMR-EFEIIWVTKHVLkGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLS--- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lMSMTTNLYeghIEKDARefldkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIsd 801
Cdd:cd13995    143 -VQMTEDVY---VPKDLR--------GTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYL-- 208
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  802 einWPEKDEAPP---------PDAQDLITLLLRQNPLERL 832
Cdd:cd13995    209 ---YIIHKQAPPlediaqdcsPAMRELLEAALERNPNHRS 245
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
579-831 1.41e-19

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: 91.03  E-value: 1.41e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINkqnlilrnqiQQAFVERDILTFA--ENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd13991     14 IGRGSFGEVHRMEDKQTGFQCAVKKVR----------LEVFRAEELMACAglTSPRVVPLYGAVREGPWVNIFMDLKEGG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG-HIKLTDFGLSKvglmsmttNLYEGHIE 735
Cdd:cd13991     84 SLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHAE--------CLDPDGLG 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  736 KDAreFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEinwPEKDEAPP-- 813
Cdd:cd13991    156 KSL--FTGDYIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEP---PPLREIPPsc 230
                          250
                   ....*....|....*....
gi 1988312908  814 -PDAQDLITLLLRQNPLER 831
Cdd:cd13991    231 aPLTAQAIQAGLRKEPVHR 249
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
570-845 1.52e-19

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: 91.27  E-value: 1.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd06642      3 EELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEA--EDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNmGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNL 729
Cdd:cd06642     81 MEYLGGGSALDLLKP-GPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAG--------QL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 YEGHIEKDArefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKD 809
Cdd:cd06642    152 TDTQIKRNT-------FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQ 224
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  810 EAPPpdAQDLITLLLRQNPLERlgtGGAYEVKQHRF 845
Cdd:cd06642    225 HSKP--FKEFVEACLNKDPRFR---PTAKELLKHKF 255
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
573-831 1.80e-19

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 90.63  E-value: 1.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVY----FVRHKESRQRFAMKKINKQNlilRNQIQQAFV-ERDILTFAENPFVVSMY--CSFEtrRH 645
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYkgtlKGEGENTKIKVAVKTLKEGA---DEEEREDFLeEASIMKKLDHPNIVKLLgvCTQG--EP 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCAT-LMKNMGPLPVDMaRMYFAETV-LALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGlm 723
Cdd:pfam07714   76 LYIVTEYMPGGDLLDfLRKHKRKLTLKD-LLSMALQIaKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDI-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttnlyeghieKDAREFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFL-VGCVPFFGDTPEELFGQVISD 801
Cdd:pfam07714  153 ------------YDDDYYRKRGGGKLPiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDG 220
                          250       260       270
                   ....*....|....*....|....*....|
gi 1988312908  802 EInwPEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:pfam07714  221 YR--LPQPENCPDELYDLMKQCWAYDPEDR 248
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
587-846 1.85e-19

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


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 90.68  E-value: 1.85e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  587 VYFVRHKESRQRFAMKKINKQNLILRNQiqQAFVERDIltfaenPFVVSMYCSFETRRHLCMVMEYVEGG---------- 656
Cdd:cd05576     15 VLLVMDTRTQETFILKGLRKSSEYSRER--KTIIPRCV------PNMVCLRKYIISEESVFLVLQHAEGGklwsylskfl 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 ------------DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFG-LSKVglm 723
Cdd:cd05576     87 ndkeihqlfadlDERLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWSEV--- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttnlyEGHIEKDAREFLdkqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVG-----CVPFFGDTPEELfgqv 798
Cdd:cd05576    164 -------EDSCDSDAIENM---------YCAPEVGGISEETEACDWWSLGALLFELLTGkalveCHPAGINTHTTL---- 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988312908  799 isdeiNWPEKDEAPppdAQDLITLLLRQNPLERLGTGGA--YEVKQHRFF 846
Cdd:cd05576    224 -----NIPEWVSEE---ARSLLQQLLQFNPTERLGAGVAgvEDIKSHPFF 265
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
571-843 2.38e-19

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: 90.70  E-value: 2.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLIL-RNQIQQafvERDILTFAENPFVVSMYCSFETRR----- 644
Cdd:cd14048      6 TDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELaREKVLR---EVRALAKLDHPGIVRYFNAWLERPpegwq 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 ------HLCMVMEYVEGGDCATLM---KNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDF 715
Cdd:cd14048     83 ekmdevYLYIQMQLCRKENLKDWMnrrCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  716 GLskvglmsmTTNLYEGHIEKDAREFLD------KQVcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGcvpfFGD 789
Cdd:cd14048    163 GL--------VTAMDQGEPEQTVLTPMPayakhtGQV-GTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYS----FST 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  790 TPEELfgQVISD--EINWPEKDEAPPPDAQDLITLLLRQNPLERlgtGGAYEVKQH 843
Cdd:cd14048    230 QMERI--RTLTDvrKLKFPALFTNKYPEERDMVQQMLSPSPSER---PEAHEVIEH 280
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
641-832 2.94e-19

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: 90.60  E-value: 2.94e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 ETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGL 717
Cdd:cd14171     79 SPRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGF 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SKVGLMSMTTNLYeghiekdarefldkqvcgTPEYIAPEVILRQ-----------------GYGKPVDWWAMGIILYEFL 780
Cdd:cd14171    159 AKVDQGDLMTPQF------------------TPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIML 220
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  781 VGCVPFFGDTP-----EELFGQVISDEINWPEKD-EAPPPDAQDLITLLLRQNPLERL 832
Cdd:cd14171    221 CGYPPFYSEHPsrtitKDMKRKIMTGSYEFPEEEwSQISEMAKDIVRKLLCVDPEERM 278
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
579-846 2.94e-19

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: 90.85  E-value: 2.94e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQQA--FVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd06657     28 IGEGSTGIVCIATVKSSGKLVAVKKMD-----LRKQQRREllFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGG 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAeTVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglmsmttnlyeGHIEK 736
Cdd:cd06657    103 ALTDIVTHTRMNEEQIAAVCLA-VLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFC-------------AQVSK 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 DAREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVisdeinwpeKDEAPP--- 813
Cdd:cd06657    169 EVPR--RKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMI---------RDNLPPklk 237
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1988312908  814 ------PDAQDLITLLLRQNPLERlgtGGAYEVKQHRFF 846
Cdd:cd06657    238 nlhkvsPSLKGFLDRLLVRDPAQR---ATAAELLKHPFL 273
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
571-789 3.62e-19

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: 89.58  E-value: 3.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETI-KLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilrNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14108      1 TDYYDIhKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRA----KKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMaRMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG--HIKLTDFGlskvGLMSMTT 727
Cdd:cd14108     77 TELCHEELLERITKRPTVCESEV-RSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFG----NAQELTP 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  728 NlyeghiekdareflDKQVC--GTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD 789
Cdd:cd14108    152 N--------------EPQYCkyGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGE 201
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
576-806 4.54e-19

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: 90.07  E-value: 4.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKL--ISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd07871      8 VKLdkLGEGTYATVFKGRSKLTENLVALKEIRLEHE--EGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGgDCATLMKNMGPL-PVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLYEG 732
Cdd:cd07871     86 DS-DLKQYLDNCGNLmSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA--KSVPTKTYSN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HIEkdarefldkqvcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE-------LFGQVISDeiN 804
Cdd:cd07871    163 EVV-------------TLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEelhlifrLLGTPTEE--T 227

                   ..
gi 1988312908  805 WP 806
Cdd:cd07871    228 WP 229
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
518-832 4.88e-19

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 92.79  E-value: 4.88e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  518 PRYIISQLGLNKDPLEEMAHLGNYDSGTAEtpETDESVSSsnaslKLRRKPRESdFETIKLISNGAYGAVYFVRHKESRQ 597
Cdd:PTZ00036    21 NKGGSGKFEMNDKKLDEEERSHNNNAGEDE--DEEKMIDN-----DINRSPNKS-YKLGNIIGNGSFGVVYEAICIDTSE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  598 RFAMKKI-------NKQNLILRNqiqqafVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEggdcATLMKNMG---- 666
Cdd:PTZ00036    93 KVAIKKVlqdpqykNRELLIMKN------LNHINIIFLKDYYYTECFKKNEKNIFLNVVMEFIP----QTVHKYMKhyar 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  667 ---PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH-IKLTDFGLSKvglmsmttNLYEGHiekdaREFl 742
Cdd:PTZ00036   163 nnhALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAK--------NLLAGQ-----RSV- 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  743 dKQVCgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS-----------------DEIN 804
Cdd:PTZ00036   229 -SYIC-SRFYRAPELMLgATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQvlgtptedqlkemnpnyADIK 306
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1988312908  805 WPE---KD------EAPPPDAQDLITLLLRQNPLERL 832
Cdd:PTZ00036   307 FPDvkpKDlkkvfpKGTPDDAINFISQFLKYEPLKRL 343
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
582-831 6.91e-19

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: 88.65  E-value: 6.91e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKEsrQRFAMKKINKQnlilrnQIQQAF-VERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCAT 660
Cdd:cd14058      4 GSFGVVCKARWRN--QIVAVKIIESE------SEKKAFeVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  661 LMKNMGPLPVdmarmYFAETVL--------ALEYLHNYG---IVHRDLKPDNLLVTSMGH-IKLTDFGLSKVGLMSMTTN 728
Cdd:cd14058     76 VLHGKEPKPI-----YTAAHAMswalqcakGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGTACDISTHMTNN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 LyeghiekdarefldkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG-DTPEELFGQVISDEINWPE 807
Cdd:cd14058    151 K------------------GSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHiGGPAFRIMWAVHNGERPPL 212
                          250       260
                   ....*....|....*....|....
gi 1988312908  808 KDEAPPPdAQDLITLLLRQNPLER 831
Cdd:cd14058    213 IKNCPKP-IESLMTRCWSKDPEKR 235
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
573-849 7.54e-19

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: 90.82  E-value: 7.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLIlrnQIQQAFVERDILTFAENPFVVSM---YC---SFETRR 644
Cdd:cd07851     17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfQSAI---HAKRTYRELRLLKHMKHENVIGLldvFTpasSLEDFQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVeGGDCATLMKnMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMS 724
Cdd:cd07851     94 DVYLVTHLM-GADLNNIVK-CQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTtnlyeGHIekdarefldkqvcGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGD-------------- 789
Cdd:cd07851    172 MT-----GYV-------------ATRWYRAPEIMLnWMHYNQTVDIWSVGCIMAELLTGKTLFPGSdhidqlkrimnlvg 233
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  790 TPEELFGQVISDEI--NW-------PEKD-----EAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSL 849
Cdd:cd07851    234 TPDEELLKKISSESarNYiqslpqmPKKDfkevfSGANPLAIDLLEKMLVLDPDKRI---TAAEALAHPYLAEY 304
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
573-846 7.72e-19

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: 89.46  E-value: 7.72e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd07836      2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAE--EGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGgDCATLMK---NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTnl 729
Cdd:cd07836     80 MDK-DLKKYMDthgVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNT-- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 yeghiekdareFLDKQVcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS-----DEI 803
Cdd:cd07836    157 -----------FSNEVV--TLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRimgtpTES 223
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  804 NWPEKDEAP---------------------PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07836    224 TWPGISQLPeykptfpryppqdlqqlfphaDPLGIDLLHRLLQLNPELRI---SAHDALQHPWF 284
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
572-795 9.18e-19

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 89.02  E-value: 9.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnliLRNQIQ----QAFVERDILTFAENPFVVSMYCSFETRRHLC 647
Cdd:cd07861      1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIR-----LESEEEgvpsTAIREISLLKELQHPNIVCLEDVLMQENRLY 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEggdcATLMKNMGPLPVD------MARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVg 721
Cdd:cd07861     76 LVFEFLS----MDLKKYLDSLPKGkymdaeLVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARA- 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  722 lMSMTTNLYEGHIEkdarefldkqvcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP-EELF 795
Cdd:cd07861    151 -FGIPVRVYTHEVV-------------TLWYRAPEVLLgSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEiDQLF 212
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
570-785 9.69e-19

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: 88.98  E-value: 9.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd06641      3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEA--EDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNmGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNL 729
Cdd:cd06641     81 MEYLGGGSALDLLEP-GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAG--------QL 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  730 YEGHIEKDarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVP 785
Cdd:cd06641    152 TDTQIKRN-------*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
570-785 1.33e-18

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: 88.57  E-value: 1.33e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd06640      3 EELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEA--EDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKnMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNL 729
Cdd:cd06640     81 MEYLGGGSALDLLR-AGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAG--------QL 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  730 YEGHIEKDArefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVP 785
Cdd:cd06640    152 TDTQIKRNT-------FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
568-786 1.96e-18

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: 88.14  E-value: 1.96e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESD-FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLIlRNQIQqafVERDIL-TFAENPFVVSMYCSF----- 640
Cdd:cd06638     14 PDPSDtWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDI-DEEIE---AEYNILkALSDHPNVVKFYGMYykkdv 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 ETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFA----ETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFG 716
Cdd:cd06638     90 KNGDQLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAyilhEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFG 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  717 LSkvglmsmtTNLYEGHIEKDARefldkqvCGTPEYIAPEVI-----LRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd06638    170 VS--------AQLTSTRLRRNTS-------VGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPL 229
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
582-786 2.17e-18

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: 88.70  E-value: 2.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAfvERDILTFAENPFVVSMYCSFE--TRRHLCMVMEYVEGGDCA 659
Cdd:cd13988      4 GATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQMR--EFEVLKKLNHKNIVKLFAIEEelTTRHKVLVMELCPCGSLY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  660 TLMK---NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLvTSMGH-----IKLTDFGLskvglmsmttnlye 731
Cdd:cd13988     82 TVLEepsNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIM-RVIGEdgqsvYKLTDFGA-------------- 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  732 ghiekdAREFLDKQ----VCGTPEYIAPEV----ILRQG----YGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd13988    147 ------ARELEDDEqfvsLYGTEEYLHPDMyeraVLRKDhqkkYGATVDLWSIGVTFYHAATGSLPF 207
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
575-832 4.01e-18

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: 87.78  E-value: 4.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  575 TIKLISNGAYGAVYFVRHKESRQRFAMKKIN-----KQNLILRNQIQQAFVERDILTFAENpfvvsmycSFETRRHLCMV 649
Cdd:cd14170      6 TSQVLGLGINGKVLQIFNKRTQEKFALKMLQdcpkaRREVELHWRASQCPHIVRIVDVYEN--------LYAGRKCLLIV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMG--PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM---GHIKLTDFGLSKvglms 724
Cdd:cd14170     78 MECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAK----- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghiEKDAREFLDKQvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFF---------GDTPEELF 795
Cdd:cd14170    153 ----------ETTSHNSLTTP-CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYsnhglaispGMKTRIRM 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  796 GQVISDEINWPEKDEapppDAQDLITLLLRQNPLERL 832
Cdd:cd14170    222 GQYEFPNPEWSEVSE----EVKMLIRNLLKTEPTQRM 254
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
577-786 4.81e-18

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: 86.67  E-value: 4.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKI--NKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETR--RHLCMVMEY 652
Cdd:cd06651     13 KLLGQGAFGRVYLCYDVDTGRELAAKQVqfDPESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFMEY 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmSMTTNLYEG 732
Cdd:cd06651     93 MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK----RLQTICMSG 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  733 HIEkdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd06651    169 TGI--------RSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
579-786 5.00e-18

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: 87.62  E-value: 5.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQnlilrnqiQQAFVERDILTF---AENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd14180     14 LGEGSFSVCRKCRHRQSGQEYAVKIISRR--------MEANTQREVAALrlcQSHPNIVALHEVLHDQYHTYLVMELLRG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSKV---GLMSMTTNl 729
Cdd:cd14180     86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLrpqGSRPLQTP- 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  730 yeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14180    165 -----------------CFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPF 204
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
582-831 8.18e-18

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: 86.01  E-value: 8.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKeSRQRFAMKKINKQNLilRNQIQQAFVER-DILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCAT 660
Cdd:cd14027      4 GGFGKVSLCFHR-TQGLVVLKTVYTGPN--CIEHNEALLEEgKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  661 LMKNMgPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNlyEGHIEKDARE 740
Cdd:cd14027     81 VLKKV-SVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTK--EEHNEQREVD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  741 FLDKQVCGTPEYIAPEViLRQGYGKPV---DWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEiNWPEKDEAP---PP 814
Cdd:cd14027    158 GTAKKNAGTLYYMAPEH-LNDVNAKPTeksDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSG-NRPDVDDITeycPR 235
                          250
                   ....*....|....*..
gi 1988312908  815 DAQDLITLLLRQNPLER 831
Cdd:cd14027    236 EIIDLMKLCWEANPEAR 252
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
579-780 8.34e-18

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: 85.78  E-value: 8.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKqnliLRNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGD 657
Cdd:cd14221      1 LGKGCFGQAIKVTHRETGEVMVMKELIR----FDEETQRTFLkEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLMKNMGPLPVDMARMYFAETVLA-LEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvgLMSMTTNLYEGHIE- 735
Cdd:cd14221     77 LRGIIKSMDSHYPWSQRVSFAKDIASgMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLAR--LMVDEKTQPEGLRSl 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1988312908  736 --KDAREflDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd14221    155 kkPDRKK--RYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
562-791 9.62e-18

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: 86.20  E-value: 9.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  562 LKLRRKPRESD-FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlILRNQIQqafVERDILTFAEN-PFVVSMYCS 639
Cdd:cd06639     12 LGLESLADPSDtWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPIS-DVDEEIE---AEYNILRSLPNhPNVVKFYGM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 FETRRH-----LCMVMEYVEGGDCATLMKNM----GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHI 710
Cdd:cd06639     88 FYKADQyvggqLWLVLELCNGGSVTELVKGLlkcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGV 167
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  711 KLTDFGLSkvglmsmtTNLYEGHIEKDARefldkqvCGTPEYIAPEVILRQ-----GYGKPVDWWAMGIILYEFLVGCVP 785
Cdd:cd06639    168 KLVDFGVS--------AQLTSARLRRNTS-------VGTPFWMAPEVIACEqqydySYDARCDVWSLGITAIELADGDPP 232

                   ....*.
gi 1988312908  786 FFGDTP 791
Cdd:cd06639    233 LFDMHP 238
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
586-790 1.12e-17

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: 86.51  E-value: 1.12e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  586 AVYFVRHKESRQRFAMKKInkqnlilrnQIQQAFVERDiltfAENPF-VVSMYCSFETRRHLCMVMEYVEGgDCATLMKN 664
Cdd:cd14135     30 AIKIIRNNELMHKAGLKEL---------EILKKLNDAD----PDDKKhCIRLLRHFEHKNHLCLVFESLSM-NLREVLKK 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  665 MGP---LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIKLTDFGLSkvglmsmttnlyeGHIEKDARe 740
Cdd:cd14135     96 YGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNeKKNTLKLCDFGSA-------------SDIGENEI- 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  741 fldkqvcgTPE-----YIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDT 790
Cdd:cd14135    162 --------TPYlvsrfYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKT 208
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
576-849 1.20e-17

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: 86.21  E-value: 1.20e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKL--ISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd07873      5 IKLdkLGEGTYATVYKGRSKLTDNLVALKEIRLEHE--EGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGgDCATLMKNMGPLpVDM--ARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLYE 731
Cdd:cd07873     83 DK-DLKQYLDDCGNS-INMhnVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA--KSIPTKTYS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 GHIEkdarefldkqvcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE-------LFGQ------ 797
Cdd:cd07873    159 NEVV-------------TLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEqlhfifrILGTpteetw 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  798 --VISDE----INWPE------KDEAP--PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRSL 849
Cdd:cd07873    226 pgILSNEefksYNYPKyradalHNHAPrlDSDGADLLSKLLQFEGRKRI---SAEEAMKHPYFHSL 288
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
569-807 1.85e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 89.80  E-value: 1.85e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSF--ETRRHL 646
Cdd:PTZ00266    11 RLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREK-SQLVIEVNVMRELKHKNIVRYIDRFlnKANQKL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCA----TLMKNMGPLP----VDMARmyfaETVLALEYLHNYG-------IVHRDLKPDNL-LVTSMGHI 710
Cdd:PTZ00266    90 YILMEFCDAGDLSrniqKCYKMFGKIEehaiVDITR----QLLHALAYCHNLKdgpngerVLHRDLKPQNIfLSTGIRHI 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  711 ----------------KLTDFGLSK-VGLMSMTtnlyeghiekdarefldKQVCGTPEYIAPEVILRQ--GYGKPVDWWA 771
Cdd:PTZ00266   166 gkitaqannlngrpiaKIGDFGLSKnIGIESMA-----------------HSCVGTPYYWSPELLLHEtkSYDDKSDMWA 228
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1988312908  772 MGIILYEFLVGCVPFFGDTPeelFGQVISDEINWPE 807
Cdd:PTZ00266   229 LGCIIYELCSGKTPFHKANN---FSQLISELKRGPD 261
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
573-789 2.25e-17

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: 86.31  E-value: 2.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLilrNQIQQAFVERDILTFAENPFVVSMYCSF------ETRR 644
Cdd:cd07850      2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSRpfQNV---THAKRAYRELVLMKLVNHKNIIGLLNVFtpqkslEEFQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGDCATLMknmgpLPVDMARM-YFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGL 722
Cdd:cd07850     79 DVYLVMELMDANLCQVIQ-----MDLDHERMsYLLYQMLcGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  723 MSMTTNLYeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD 789
Cdd:cd07850    154 TSFMMTPY----------------VVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGT 204
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
572-834 2.25e-17

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: 84.74  E-value: 2.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKL---ISNGAYGAVYFVRHKEsrQRFAMKKINKQ--NLILRNQIQQafvERDILTFA-ENPFVVSMYCSFETRRH 645
Cdd:cd13979      1 DWEPLRLqepLGSGGFGSVYKATYKG--ETVAVKIVRRRrkNRASRQSFWA---ELNAARLRhENIVRVLAAETGTDFAS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMV-MEYVEGGdcaTLMKNM----GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS-K 719
Cdd:cd13979     76 LGLIiMEYCGNG---TLQQLIyegsEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSvK 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 VGlmsmttnlyeghiEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd13979    153 LG-------------EGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVA 219
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1988312908  800 SD--EINWPEKDEAPPPDAQDLITLLLRQNPLERLGT 834
Cdd:cd13979    220 KDlrPDLSGLEDSEFGQRLRSLISRCWSAQPAERPNA 256
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
569-849 2.33e-17

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: 85.51  E-value: 2.33e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCM 648
Cdd:cd07869      3 KADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEE--EGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTN 728
Cdd:cd07869     81 VFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARA--KSVPSH 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 LYEGHIEkdarefldkqvcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFG-----DTPEELFGQV-ISD 801
Cdd:cd07869    159 TYSNEVV-------------TLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmkdiqDQLERIFLVLgTPN 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  802 EINWPEKDEAP--PPD----------------------AQDLITLLLRQNPLERLGTGGAYevkQHRFFRSL 849
Cdd:cd07869    226 EDTWPGVHSLPhfKPErftlyspknlrqawnklsyvnhAEDLASKLLQCFPKNRLSAQAAL---SHEYFSDL 294
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
571-831 2.96e-17

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: 84.87  E-value: 2.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNqIQQAFVERDILTFAENPFVVSMYCSFETRRHLcmvM 650
Cdd:cd14049      6 NEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRD-CMKVLREVKVLAGLQHPNIVGYHTAWMEHVQL---M 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDC------------------ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIK 711
Cdd:cd14049     82 LYIQMQLCelslwdwivernkrpceeEFKSAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVR 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  712 LTDFGLSKVGLMSMTTNLYEghiEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLvgcVPFFGDTP 791
Cdd:cd14049    162 IGDFGLACPDILQDGNDSTT---MSRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPFGTEME 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1988312908  792 E-ELFGQVISDEInwPEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd14049    236 RaEVLTQLRNGQI--PKSLCKRWPVQAKYIKLLTSTEPSER 274
pknD PRK13184
serine/threonine-protein kinase PknD;
573-786 4.16e-17

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 88.67  E-value: 4.16e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK---QNLILRNQ-IQQAFVERDILtfaeNPFVVSMYCSFETRRHLCM 648
Cdd:PRK13184     4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREdlsENPLLKKRfLREAKIAADLI----HPGIVPVYSICSDGDPVYY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNM---GPLPVDMARMYFAETVLAL--------EYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGL 717
Cdd:PRK13184    80 TMPYIEGYTLKSLLKSVwqkESLSKELAEKTSVGAFLSIfhkicatiEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SKVGLMsmttnlyeghiEKDAREFLD--------------KQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGC 783
Cdd:PRK13184   160 AIFKKL-----------EEEDLLDIDvdernicyssmtipGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLS 228

                   ...
gi 1988312908  784 VPF 786
Cdd:PRK13184   229 FPY 231
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
573-846 4.25e-17

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: 84.41  E-value: 4.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDILTFAE--NPFVVSMYCSFETRRHLCMVM 650
Cdd:cd07839      2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDD---DDEGVPSSALREICLLKElkHKNIVRLYDVLHSDKKLTLVF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYveggdCATLMKNM-----GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglmsm 725
Cdd:cd07839     79 EY-----CDQDLKKYfdscnGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGL-------- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 ttnlyeghiekdAREFLDKQVCGTPE-----YIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFF-----GDTPEEL 794
Cdd:cd07839    146 ------------ARAFGIPVRCYSAEvvtlwYRPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPLFpgndvDDQLKRI 213
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  795 FGQVIS-DEINWPEKDEAPP---------------------PDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07839    214 FRLLGTpTEESWPGVSKLPDykpypmypattslvnvvpklnSTGRDLLQNLLVCNPVQRI---SAEEALQHPYF 284
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
578-831 4.53e-17

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: 83.82  E-value: 4.53e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKEsrQRFAMKKINKQNLILR-NQIQQAFVERDILTFAenpfvVSMYCSFE-------TRRH---- 645
Cdd:cd14000      1 LLGDGGFGSVYRASYKG--EPVAVKIFNKHTSSNFaNVPADTMLRHLRATDA-----MKNFRLLRqeltvlsHLHHpsiv 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 ---------LCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVL----ALEYLHNYGIVHRDLKPDNLLVTSMG---- 708
Cdd:cd14000     74 yllgigihpLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNVLVWTLYpnsa 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  709 -HIKLTDFGLSKvglmsmttnlyeghieKDAREFLdKQVCGTPEYIAPEVILRQG-YGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14000    154 iIIKIADYGISR----------------QCCRMGA-KGSEGTPGFRAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPM 216
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908  787 FG--DTPEELfgqVISDEINWP--EKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd14000    217 VGhlKFPNEF---DIHGGLRPPlkQYECAPWPEVEVLMKKCWKENPQQR 262
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
579-826 5.06e-17

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: 82.93  E-value: 5.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYfvRHKESRQRFAMKKINKQNlilrnqiqqafvERDI--LTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd14059      1 LGSGAQGAVF--LGKFRGEEVAVKKVRDEK------------ETDIkhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYG 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyeghiek 736
Cdd:cd14059     67 QLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSK----------------- 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  737 darEFLDKQV----CGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG-DTPEELFGqVISDEINWPEKDEA 811
Cdd:cd14059    130 ---ELSEKSTkmsfAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDvDSSAIIWG-VGSNSLQLPVPSTC 205
                          250
                   ....*....|....*
gi 1988312908  812 PppdaqDLITLLLRQ 826
Cdd:cd14059    206 P-----DGFKLLMKQ 215
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
612-846 5.29e-17

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 83.43  E-value: 5.29e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  612 RNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVM--EYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLH- 688
Cdd:cd13983     41 KAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHt 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  689 -NYGIVHRDLKPDNLLVT-SMGHIKLTDFGLSKVGLMSMTtnlyeghiekdarefldKQVCGTPEYIAPEvILRQGYGKP 766
Cdd:cd13983    121 rDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQSFA-----------------KSVIGTPEFMAPE-MYEEHYDEK 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  767 VDWWAMGIILYEFLVGCVPFFG-DTPEELFGQVISDEInwPEKDEA-PPPDAQDLITLLLRQnPLERLgtgGAYEVKQHR 844
Cdd:cd13983    183 VDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTSGIK--PESLSKvKDPELKDFIEKCLKP-PDERP---SARELLEHP 256

                   ..
gi 1988312908  845 FF 846
Cdd:cd13983    257 FF 258
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
573-788 8.66e-17

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: 84.57  E-value: 8.66e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLILrnqIQQAFVERDILTFAENPFVVSMY------CSFETRR 644
Cdd:cd07879     17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSRpfQSEIF---AKRAYRELTLLKHMQHENVIGLLdvftsaVSGDEFQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEggdcATLMKNMG-PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLM 723
Cdd:cd07879     94 DFYLVMPYMQ----TDLQKIMGhPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADA 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  724 SMTtnlyeGHIEkdarefldkqvcgTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFG 788
Cdd:cd07879    170 EMT-----GYVV-------------TRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKG 217
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
576-846 9.35e-17

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: 83.47  E-value: 9.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKI--NKQNLILRNQIQQAfverDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd07870      5 LEKLGEGSYATVYKGISRINGQLVALKVIsmKTEEGVPFTAIREA----SLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLYEGH 733
Cdd:cd07870     81 HTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARA--KSIPSQTYSSE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEkdarefldkqvcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFG--DTPEEL--FGQVIS--DEINWP 806
Cdd:cd07870    159 VV-------------TLWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFPGvsDVFEQLekIWTVLGvpTEDTWP 225
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  807 EKDEAP------------------------PPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07870    226 GVSKLPnykpewflpckpqqlrvvwkrlsrPPKAEDLASQMLMMFPKDRI---SAQDALLHPYF 286
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
579-780 9.35e-17

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: 82.94  E-value: 9.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNlilrNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGD 657
Cdd:cd14154      1 LGKGFFGQAIKVTHRETGEVMVMKELIRFD----EEAQRNFLkEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLMKNMG-PLPVdMARMYFAETVLA-LEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV--------GLMSMTT 727
Cdd:cd14154     77 LKDVLKDMArPLPW-AQRVRFAKDIASgMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLiveerlpsGNMSPSE 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  728 NLYegHIEKDARefldKQ---VCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd14154    156 TLR--HLKSPDR----KKrytVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
560-787 1.24e-16

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: 83.56  E-value: 1.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  560 ASLKLRRKPrESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSmYCS 639
Cdd:cd06635     15 AELFFKEDP-EKLFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIE-YKG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 FETRRHLC-MVMEYVEGGDCATLMKNMGPL-PVDMARMYFAeTVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGl 717
Cdd:cd06635     93 CYLREHTAwLVMEYCLGSASDLLEVHKKPLqEIEIAAITHG-ALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG- 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  718 skvglmsmttnlyEGHIEKDAREFLdkqvcGTPEYIAPEVILRQGYGK---PVDWWAMGIILYEFLVGCVPFF 787
Cdd:cd06635    171 -------------SASIASPANSFV-----GTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLF 225
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
571-846 1.37e-16

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: 83.19  E-value: 1.37e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKInkqnliLRNQIQQAFV-----ERDILTFAENPFVVSMY--CSFET- 642
Cdd:cd07865     12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKV------LMENEKEGFPitalrEIKILQLLKHENVVNLIeiCRTKAt 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  643 -----RRHLCMVMEYVEGgDCATLMKNMG---PLPV--DMARMYFAetvlALEYLHNYGIVHRDLKPDNLLVTSMGHIKL 712
Cdd:cd07865     86 pynryKGSIYLVFEFCEH-DLAGLLSNKNvkfTLSEikKVMKMLLN----GLYYIHRNKILHRDMKAANILITKDGVLKL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  713 TDFGLSKVglMSMTTNlyeghieKDAREFLDKQVcgTPEYIAPEVIL--RQgYGKPVDWWAMGIILYEFLVGCVPFFGDT 790
Cdd:cd07865    161 ADFGLARA--FSLAKN-------SQPNRYTNRVV--TLWYRPPELLLgeRD-YGPPIDMWGAGCIMAEMWTRSPIMQGNT 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  791 PEE---LFGQV---ISDEInWP--------EKDEAPP----------------PDAQDLITLLLRQNPLERLgtgGAYEV 840
Cdd:cd07865    229 EQHqltLISQLcgsITPEV-WPgvdklelfKKMELPQgqkrkvkerlkpyvkdPYALDLIDKLLVLDPAKRI---DADTA 304

                   ....*.
gi 1988312908  841 KQHRFF 846
Cdd:cd07865    305 LNHDFF 310
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
571-846 1.47e-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: 83.67  E-value: 1.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnLILRNQIQQAFVERDILTFAENPFVVSMY------------- 637
Cdd:cd07854      5 SRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIV---LTDPQSVKHALREIKIIRRLDHDNIVKVYevlgpsgsdlted 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  638 -CSFETRRHLCMVMEYVEGgDCATLMkNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV-TSMGHIKLTDF 715
Cdd:cd07854     82 vGSLTELNSVYIVQEYMET-DLANVL-EQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFInTEDLVLKIGDF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  716 GLSKV--------GLMSMTTNlyeghiekdarefldkqvcgTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd07854    160 GLARIvdphyshkGYLSEGLV--------------------TKWYRSPRLLLSpNNYTKAIDMWAAGCIFAEMLTGKPLF 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  787 FGDTPEELFgQVISDEI----------------------NW----PEKDEAP--PPDAQDLITLLLRQNPLERLgtgGAY 838
Cdd:cd07854    220 AGAHELEQM-QLILESVpvvreedrnellnvipsfvrndGGeprrPLRDLLPgvNPEALDFLEQILTFNPMDRL---TAE 295

                   ....*...
gi 1988312908  839 EVKQHRFF 846
Cdd:cd07854    296 EALMHPYM 303
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
573-829 1.49e-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: 83.95  E-value: 1.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLIlrnQIQQAFVERDILTFAENPFVVSMY------CSFETRR 644
Cdd:cd07878     17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRpfQSLI---HARRTYRELRLLKHMKHENVIGLLdvftpaTSIENFN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVeGGDCATLMKnMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMS 724
Cdd:cd07878     94 EVYLVTNLM-GADLNNIVK-CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTtnlyeGHIekdarefldkqvcGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGD-------------- 789
Cdd:cd07878    172 MT-----GYV-------------ATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNdyidqlkrimevvg 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  790 TPEELFGQVISDEINWPEKDEAPPPDAQDLITLLLRQNPL 829
Cdd:cd07878    234 TPSPEVLKKISSEHARKYIQSLPHMPQQDLKKIFRGANPL 273
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
572-843 1.77e-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: 84.03  E-value: 1.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLIlrnQIQQAFVERDILTFAENPFVVSMYCSFETR-----R 644
Cdd:cd07853      1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMPNvfQNLV---SCKRVFRELKMLCFFKHDNVLSALDILQPPhidpfE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGgDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGlms 724
Cdd:cd07853     78 EIYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVE--- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghiEKDAREFLDKQVCgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFfgdtpeelfgqvisdei 803
Cdd:cd07853    154 ----------EPDESKHMTQEVV-TQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILF----------------- 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1988312908  804 nwpekdEAPPPDAQ-DLITLLLRQNPLERLGTGGAyEVKQH 843
Cdd:cd07853    206 ------QAQSPIQQlDLITDLLGTPSLEAMRSACE-GARAH 239
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
641-846 1.86e-16

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: 81.24  E-value: 1.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 ETRRHLCMVMEYvegGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLvtsmghikLTDFGLSKV 720
Cdd:cd14022     57 ETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFV--------FKDEERTRV 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  721 GLMSMT-TNLYEGHIEkdarEFLDKQVCgtPEYIAPEVILRQGY--GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQ 797
Cdd:cd14022    126 KLESLEdAYILRGHDD----SLSDKHGC--PAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSK 199
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908  798 VISDEINWPekdEAPPPDAQDLITLLLRQNPLERLGTggaYEVKQHRFF 846
Cdd:cd14022    200 IRRGQFNIP---ETLSPKAKCLIRSILRREPSERLTS---QEILDHPWF 242
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
570-817 2.21e-16

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: 82.01  E-value: 2.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKL---ISNGAYGAVYfvRHKESRQRFAMKKINKQ-NLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRH 645
Cdd:cd14145      2 EIDFSELVLeeiIGIGGFGKVY--RAIWIGDEVAVKAARHDpDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIV---HRDLKPDNLLVTSMGH--------IKLTD 714
Cdd:cd14145     80 LCLVMEFARGGPLNRVLSGK-RIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKVEngdlsnkiLKITD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  715 FGLSKVglMSMTTNLyeghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG-DTPEE 793
Cdd:cd14145    159 FGLARE--WHRTTKM---------------SAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGiDGLAV 221
                          250       260
                   ....*....|....*....|....
gi 1988312908  794 LFGqVISDEINWPEKDEAPPPDAQ 817
Cdd:cd14145    222 AYG-VAMNKLSLPIPSTCPEPFAR 244
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
633-782 2.90e-16

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: 82.62  E-value: 2.90e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  633 VVSMYCSFETR----RHLCMVMEyVEGGDCATLMKNMGP--LPVDMARMYFAETVLALEYLHNY-GIVHRDLKPDNLLVT 705
Cdd:cd14136     76 VVQLLDDFKHTgpngTHVCMVFE-VLGPNLLKLIKRYNYrgIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLC 154
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  706 -SMGHIKLTDFGlskvglmsmTTNLYEGHIEKDARefldkqvcgTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVG 782
Cdd:cd14136    155 iSKIEVKIADLG---------NACWTDKHFTEDIQ---------TRQYRSPEVILGAGYGTPADIWSTACMAFELATG 214
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
573-831 2.92e-16

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: 82.16  E-value: 2.92e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQN-------------LILRNQIQQAFVE-RDILTFAENPFvvsmyc 638
Cdd:cd07864      9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNekegfpitaireiKILRQLNHRSVVNlKEIVTDKQDAL------ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  639 SFETR-RHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGL 717
Cdd:cd07864     83 DFKKDkGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SKvglmsmttnLYEghiEKDAREFLDKQVcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGcVPFFGDTPE---- 792
Cdd:cd07864    163 AR---------LYN---SEESRPYTNKVI--TLWYRPPELLLgEERYGPAIDVWSCGCILGELFTK-KPIFQANQElaql 227
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  793 ELFGQVISDEI--NWPEKDEAP----------------------PPDAQDLITLLLRQNPLER 831
Cdd:cd07864    228 ELISRLCGSPCpaVWPDVIKLPyfntmkpkkqyrrrlreefsfiPTPALDLLDHMLTLDPSKR 290
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
579-787 3.06e-16

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: 81.93  E-value: 3.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQIQQAfVERDILTFAENPFVVSMYCSFETRRHLC------MVMEY 652
Cdd:cd14038      2 LGTGGFGNVLRWINQETGEQVAIKQC-RQELSPKNRERWC-LEIQIMKRLNHPNVVAARDVPEGLQKLApndlplLAMEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCA---TLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTS----MGHiKLTDFGLSKvglmsm 725
Cdd:cd14038     80 CQGGDLRkylNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQgeqrLIH-KIIDLGYAK------ 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  726 ttnlyeghiEKDAREFLDKQVcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFF 787
Cdd:cd14038    153 ---------ELDQGSLCTSFV-GTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL 204
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
582-811 3.88e-16

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 81.45  E-value: 3.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNlilrnqIQQAFVERDI--LTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDca 659
Cdd:cd14104     11 GQFGIVHRCVETSSKKTYMAKFVKVKG------ADQVLVKKEIsiLNIARHRNILRLHESFESHEELVMIFEFISGVD-- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  660 tLMKNMGPLPVDMARM----YFAETVLALEYLHNYGIVHRDLKPDNLLVTSM--GHIKLTDFGLSKvglmsmttNLYEGh 733
Cdd:cd14104     83 -IFERITTARFELNEReivsYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSR--------QLKPG- 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  734 iEKDAREFLdkqvcgTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEinWPEKDEA 811
Cdd:cd14104    153 -DKFRLQYT------SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAE--YAFDDEA 221
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
573-752 4.00e-16

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: 80.96  E-value: 4.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMK--KINKQNLILRNqiqqafvERDIL-TFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14016      2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKieKKDSKHPQLEY-------EAKVYkLLQGGPGIPRLYWFGQEGDYNVMV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVeGGDCATLMKNMGplpvdmaRMYFAETVL--------ALEYLHNYGIVHRDLKPDNLLV---TSMGHIKLTDFGLS 718
Cdd:cd14016     75 MDLL-GPSLEDLFNKCG-------RKFSLKTVLmladqmisRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLA 146
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1988312908  719 KVgLMSMTTNLyegHIEKdaREflDKQVCGTPEY 752
Cdd:cd14016    147 KK-YRDPRTGK---HIPY--RE--GKSLTGTARY 172
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
560-787 4.40e-16

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: 81.61  E-value: 4.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  560 ASLKLRRKPrESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCS 639
Cdd:cd06634      5 AELFFKDDP-EKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 FETRRHLCMVMEYVEGGDCATLMKNMGPL-PVDMARMYFAeTVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGls 718
Cdd:cd06634     84 YLREHTAWLVMEYCLGSASDLLEVHKKPLqEVEIAAITHG-ALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG-- 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  719 kvglmsmttnlyEGHIEKDAREFLdkqvcGTPEYIAPEVILRQGYGK---PVDWWAMGIILYEFLVGCVPFF 787
Cdd:cd06634    161 ------------SASIMAPANSFV-----GTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLF 215
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
573-849 5.08e-16

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 81.40  E-value: 5.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKInkqnlilrnQIQQ--------AFVERDILTFAENPFVVSMYCSFETRR 644
Cdd:PLN00009     4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKI---------RLEQedegvpstAIREISLLKEMQHGNIVRLQDVVHSEK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEggdcATLMKNMGPLP-----VDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHIKLTDFGLS 718
Cdd:PLN00009    75 RLYLVFEYLD----LDLKKHMDSSPdfaknPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLA 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 KVGLMSMTTNLYEghiekdarefldkqvCGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEfLVGCVPFF-GDTP-EELF 795
Cdd:PLN00009   151 RAFGIPVRTFTHE---------------VVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAE-MVNQKPLFpGDSEiDELF 214
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  796 G--QVIS--DEINWPE-------KDEAPP--------------PDAQDLITLLLRQNPLERLGTGGAYEvkqHRFFRSL 849
Cdd:PLN00009   215 KifRILGtpNEETWPGvtslpdyKSAFPKwppkdlatvvptlePAGVDLLSKMLRLDPSKRITARAALE---HEYFKDL 290
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
573-831 6.87e-16

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: 80.42  E-value: 6.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQNlilRNQIQQAFVERDILTFAENPFVVSM--YCSFETRRHLC--- 647
Cdd:cd13986      2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHS---KEDVKEAMREIENYRLFNHPNILRLldSQIVKEAGGKKevy 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNM----GPLPVDMARMYFAETVLALEYLHNYGIV---HRDLKPDNLLVTSMGHIKLTDFGlskv 720
Cdd:cd13986     79 LLLPYYKRGSLQDEIERRlvkgTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLG---- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  721 glmSMT--TNLYEGHIEKDAREFLDKQVCgTPEYIAPE---VILRQGYGKPVDWWAMGIILYEFLVGCVPFfgdtpEELF 795
Cdd:cd13986    155 ---SMNpaRIEIEGRREALALQDWAAEHC-TMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPF-----ERIF 225
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1988312908  796 GQ-------VISDEINWPEKdEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd13986    226 QKgdslalaVLSGNYSFPDN-SRYSEELHQLVKSMLVVNPAER 267
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
578-831 7.40e-16

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: 80.00  E-value: 7.40e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPF----VVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14102      7 VLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIVLLKKVGSgfrgVIKLLDWYERPDGFLIVMERP 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 E-GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV-TSMGHIKLTDFGlskvglmsmttnlyE 731
Cdd:cd14102     87 EpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVdLRTGELKLIDFG--------------S 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 GHIEKDArefLDKQVCGTPEYIAPEVILRQGY-GKPVDWWAMGIILYEFLVGCVPFFGDtpEE------LFGQVISdein 804
Cdd:cd14102    153 GALLKDT---VYTDFDGTRVYSPPEWIRYHRYhGRSATVWSLGVLLYDMVCGDIPFEQD--EEilrgrlYFRRRVS---- 223
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  805 wpekdeappPDAQDLITLLLRQNPLER 831
Cdd:cd14102    224 ---------PECQQLIKWCLSLRPSDR 241
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
582-793 7.44e-16

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: 79.87  E-value: 7.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQqafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATL 661
Cdd:cd14111     14 GRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVLQ----EYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELLHS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  662 MKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGlskvglmSMTTNLYEGHIEKDARef 741
Cdd:cd14111     90 LIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG-------SAQSFNPLSLRQLGRR-- 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  742 ldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEE 793
Cdd:cd14111    161 -----TGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQE 207
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
573-786 1.03e-15

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: 80.05  E-value: 1.03e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnlILRNQIQQAFVERDILT-FAENPFVVSMYCSFETRR------H 645
Cdd:cd06636     18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKkYSHHRNIATYYGAFIKKSppghddQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNM--GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglm 723
Cdd:cd06636     94 LWLVMEFCGAGSVTDLVKNTkgNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQ--- 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  724 smttnlyeghiekdarefLDKQV------CGTPEYIAPEVIL-----RQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd06636    171 ------------------LDRTVgrrntfIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
571-846 1.26e-15

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: 80.44  E-value: 1.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKInkqnlILRNQIQ----QAFVERDILTFAENPFVVSM------YCSF 640
Cdd:cd07866      8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKKI-----LMHNEKDgfpiTALREIKILKKLKHPNVVPLidmaveRPDK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 ETRRHLC--MVMEYVEGgDCATLMKNmgP---LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDF 715
Cdd:cd07866     83 SKRKRGSvyMVTPYMDH-DLSGLLEN--PsvkLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADF 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  716 GLSKVglmsmttnlYEGHIEK-------DAREFLDKQVcgTPEYIAPEVIL--RQgYGKPVDWWAMGIILYEFLVGcVPF 786
Cdd:cd07866    160 GLARP---------YDGPPPNpkgggggGTRKYTNLVV--TRWYRPPELLLgeRR-YTTAVDIWGIGCVFAEMFTR-RPI 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  787 FGDTPEELFGQVISD------EINWPEKDEAPP----------------------PDAQDLITLLLRQNPLERLgtgGAY 838
Cdd:cd07866    227 LQGKSDIDQLHLIFKlcgtptEETWPGWRSLPGcegvhsftnyprtleerfgklgPEGLDLLSKLLSLDPYKRL---TAS 303

                   ....*...
gi 1988312908  839 EVKQHRFF 846
Cdd:cd07866    304 DALEHPYF 311
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
576-792 1.75e-15

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: 80.37  E-value: 1.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKkinkqnlILRNQ---IQQAFVERDILTFAENPF-------VVSMYCSFETRRH 645
Cdd:cd14212      4 LDLLGQGTFGQVVKCQDLKTNKLVAVK-------VLKNKpayFRQAMLEIAILTLLNTKYdpedkhhIVRLLDHFMHHGH 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVeGGDCATLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSM--GHIKLTDFGLSkvg 721
Cdd:cd14212     77 LCIVFELL-GVNLYELLKqnQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGSA--- 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  722 LMSMTTnLYEgHIEkdARefldkqvcgtpEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGcVPFFGDTPE 792
Cdd:cd14212    153 CFENYT-LYT-YIQ--SR-----------FYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPLFPGNSE 207
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
579-794 1.80e-15

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: 78.69  E-value: 1.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKI---NKQNLILRnqiqqafvERDILTFAENPFVVSMY--CSFETRRHLcmVMEYV 653
Cdd:cd14065      1 LGKGFFGEVYKVTHRETGKVMVMKELkrfDEQRSFLK--------EVKLMRRLSHPNILRFIgvCVKDNKLNF--ITEYV 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMG-PLPVDMaRMYFAETVLA-LEYLHNYGIVHRDLKPDNLLVTSMGHIK---LTDFGLSKVgLMSMTTN 728
Cdd:cd14065     71 NGGTLEELLKSMDeQLPWSQ-RVSLAKDIASgMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLARE-MPDEKTK 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  729 lyeghiEKDAREFLDkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEfLVGCVPffgDTPEEL 794
Cdd:cd14065    149 ------KPDRKKRLT--VVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCE-IIGRVP---ADPDYL 202
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
576-813 2.16e-15

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: 79.72  E-value: 2.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVrHKESRQRFAMKKINKQNLILRNQIQQ-----AFVERDILTFAENPFVVSMYCSFE-TRRHLCMV 649
Cdd:cd14041     11 LHLLGRGGFSEVYKA-FDLTEQRYVAVKIHQLNKNWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSlDTDSFCTV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYG--IVHRDLKPDNLLV---TSMGHIKLTDFGLSKVglms 724
Cdd:cd14041     90 LEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGLSKI---- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTTNLYEghiEKDAREfLDKQVCGTPEYIAPEVILrQGYGKP-----VDWWAMGIILYEFLVGCVPFFGDTPEELFGQ-- 797
Cdd:cd14041    166 MDDDSYN---SVDGME-LTSQGAGTYWYLPPECFV-VGKEPPkisnkVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQen 240
                          250
                   ....*....|....*...
gi 1988312908  798 --VISDEINWPEKDEAPP 813
Cdd:cd14041    241 tiLKATEVQFPPKPVVTP 258
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
630-834 2.17e-15

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: 78.56  E-value: 2.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  630 NPFVVSMYCSFETRR------HLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLL 703
Cdd:cd14012     57 HPNLVSYLAFSIERRgrsdgwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVL 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  704 VTSMGH---IKLTDFGLSKVgLMSMTTNlyeghiekdAREFLDKQVCgtpeYIAPEVILRQG-YGKPVDWWAMGIILYEF 779
Cdd:cd14012    137 LDRDAGtgiVKLTDYSLGKT-LLDMCSR---------GSLDEFKQTY----WLPPELAQGSKsPTRKTDVWDLGLLFLQM 202
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  780 LVGCVPFFGDTPEELFgqVISDEInwpekdeapPPDAQDLITLLLRQNPLERLGT 834
Cdd:cd14012    203 LFGLDVLEKYTSPNPV--LVSLDL---------SASLQDFLSKCLSLDPKKRPTA 246
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
578-828 2.84e-15

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: 78.54  E-value: 2.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFV--RHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd14146      1 IIGVGGFGKVYRAtwKGQEVAVKAARQDPDEDIKATAESVRQ---EAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 G--DCATLMKNMGPLPVDMARM-------YFAETVLALEYLHNYGIV---HRDLKPDN-LLVTSMGH-------IKLTDF 715
Cdd:cd14146     78 GtlNRALAAANAAPGPRRARRIpphilvnWAVQIARGMLYLHEEAVVpilHRDLKSSNiLLLEKIEHddicnktLKITDF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  716 GLSKVglMSMTTNLyeghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG-DTPEEL 794
Cdd:cd14146    158 GLARE--WHRTTKM---------------SAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGiDGLAVA 220
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  795 FGqVISDEINWPEKDEAPPPDAQdLITLLLRQNP 828
Cdd:cd14146    221 YG-VAVNKLTLPIPSTCPEPFAK-LMKECWEQDP 252
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
573-846 3.67e-15

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: 78.47  E-value: 3.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQnlilRNQIQQAFVERDILT---FAENPFVVSMY-CSFE-TRRHLC 647
Cdd:cd07831      1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKH----FKSLEQVNNLREIQAlrrLSPHPNILRLIeVLFDrKTGRLA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGgDCATLMKN-MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSmGHIKLTDFGlskvglmsmt 726
Cdd:cd07831     77 LVFELMDM-NLYELIKGrKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFG---------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeghiekDAREFLDKQvcgtP--EYI------APEVILRQG-YGKPVDWWAMGIILYEfLVGCVPFF---------- 787
Cdd:cd07831    145 ----------SCRGIYSKP----PytEYIstrwyrAPECLLTDGyYGPKMDIWAVGCVFFE-ILSLFPLFpgtneldqia 209
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  788 ------GDTPEEL---FGQVISDEINWPEKDEA--------PPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07831    210 kihdvlGTPDAEVlkkFRKSRHMNYNFPSKKGTglrkllpnASAEGLDLLKKLLAYDPDERI---TAKQALRHPYF 282
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
573-846 3.84e-15

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: 78.72  E-value: 3.84e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKinkQNLILRNQIQQAFVERDI---LTFAENPFVVSMYCSFET----RRH 645
Cdd:cd07837      3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKK---TRLEMEEEGVPSTALREVsllQMLSQSIYIVRLLDVEHVeengKPL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGgDCATLMKNMG-----PLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV-TSMGHIKLTDFGLSK 719
Cdd:cd07837     80 LYLVFEYLDT-DLKKFIDSYGrgphnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQKGLLKIADLGLGR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 VglMSMTTNLYEGHIEkdarefldkqvcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGD--------- 789
Cdd:cd07837    159 A--FTIPIKSYTHEIV-------------TLWYRAPEVLLgSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDselqqllhi 223
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  790 -----TPEELFGQVISDEINWPEKDEAPP-----------PDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07837    224 frllgTPNEEVWPGVSKLRDWHEYPQWKPqdlsravpdlePEGVDLLTKMLAYDPAKRI---SAKAALQHPYF 293
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
633-805 4.02e-15

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: 77.70  E-value: 4.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  633 VVSMYCSFETRRHLCMVMEYVEG-GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT-SMGHI 710
Cdd:cd14100     67 VIRLLDWFERPDSFVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGEL 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  711 KLTDFGlskvglmsmttnlyEGHIEKDA--REFLDKQVCGTPEYIApeviLRQGYGKPVDWWAMGIILYEFLVGCVPFFG 788
Cdd:cd14100    147 KLIDFG--------------SGALLKDTvyTDFDGTRVYSPPEWIR----FHRYHGRSAAVWSLGILLYDMVCGDIPFEH 208
                          170       180
                   ....*....|....*....|....*..
gi 1988312908  789 DtpEE------LFGQVISDE----INW 805
Cdd:cd14100    209 D--EEiirgqvFFRQRVSSEcqhlIKW 233
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
582-846 4.29e-15

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: 78.19  E-value: 4.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKInkqnlilrnQIQQ-------AFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd07844     11 GSYATVYKGRSKLTGQLVALKEI---------RLEHeegapftAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GgDCATLMKNMGP-LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLYEGH 733
Cdd:cd07844     82 T-DLKQYMDDCGGgLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARA--KSVPSKTYSNE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEkdarefldkqvcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGcVPFF---GDTPEELfgQVI------SDEI 803
Cdd:cd07844    159 VV-------------TLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATG-RPLFpgsTDVEDQL--HKIfrvlgtPTEE 222
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  804 NWPE-------KDEAPP-----------------PDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd07844    223 TWPGvssnpefKPYSFPfypprplinhaprldriPHGEELALKFLQYEPKKRI---SAAEAMKHPYF 286
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
579-846 4.50e-15

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: 78.22  E-value: 4.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFET----RRHLCMVMEYVE 654
Cdd:cd14031     18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQ-QRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYG--IVHRDLKPDNLLVTS-MGHIKLTDFGLSKVglmsmttnlye 731
Cdd:cd14031     97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL----------- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekdAREFLDKQVCGTPEYIAPEvILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEA 811
Cdd:cd14031    166 ------MRTSFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFNKV 238
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1988312908  812 PPPDAQDLITLLLRQNPLERLGTggaYEVKQHRFF 846
Cdd:cd14031    239 TDPEVKEIIEGCIRQNKSERLSI---KDLLNHAFF 270
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
576-849 5.05e-15

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: 78.50  E-value: 5.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKL--ISNGAYGAVYFVRHKESRQRFAMKKINKQNLilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd07872      9 IKLekLGEGTYATVFKGRSKLTENLVALKEIRLEHE--EGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGgDCATLMKNMGP-LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLYEG 732
Cdd:cd07872     87 DK-DLKQYMDDCGNiMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA--KSVPTKTYSN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HIEkdarefldkqvcgTPEYIAPEVILRQG-YGKPVDWWAMGIILYEFLVGCVPFFGDTPEE-------LFGQVISDeiN 804
Cdd:cd07872    164 EVV-------------TLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDelhlifrLLGTPTEE--T 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  805 WP---EKDE-----------------APPPDAQ--DLITLLLRQNPLERLgtgGAYEVKQHRFFRSL 849
Cdd:cd07872    229 WPgisSNDEfknynfpkykpqplinhAPRLDTEgiELLTKFLQYESKKRI---SAEEAMKHAYFRSL 292
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
573-829 5.17e-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: 79.23  E-value: 5.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLILrnqIQQAFVERDILTFAENPFVVSMYCSFETRRHL---- 646
Cdd:cd07880     17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpfQSELF---AKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfh 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 --CMVMEYVeGGDCATLMKnMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMS 724
Cdd:cd07880     94 dfYLVMPFM-GTDLGKLMK-HEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 MTtnlyeGHIEkdarefldkqvcgTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFGD-------------- 789
Cdd:cd07880    172 MT-----GYVV-------------TRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHdhldqlmeimkvtg 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  790 TPEELFGQVI--SDEINWPEKdeAPPPDAQDLITLLLRQNPL 829
Cdd:cd07880    234 TPSKEFVQKLqsEDAKNYVKK--LPRFRKKDFRSLLPNANPL 273
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
570-791 6.30e-15

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: 78.49  E-value: 6.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYfvRHKESRQRFAMKKINKQNLIlRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd08216      1 ELLYEIGKCFKGGGVVHLA--KHKPTNTLVAVKKINLESDS-KEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGP--LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTdfglskvGLMSMTT 727
Cdd:cd08216     78 TPLMAYGSCRDLLKTHFPegLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLS-------GLRYAYS 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  728 NLYEGHIEKDAREFldkqvcgtPEYI-------APEViLRQ---GYGKPVDWWAMGIILYEFLVGCVPFFgDTP 791
Cdd:cd08216    151 MVKHGKRQRVVHDF--------PKSSeknlpwlSPEV-LQQnllGYNEKSDIYSVGITACELANGVVPFS-DMP 214
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
578-786 6.82e-15

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 77.33  E-value: 6.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVY--FVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd14148      1 IIGVGGFGKVYkgLWRGEEVAVKAARQDPDEDIAVTAENVRQ---EARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIV---HRDLKPDNLLVT--------SMGHIKLTDFGLSKVglMS 724
Cdd:cd14148     78 GALNRALAGK-KVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILepienddlSGKTLKITDFGLARE--WH 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  725 MTTNLyeghiekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14148    155 KTTKM---------------SAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
649-831 8.48e-15

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: 81.04  E-value: 8.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG---HIKLTDFGLSkvglmsm 725
Cdd:TIGR03903   57 VFEYVPGRTLREVLAADGALPAGETGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIG------- 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  726 tTNLYEGHIEKDAREFLDKQVCGTPEYIAPEvilrQGYGKPV----DWWAMGIILYEFLVGCVPFFGDTPEE-LFGQVIS 800
Cdd:TIGR03903  130 -TLLPGVRDADVATLTRTTEVLGTPTYCAPE----QLRGEPVtpnsDLYAWGLIFLECLTGQRVVQGASVAEiLYQQLSP 204
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1988312908  801 DEINWPEKDEAPPpdAQDLITLLLRQNPLER 831
Cdd:TIGR03903  205 VDVSLPPWIAGHP--LGQVLRKALNKDPRQR 233
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
577-832 8.60e-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: 77.55  E-value: 8.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKI----NKQNLILRNQIQqaFVERdiLTFAEN--PFVVSMYCSFETRRHLC--- 647
Cdd:cd14036      6 RVIAEGGFAFVYEAQDVGTGKEYALKRLlsneEEKNKAIIQEIN--FMKK--LSGHPNivQFCSAASIGKEESDQGQaey 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 -MVMEYVEGG--DCATLMKNMGPLPVDMARMYFAETVLALEYLHNYG--IVHRDLKPDNLLVTSMGHIKLTDFGlskvgl 722
Cdd:cd14036     82 lLLTELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFG------ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 mSMTTNLYEGHIEKDA--REFLDKQVC--GTPEYIAPEVI-LRQGY--GKPVDWWAMGIILYeFLvgCvpfFGDTPEELF 795
Cdd:cd14036    156 -SATTEAHYPDYSWSAqkRSLVEDEITrnTTPMYRTPEMIdLYSNYpiGEKQDIWALGCILY-LL--C---FRKHPFEDG 228
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  796 GQVisDEINwpEKDEAPPPDAQ-----DLITLLLRQNPLERL 832
Cdd:cd14036    229 AKL--RIIN--AKYTIPPNDTQytvfhDLIRSTLKVNPEERL 266
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
573-832 1.02e-14

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 77.98  E-value: 1.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKQ-----NLILRN---------------QIQQAFVERD--------- 623
Cdd:cd13977      2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNapenvELALREfwalssiqrqhpnviQLEECVLQRDglaqrmshg 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  624 ------ILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPvDMARMYFAETVLALEYLHNYGIVHRDL 697
Cdd:cd13977     82 ssksdlYLLLVETSLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSRRPDR-QTNTSFMLQLSSALAFLHRNQIVHRDL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  698 KPDNLLVTSMGH---IKLTDFGLSKVGLMSMTTNLYEGHIEKdarEFLdKQVCGTPEYIAPEViLRQGYGKPVDWWAMGI 774
Cdd:cd13977    161 KPDNILISHKRGepiLKVADFGLSKVCSGSGLNPEEPANVNK---HFL-SSACGSDFYMAPEV-WEGHYTAKADIFALGI 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  775 ILYEFLVGCVPFFGDTPEELFGQVISD-----------------EINWPEKDEAP-PPDAQDLITLLLRQNPLERL 832
Cdd:cd13977    236 IIWAMVERITFRDGETKKELLGTYIQQgkeivplgeallenpklELQIPLKKKKSmNDDMKQLLRDMLAANPQERP 311
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
576-786 1.02e-14

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 77.40  E-value: 1.02e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVrHKESRQRFAMKKINKQNLILRNQIQQ-----AFVERDILTFAENPFVVSMYCSFETRRH-LCMV 649
Cdd:cd14040     11 LHLLGRGGFSEVYKA-FDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSLDTDtFCTV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYG--IVHRDLKPDNLLV---TSMGHIKLTDFGLSKVglms 724
Cdd:cd14040     90 LEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKI---- 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  725 MTTNLYeghiEKDAREfLDKQVCGTPEYIAPEVILrQGYGKP-----VDWWAMGIILYEFLVGCVPF 786
Cdd:cd14040    166 MDDDSY----GVDGMD-LTSQGAGTYWYLPPECFV-VGKEPPkisnkVDVWSVGVIFFQCLYGRKPF 226
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
573-782 1.10e-14

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 77.76  E-value: 1.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKI-NKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14229      2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILkNHPSYARQGQIEVGILARLSNENADEFNFVRAYECFQHRNHTCLVFE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKN-MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLL----VTSMGHIKLTDFGlskvglmsmt 726
Cdd:cd14229     82 MLEQNLYDFLKQNkFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFG---------- 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeghiekdAREFLDKQVCGT----PEYIAPEVILRQGYGKPVDWWAMGIILYEFLVG 782
Cdd:cd14229    152 -----------SASHVSKTVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 200
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
569-832 1.21e-14

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: 77.61  E-value: 1.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLisnGAYGAVYFVRHKESRQRFAMKKINK--QNLILRnqiQQAFVERDILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd07856     11 RYSDLQPVGM---GAFGLVCSARDQLTGQNVAVKKIMKpfSTPVLA---KRTYRELKLLKHLRHENIISLSDIFISPLED 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMT 726
Cdd:cd07856     85 IYFVTELLGTDLHRLLTSR-PLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQMT 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeGHIEkdarefldkqvcgTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGcVPFF----------------GD 789
Cdd:cd07856    164 -----GYVS-------------TRYYRAPEIMLTwQKYDVEVDIWSAGCIFAEMLEG-KPLFpgkdhvnqfsiitellGT 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  790 TPEELFGQVISDEI-----NWPEKDEAP--------PPDAQDLITLLLRQNPLERL 832
Cdd:cd07856    225 PPDDVINTICSENTlrfvqSLPKRERVPfsekfknaDPDAIDLLEKMLVFDPKKRI 280
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
644-836 1.37e-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: 76.07  E-value: 1.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEG------------GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIK 711
Cdd:cd14024     45 EGVCSVLEVVIGqdrayaffsrhyGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTK 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  712 LTDFGLSKVGLMSmttnlyeghieKDAREFLDKQVCgtPEYIAPEVI-LRQGY-GKPVDWWAMGIILYEFLVGCVPFFGD 789
Cdd:cd14024    125 LVLVNLEDSCPLN-----------GDDDSLTDKHGC--PAYVGPEILsSRRSYsGKAADVWSLGVCLYTMLLGRYPFQDT 191
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1988312908  790 TPEELFGQVISDEINWPEKDEAPppdAQDLITLLLRQNPLERLGTGG 836
Cdd:cd14024    192 EPAALFAKIRRGAFSLPAWLSPG---ARCLVSCMLRRSPAERLKASE 235
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
577-788 1.55e-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: 76.38  E-value: 1.55e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQRFAMKKinkQNLILRNQIQQAFVERDILTFAENPF--VVSMY--CSfetrRHLCMVMEY 652
Cdd:cd14025      2 EKVGSGGFGQVYKVRHKHWKTWLAIKC---PPSLHVDDSERMELLEEAKKMEMAKFrhILPVYgiCS----EPVGLVMEY 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMgPLPVDMARMYFAETVLALEYLH--NYGIVHRDLKPDNLLVTSMGHIKLTDFGLSK-VGLMSMTtnl 729
Cdd:cd14025     75 METGSLEKLLASE-PLPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLAKwNGLSHSH--- 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  730 yegHIEKDArefldkqVCGTPEYIAPEVILRQG--YGKPVDWWAMGIILYEFLVGCVPFFG 788
Cdd:cd14025    151 ---DLSRDG-------LRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPFAG 201
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
573-789 1.58e-14

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 78.25  E-value: 1.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKkinkqnlILRNQIQ---QAFVERDILTF-----AENPF-VVSMYCSFETR 643
Cdd:cd14224     67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALK-------MVRNEKRfhrQAAEEIRILEHlkkqdKDNTMnVIHMLESFTFR 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGGDCATLMKN-MGPLPVDMARMyFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGH--IKLTDFGLSk 719
Cdd:cd14224    140 NHICMTFELLSMNLYELIKKNkFQGFSLQLVRK-FAHSILqCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSS- 217
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  720 vglmsmttnLYEghiekDAREFLDKQvcgTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGD 789
Cdd:cd14224    218 ---------CYE-----HQRIYTYIQ---SRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGE 270
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
576-787 1.59e-14

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: 77.41  E-value: 1.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLI-----------LRNQIQQAFVE-RDILTFAENPFVVSMYCSFE 641
Cdd:cd07858     10 IKPIGRGAYGIVCSAKNSETNEKVAIKKIANafDNRIdakrtlreiklLRHLDHENVIAiKDIMPPPHREAFNDVYIVYE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 trrhlcmVMEyvegGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvg 721
Cdd:cd07858     90 -------LMD----TDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLAR-- 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  722 lmsmTTNlyeghiekDAREFLDKQVCgTPEYIAPEVILR-QGYGKPVDWWAMGIILYEfLVGCVPFF 787
Cdd:cd07858    157 ----TTS--------EKGDFMTEYVV-TRWYRAPELLLNcSEYTTAIDVWSVGCIFAE-LLGRKPLF 209
PDZ smart00228
Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF ...
1145-1227 1.71e-14

Domain present in PSD-95, Dlg, and ZO-1/2; Also called DHR (Dlg homologous region) or GLGF (relatively well conserved tetrapeptide in these domains). Some PDZs have been shown to bind C-terminal polypeptides; others appear to bind internal (non-C-terminal) polypeptides. Different PDZs possess different binding specificities.


Pssm-ID: 214570 [Multi-domain]  Cd Length: 85  Bit Score: 70.87  E-value: 1.71e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  1145 IVIHSSGKNYGFTIRairvyvgDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKV 1224
Cdd:smart00228    5 VELEKGGGGLGFSLV-------GGKDEGGGVVVSSVVPGSPAAKAGLRVGDVILEVNGTSVEGLTHLEAVDLLKKAGGKV 77

                    ...
gi 1988312908  1225 SIT 1227
Cdd:smart00228   78 TLT 80
PDZ_NHERF-like cd06768
PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related ...
1146-1225 1.99e-14

PDZ domains of the Na+/H+ exchange regulatory cofactor (NHERF) family (NHERF1-4), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of the Na+/H+ exchange regulatory cofactor (NHERF) family of multi-PDZ-domain-containing scaffolding proteins (NHERF1-4), and related domains. The NHERF family includes NHERF1 (also known as EBP50), NHERF2 (also known as E3KARP; TKA-1; SIP-1), NHERF3 (also known as CAP70; CLAMP; Napi-Cap-1; PDZD1) and NHERF4 (also known as IKEPP; PDZK2; Napi-Cap-2). NHERF1 and NHERF2 have tandem PDZ domains (PDZ1-2); NHERF3 and NHERF4 have four PDZ domains (PDZ1-4). NHERFs are involved in the regulation of multiple receptors or transporters, such as type II sodium-phosphate cotransporter (Npt2a), purinergic P2Y1 receptor P2Y1R, the beta2-adrenergic receptor (beta2-AR), parathyroid hormone receptor type 1 (PTHR), the lysophosphatidic acid receptors (LPARs), sodium-hydrogen exchanger 3 (NHE3), and cystic fibrosis transmembrane conductance regulator (CFTR). NHERF-PDZ1 domain interaction partners include Npt2a, purinergic P2Y1 receptor, beta2-AR, CFTR, PTHR, NH3, G-protein-coupled receptor kinase 6 (GRK6A), platelet-derived growth factor receptor (PDGFR), B1 subunit of the H+ATPase, cholesterol, receptor for activated C-kinase RACK1, aquaporin 9, among others. The NHERF PDZ2 domain interacts with fewer proteins: NHERF1 PDZ2 binds Npt2a, PTHR, beta-catenin, aquaporin 9, and RACK1; NHERF2 PDZ2 binds LPA2, P2Y1R, and NHE3, cGMP-dependent protein kinase type II (cGKII). NHERF4 PDZ1 and PDZ4 bind the epithelial Ca(2+) channels TRPV5 and TRPV6. NHERF2/NHERF3 heterodimerization is mediated by PDZ domains of NHERF2 and the C-terminal PDZ domain recognition motif of NHERF3. NHERF4 regulates several transporters mediating influx of xenobiotics and nutrients in the small intestine. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This NHERF-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467249 [Multi-domain]  Cd Length: 80  Bit Score: 70.55  E-value: 1.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1146 VIHSSGKNYGFTIRAIRVYVGdsdiytvhHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKVS 1225
Cdd:cd06768      4 HLVKGPEGYGFNLHAEKGRPG--------HFIREVDPGSPAERAGLKDGDRLVEVNGENVEGESHEQVVEKIKASGNQVT 75
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
573-799 2.11e-14

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: 77.38  E-value: 2.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNlilRNQIQQAFVERDILTFAENPFVVSMYCSF------ETRR 644
Cdd:cd07876     23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRpfQN---QTHAKRAYRELVLLKCVNHKNIISLLNVFtpqkslEEFQ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGDCATLMknmgpLPVDMARMYFA--ETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvgl 722
Cdd:cd07876    100 DVYLVMELMDANLCQVIH-----MELDHERMSYLlyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--- 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  723 mSMTTNlyeghiekdareFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd07876    172 -TACTN------------FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVI 235
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
573-788 2.99e-14

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: 77.00  E-value: 2.99e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNLIlrnQIQQAFVERDILTFAENPFVVSMYCSFETRRHL---- 646
Cdd:cd07877     19 YQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRpfQSII---HAKRTYRELRLLKHMKHENVIGLLDVFTPARSLeefn 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 -CMVMEYVEGGDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSM 725
Cdd:cd07877     96 dVYLVTHLMGADLNNIVKCQ-KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEM 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  726 TtnlyeGHIekdarefldkqvcGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFFG 788
Cdd:cd07877    175 T-----GYV-------------ATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPG 220
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
576-786 3.01e-14

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 75.78  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKI---NKQNL-ILRNQIQ---QAFVERDILTFAENPFVVSMYCSFEtrrhLCM 648
Cdd:cd14037      8 EKYLAEGGFAHVYLVKTSNGGNRAALKRVyvnDEHDLnVCKREIEimkRLSGHKNIVGYIDSSANRSGNGVYE----VLL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKnmgplpvdmARMY-----------FAETVLALEYLHNYG--IVHRDLKPDNLLVTSMGHIKLTDF 715
Cdd:cd14037     84 LMEYCKGGGVIDLMN---------QRLQtglteseilkiFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDF 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  716 GLSKVGLMSMTTNLYEGHIEKDArefldkQVCGTPEYIAPEVI---LRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14037    155 GSATTKILPPQTKQGVTYVEEDI------KKYTTLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPF 222
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
573-787 3.10e-14

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 76.66  E-value: 3.10e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKkinkqnlILRNQ---IQQAFVERDILTF-----AENPF-VVSMYCSFETR 643
Cdd:cd14225     45 YEILEVIGKGSFGQVVKALDHKTNEHVAIK-------IIRNKkrfHHQALVEVKILDAlrrkdRDNSHnVIHMKEYFYFR 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVeGGDCATLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH--IKLTDFGLSk 719
Cdd:cd14225    118 NHLCITFELL-GMNLYELIKknNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGSS- 195
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  720 vglmsmttnLYEghiekDAREFLDKQvcgTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGcVPFF 787
Cdd:cd14225    196 ---------CYE-----HQRVYTYIQ---SRFYRSPEVILGLPYSMAIDMWSLGCILAELYTG-YPLF 245
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
645-817 3.30e-14

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: 75.12  E-value: 3.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGdcaTLMKNMGPLPVDMARM--YFAETVLALEYLHNYG---IVHRDLKPDN-LLVTSMGH-------IK 711
Cdd:cd14061     67 NLCLVMEYARGG---ALNRVLAGRKIPPHVLvdWAIQIARGMNYLHNEApvpIIHRDLKSSNiLILEAIENedlenktLK 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  712 LTDFGLSKVglMSMTTNLYEGhiekdarefldkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTP 791
Cdd:cd14061    144 ITDFGLARE--WHKTTRMSAA---------------GTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDG 206
                          170       180
                   ....*....|....*....|....*.
gi 1988312908  792 EELFGQVISDEINWPEKDEAPPPDAQ 817
Cdd:cd14061    207 LAVAYGVAVNKLTLPIPSTCPEPFAQ 232
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
573-789 4.60e-14

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: 75.78  E-value: 4.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESR--QRFAMKKInKQNLILRNQIQQAFVeRDILTFAE--NPFVVSMYCSF--ETRRHL 646
Cdd:cd07842      2 YEIEGCIGRGTYGRVYKAKRKNGKdgKEYAIKKF-KGDKEQYTGISQSAC-REIALLRElkHENVVSLVEVFleHADKSV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGgDCATLMK-----NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH----IKLTDFGL 717
Cdd:cd07842     80 YLLFDYAEH-DLWQIIKfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPergvVKIGDLGL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  718 SKVgLMSMTTNLYEGhiekdareflDKQVCgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGD 789
Cdd:cd07842    159 ARL-FNAPLKPLADL----------DPVVV-TIWYRAPELLLgARHYTKAIDIWAIGCIFAELLTLEPIFKGR 219
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
572-831 4.64e-14

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 75.07  E-value: 4.64e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKL---ISNGAYGAVY-------FVRHKESRQrfamkKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFE 641
Cdd:cd14147      1 SFQELRLeevIGIGGFGKVYrgswrgeLVAVKAARQ-----DPDEDISVTAESVRQ---EARLFAMLAHPNIIALKAVCL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 TRRHLCMVMEYVEGGDCATLMKNMgPLPVDMARMYFAETVLALEYLHNYGIV---HRDLKPDNLLVT------SMGH--I 710
Cdd:cd14147     73 EEPNLCLVMEYAAGGPLSRALAGR-RVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLqpiendDMEHktL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  711 KLTDFGLSKvglmsmttnlyEGHiekdarEFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG-D 789
Cdd:cd14147    152 KITDFGLAR-----------EWH------KTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGiD 214
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1988312908  790 TPEELFGqVISDEINWPEKDEAPPPDAQdLITLLLRQNPLER 831
Cdd:cd14147    215 CLAVAYG-VAVNKLTLPIPSTCPEPFAQ-LMADCWAQDPHRR 254
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
579-850 4.87e-14

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 75.34  E-value: 4.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKInKQNLILRNQiQQAFVERDILTFAENPFVVSMYCSFETRRHLC-----MVMEYV 653
Cdd:cd14039      1 LGTGGFGNVCLYQNQETGEKIAIKSC-RLELSVKNK-DRWCHEIQIMKKLNHPNVVKACDVPEEMNFLVndvplLAMEYC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLM---KNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG----HiKLTDFGLSKvglmsmt 726
Cdd:cd14039     79 SGGDLRKLLnkpENCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkivH-KIIDLGYAK------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tNLYEGHiekdarefLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDT-------------PEE 793
Cdd:cd14039    151 -DLDQGS--------LCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNLqpftwhekikkkdPKH 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  794 LFG-QVISDEINWpeKDEAPPPDA---------QDLITLLLRQNPLERlGTGGAYEVKQHRFFRSLD 850
Cdd:cd14039    222 IFAvEEMNGEVRF--STHLPQPNNlcslivepmEGWLQLMLNWDPVQR-GGGLDTDSKQPRCFVLMD 285
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
576-786 5.06e-14

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: 74.95  E-value: 5.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd14026      2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLM--KNMGP---LPVDMARMYfaETVLALEYLHNYG--IVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTtn 728
Cdd:cd14026     82 GSLNELLheKDIYPdvaWPLRLRILY--EIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSIS-- 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  729 lyEGHIEKDAREfldkqvCGTPEYIAPEVI---LRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14026    158 --QSRSSKSAPE------GGTIIYMPPEEYepsQKRRASVKHDIYSYAIIMWEVLSRKIPF 210
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
573-799 5.88e-14

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: 76.24  E-value: 5.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHL---- 646
Cdd:cd07875     26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRpfQN---QTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefq 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 --CMVMEYVEGGDCATLMknmgpLPVDMARMYFA--ETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGL 722
Cdd:cd07875    103 dvYIVMELMDANLCQVIQ-----MELDHERMSYLlyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 177
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  723 MSmttnlyeghiekdareFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd07875    178 TS----------------FMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVI 238
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
542-791 5.96e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 76.07  E-value: 5.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  542 DSGTAETPETDESVSSSNASLKLRRKPRESDFETIKLISNGAYGAVyFVRHKESRQRFAMKKINKQNLILrnqiqqafVE 621
Cdd:PHA03209    37 DDDSASESDDDDDDGLIPTKQKAREVVASLGYTVIKTLTPGSEGRV-FVATKPGQPDPVVLKIGQKGTTL--------IE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  622 RDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDN 701
Cdd:PHA03209   108 AMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTEN 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  702 LLVTSMGHIKLTDFGLSKVGLMsmttnlyeghiekdAREFLDkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLV 781
Cdd:PHA03209   188 IFINDVDQVCIGDLGAAQFPVV--------------APAFLG--LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEMLA 251
                          250
                   ....*....|
gi 1988312908  782 GCVPFFGDTP 791
Cdd:PHA03209   252 YPSTIFEDPP 261
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
656-832 6.05e-14

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: 74.00  E-value: 6.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKpdnllvtsMGHIKLTDFGLSKVGLMSmttnLYEGHIE 735
Cdd:cd13976     69 GDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLK--------LRKFVFADEERTKLRLES----LEDAVIL 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  736 KDAREFL-DKQVCgtPEYIAPEVILRQGY--GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWPekdEAP 812
Cdd:cd13976    137 EGEDDSLsDKHGC--PAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIP---ETL 211
                          170       180
                   ....*....|....*....|
gi 1988312908  813 PPDAQDLITLLLRQNPLERL 832
Cdd:cd13976    212 SPRARCLIRSLLRREPSERL 231
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
579-847 9.15e-14

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: 74.32  E-value: 9.15e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLIlRNQIQQAFVERDILTFAENPFVVSMYCSFET----RRHLCMVMEYVE 654
Cdd:cd14030     33 IGRGSFKTVYKGLDTETTVEVAWCELQDRKLS-KSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIVLVTELMT 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYG--IVHRDLKPDNLLVTS-MGHIKLTDFGLSKVglmsmttnlye 731
Cdd:cd14030    112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLATL----------- 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  732 ghiekdAREFLDKQVCGTPEYIAPEvILRQGYGKPVDWWAMGIILYEFLVGCVPFFG-DTPEELFGQVISDeINWPEKDE 810
Cdd:cd14030    181 ------KRASFAKSVIGTPEFMAPE-MYEEKYDESVDVYAFGMCMLEMATSEYPYSEcQNAAQIYRRVTSG-VKPASFDK 252
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1988312908  811 APPPDAQDLITLLLRQNPLERlgtggaYEVK---QHRFFR 847
Cdd:cd14030    253 VAIPEVKEIIEGCIRQNKDER------YAIKdllNHAFFQ 286
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
576-799 1.04e-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: 74.34  E-value: 1.04e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHK----ESRQRFAMKKINK-QNLILRNQIQQafvERDILTFAENPFVVSM-YCSFET-RRHLCM 648
Cdd:cd05038      9 IKQLGEGHFGSVELCRYDplgdNTGEQVAVKSLQPsGEEQHMSDFKR---EIEILRTLDHEYIVKYkGVCESPgRRSLRL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPlPVDMARMY-FAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMT 726
Cdd:cd05038     86 IMEYLPSGSLRDYLQRHRD-QIDLKRLLlFASQICkGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKV--LPED 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  727 TNLYEGHIEKDAREFldkqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFgdTPEELFGQVI 799
Cdd:cd05038    163 KEYYYVKEPGESPIF----------WYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ--SPPALFLRMI 223
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
573-799 1.35e-13

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: 75.12  E-value: 1.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINK--QNlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHL---- 646
Cdd:cd07874     19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRpfQN---QTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefq 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 --CMVMEYVEGGDCATLMknmgpLPVDMARMYFA--ETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGL 722
Cdd:cd07874     96 dvYLVMELMDANLCQVIQ-----MELDHERMSYLlyQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  723 MSMTTNLYeghiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVI 799
Cdd:cd07874    171 TSFMMTPY----------------VVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVI 231
PDZ_canonical cd00136
canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs ...
1145-1227 1.44e-13

canonical PDZ domain; Canonical PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain. PDZ domains usually bind to short specific peptide sequences located at the C-terminal end of their partner proteins known as PDZ binding motifs. These domains can also interact with internal peptide motifs and certain lipids, and can take part in a head-to-tail oligomerization with other PDZ domains. The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467153 [Multi-domain]  Cd Length: 81  Bit Score: 67.95  E-value: 1.44e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1145 IVIH-SSGKNYGFTIRairvyvGDSDiYTVHHIVWNVEEGSPACQAG-LKAGDLITHINGEPVHGLVHTEVIELLLKSGN 1222
Cdd:cd00136      2 VTLEkDPGGGLGFSIR------GGKD-GGGGIFVSRVEPGGPAARDGrLRVGDRILEVNGVSLEGLTHEEAVELLKSAGG 74

                   ....*
gi 1988312908 1223 KVSIT 1227
Cdd:cd00136     75 EVTLT 79
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
573-786 1.51e-13

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: 73.98  E-value: 1.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINkqnlILRNQIQQAFVERDILT-FAENPFVVSMYCSFETRR------H 645
Cdd:cd06637      8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKkYSHHRNIATYYGAFIKKNppgmddQ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNM--GPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglm 723
Cdd:cd06637     84 LWLVMEFCGAGSVTDLIKNTkgNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSA---- 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  724 smttnlyeghiEKDAREFLDKQVCGTPEYIAPEVIL-----RQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd06637    160 -----------QLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPL 216
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
637-846 2.18e-13

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: 72.39  E-value: 2.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  637 YCSFETRRHLCMVMEYVEG------------GDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLV 704
Cdd:cd14023     38 YIQLPSHRNITGIVEVILGdtkayvffekdfGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  705 TSMGHIKLTdfglskvglmsmTTNLYEGHIEKDAREFL-DKQVCgtPEYIAPEVILRQGY--GKPVDWWAMGIILYEFLV 781
Cdd:cd14023    118 SDEERTQLR------------LESLEDTHIMKGEDDALsDKHGC--PAYVSPEILNTTGTysGKSADVWSLGVMLYTLLV 183
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  782 GCVPFFGDTPEELFGQVISDEINWPEKDEappPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFF 846
Cdd:cd14023    184 GRYPFHDSDPSALFSKIRRGQFCIPDHVS---PKARCLIRSLLRREPSERL---TAPEILLHPWF 242
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
579-780 2.19e-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: 73.05  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNlilrNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGD 657
Cdd:cd14222      1 LGKGFFGQAIKVTHKATGKVMVMKELIRCD----EETQKTFLtEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLMKNMGPLPVDMaRMYFAETVLA-LEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGL-------MSMTTNL 729
Cdd:cd14222     77 LKDFLRADDPFPWQQ-KVSFAKGIASgMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVeekkkppPDKPTTK 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  730 YE--GHIEKDARefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd14222    156 KRtlRKNDRKKR----YTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
579-803 2.20e-13

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: 73.08  E-value: 2.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQrFAMKKINKQNlilRNQIQQAF-VERDILTFAENPFVVSMY-CSFETRRHlCMVMEYVEGG 656
Cdd:cd14066      1 IGSGGFGTVYKGVLENGTV-VAVKRLNEMN---CAASKKEFlTELEMLGRLRHPNLVRLLgYCLESDEK-LLVYEYMPNG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 ---DCATLMKNMGPLP--------VDMARmyfaetvlALEYLHNYG---IVHRDLKPDNLLVTSMGHIKLTDFGLSKVgl 722
Cdd:cd14066     76 sleDRLHCHKGSPPLPwpqrlkiaKGIAR--------GLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLARL-- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  723 msmttnlyeghIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFgDTPEELFGQVISDE 802
Cdd:cd14066    146 -----------IPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVD-ENRENASRKDLVEW 213

                   .
gi 1988312908  803 I 803
Cdd:cd14066    214 V 214
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
579-786 2.69e-13

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 72.43  E-value: 2.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYfvrhkesRQRF----AMKKIN------KQNLILRNQIQqafVER-----DILTFaenpfvvsMYCSfeTR 643
Cdd:cd14062      1 IGSGSFGTVY-------KGRWhgdvAVKKLNvtdptpSQLQAFKNEVA---VLRktrhvNILLF--------MGYM--TK 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGgdcATLMKN---------MGPLpVDMARmyfaETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTD 714
Cdd:cd14062     61 PQLAIVTQWCEG---SSLYKHlhvletkfeMLQL-IDIAR----QTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGD 132
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  715 FGLSKVGLMSMTTNLYEghiekdarefldkQVCGTPEYIAPEVILRQG---YGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14062    133 FGLATVKTRWSGSQQFE-------------QPTGSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPY 194
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
573-786 4.19e-13

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 73.13  E-value: 4.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYG-AVYFVRHKESRQRFAMKKIN-----KQNLILRNQIQQAFVERDIltfAENPFVVSMYCSFETRRHL 646
Cdd:cd14215     14 YEIVSTLGEGTFGrVVQCIDHRRGGARVALKIIKnvekyKEAARLEINVLEKINEKDP---ENKNLCVQMFDWFDYHGHM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVeGGDCATLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH--------------- 709
Cdd:cd14215     91 CISFELL-GLSTFDFLKenNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDYeltynlekkrdersv 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  710 ----IKLTDFGlskvglmSMTTNlYEGHiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVP 785
Cdd:cd14215    170 kstaIRVVDFG-------SATFD-HEHH----------STIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTL 231

                   .
gi 1988312908  786 F 786
Cdd:cd14215    232 F 232
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
579-825 4.22e-13

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: 71.89  E-value: 4.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKInKQNLI--LRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd05084      4 IGRGNFGEVFSGRLRADNTPVAVKSC-RETLPpdLKAKFLQ---EARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGP-LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV---GLMSMTTNLyeg 732
Cdd:cd05084     80 DFLTFLRTEGPrLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREeedGVYAATGGM--- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 hiekdarefldKQVcgTPEYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFfgdtpEELFGQVISDEINWPEKDEA 811
Cdd:cd05084    157 -----------KQI--PVKWTAPEALNYGRYSSESDVWSFGILLWEtFSLGAVPY-----ANLSNQQTREAVEQGVRLPC 218
                          250
                   ....*....|....
gi 1988312908  812 PPPDAQDLITLLLR 825
Cdd:cd05084    219 PENCPDEVYRLMEQ 232
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
552-782 4.36e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 73.88  E-value: 4.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  552 DESVSSSNASLKLRRKPR----ESDFETIKLISNGAYGAVYFVRHKESRQRFAMKKinkqnlilrNQIQQAFVERDILTF 627
Cdd:PHA03212    69 DEDESDADASLALCAEARagieKAGFSILETFTPGAEGFAFACIDNKTCEHVVIKA---------GQRGGTATEAHILRA 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  628 AENPFVVSMYCSFETRRHLCMVMEYVEGgDCATLMKNMGPLPV-DMarMYFAETVL-ALEYLHNYGIVHRDLKPDNLLVT 705
Cdd:PHA03212   140 INHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAIcDI--LAIERSVLrAIQYLHENRIIHRDIKAENIFIN 216
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  706 SMGHIKLTDFGlSKVGLMSMTTNLYEGHiekdarefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVG 782
Cdd:PHA03212   217 HPGDVCLGDFG-AACFPVDINANKYYGW-------------AGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATC 279
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
566-825 4.73e-13

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: 72.06  E-value: 4.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  566 RKPRESDFETIKLISNGAYGAVY---FVRHKESRQ-RFAMKKINKqnlilrNQIQQAFVE--RDILTFA--ENPFVVSMY 637
Cdd:cd05057      2 RIVKETELEKGKVLGSGAFGTVYkgvWIPEGEKVKiPVAIKVLRE------ETGPKANEEilDEAYVMAsvDHPHLVRLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  638 CSFETRRHlCMVMEYVEGGDCATLMKN----MGPLPVDMARMYFAEtvlALEYLHNYGIVHRDLKPDNLLVTSMGHIKLT 713
Cdd:cd05057     76 GICLSSQV-QLITQLMPLGCLLDYVRNhrdnIGSQLLLNWCVQIAK---GMSYLEEKRLVHRDLAARNVLVKTPNHVKIT 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  714 DFGLSKVglmsmttnlyeghIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVgcvpfFGDTP-E 792
Cdd:cd05057    152 DFGLAKL-------------LDVDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMT-----FGAKPyE 213
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1988312908  793 ELFGQVISDEINWPEKDEAPPPDAQDLITLLLR 825
Cdd:cd05057    214 GIPAVEIPDLLEKGERLPQPPICTIDVYMVLVK 246
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
573-782 1.18e-12

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 72.04  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKI-NKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVME 651
Cdd:cd14227     17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILkNHPSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKN-MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG----HIKLTDFGlskvglmsmt 726
Cdd:cd14227     97 MLEQNLYDFLKQNkFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpyRVKVIDFG---------- 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  727 tnlyeghiekdAREFLDKQVCGT----PEYIAPEVILRQGYGKPVDWWAMGIILYEFLVG 782
Cdd:cd14227    167 -----------SASHVSKAVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 215
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
571-782 1.34e-12

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 72.04  E-value: 1.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQRFAMKKI-NKQNLILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14228     15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILkNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKN-MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLL----VTSMGHIKLTDFGlskvglms 724
Cdd:cd14228     95 FEMLEQNLYDFLKQNkFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFG-------- 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  725 mttnlyeghiekdAREFLDKQVCGT----PEYIAPEVILRQGYGKPVDWWAMGIILYEFLVG 782
Cdd:cd14228    167 -------------SASHVSKAVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 215
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
579-780 1.56e-12

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 70.20  E-value: 1.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMK----KINKQNLILRNQIQQAFVERDILTFAEnpfvvsmYCSFETRRHlcMVMEYVE 654
Cdd:cd14155      1 IGSGFFSEVYKVRHRTSGQVMALKmntlSSNRANMLREVQLMNRLSHPNILRFMG-------VCVHQGQLH--ALTEYIN 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMaRMYFA-ETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---IKLTDFGLSKvglmsmTTNLY 730
Cdd:cd14155     72 GGNLEQLLDSNEPLSWTV-RVKLAlDIARGLSYLHSKGIFHRDLTSKNCLIKRDENgytAVVGDFGLAE------KIPDY 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1988312908  731 EGHIEKDArefldkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd14155    145 SDGKEKLA-------VVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
579-794 1.63e-12

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 69.95  E-value: 1.63e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQnlilRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC 658
Cdd:cd14110     11 INRGRFSVVRQCEEKRSGQMLAAKIIPYK----PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPEL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  659 ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGlskvglmsmttnlyeghiekDA 738
Cdd:cd14110     87 LYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG--------------------NA 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  739 REFLDKQVCGTP------EYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:cd14110    147 QPFNQGKVLMTDkkgdyvETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWER 208
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
582-788 2.18e-12

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: 69.60  E-value: 2.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNlilrnqiqqafVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATL 661
Cdd:cd14060      4 GSFGSVYRAIWVSQDKEVAVKKLLKIE-----------KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  662 MKNMGPLPVDMARM--YFAETVLALEYLHNYG---IVHRDLKPDNLLVTSMGHIKLTDFGLSKvgLMSMTTNLyeghiek 736
Cdd:cd14060     73 LNSNESEEMDMDQImtWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASR--FHSHTTHM------- 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  737 darefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG 788
Cdd:cd14060    144 --------SLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
579-786 3.85e-12

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: 69.26  E-value: 3.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLIlRNQIQQAFVERDILTFAENPFVVSMYCSFET--RRHLCMVM--EYVE 654
Cdd:cd14033      9 IGRGSFKTVYRGLDTETTVEVAWCELQTRKLS-KGERQRFSEEVEMLKGLQHPNIVRFYDSWKStvRGHKCIILvtELMT 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYG--IVHRDLKPDNLLVTS-MGHIKLTDFGLSKVGLMSMTtnlye 731
Cdd:cd14033     88 SGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLATLKRASFA----- 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  732 ghiekdarefldKQVCGTPEYIAPEvILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14033    163 ------------KSVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCILEMATSEYPY 204
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
568-831 4.64e-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: 68.91  E-value: 4.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESdFETIKLISNGAYGAVYFVRHKESrQRFAMKKINKQNLILrnqiqQAFVER-DILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd05072      5 PRES-IKLVKKLGAGQFGEVWMGYYNNS-TKVAVKTLKPGTMSV-----QAFLEEaNLMKTLQHDKLVRLYAVVTKEEPI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMGPLPVDMARM--YFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglms 724
Cdd:cd05072     78 YIITEYMAKGSLLDFLKSDEGGKVLLPKLidFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARV---- 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  725 mttnlyeghIEKDarEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTPEELFgQVISDE 802
Cdd:cd05072    154 ---------IEDN--EYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVM-SALQRG 221
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  803 INWPeKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd05072    222 YRMP-RMENCPDELYDIMKTCWKEKAEER 249
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
683-845 4.90e-12

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 68.71  E-value: 4.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  683 ALEYLHNYGIVHRDLKPDNLLVTSMG--HIKLTDFGLS-KVGLMSMTTNlyeghiekdarefldkqvCGTPEYIAPEVIL 759
Cdd:cd14112    111 ALHYLHFKGIAHLDVQPDNIMFQSVRswQVKLVDFGRAqKVSKLGKVPV------------------DGDTDWASPEFHN 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  760 RQGYGKP-VDWWAMGIILYEFLVGCVPFFG--DTPEELFGQVISDEINWPEKDEAPPPDAQDLITLLLRQNPLERLGTGG 836
Cdd:cd14112    173 PETPITVqSDIWGLGVLTFCLLSGFHPFTSeyDDEEETKENVIFVKCRPNLIFVEATQEALRFATWALKKSPTRRMRTDE 252

                   ....*....
gi 1988312908  837 AYEvkqHRF 845
Cdd:cd14112    253 ALE---HRW 258
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
531-788 6.49e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 70.26  E-value: 6.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  531 PLEEMAHLGNYDSGTAET-PETD------ESVSSSNASLKLRRKpresdFETIKLISNGAYGAVYF-VRH-KESRQRFAM 601
Cdd:PHA03207    50 DSDDVTHATDYDADEESLsPQTDvcqepcETTSSSDPASVVRMQ-----YNILSSLTPGSEGEVFVcTKHgDEQRKKVIV 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  602 KKINKQNLILRnqiqqafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGgDCATLMKNMGPLPVDMArMYFAETV 681
Cdd:PHA03207   125 KAVTGGKTPGR--------EIDILKTISHRAIINLIHAYRWKSTVCMVMPKYKC-DLFTYVDRSGPLPLEQA-ITIQRRL 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  682 L-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS-KVGLMSMTTNLYEGhiekdarefldkqvCGTPEYIAPEVIL 759
Cdd:PHA03207   195 LeALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAcKLDAHPDTPQCYGW--------------SGTLETNSPELLA 260
                          250       260
                   ....*....|....*....|....*....
gi 1988312908  760 RQGYGKPVDWWAMGIILYEFLVGCVPFFG 788
Cdd:PHA03207   261 LDPYCAKTDIWSAGLVLFEMSVKNVTLFG 289
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
570-831 7.92e-12

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: 68.15  E-value: 7.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKEsrQRFAMKKINKQNlilrNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd05039      5 KKDLKLGELIGKGEFGDVMLGDYRG--QKVAVKCLKDDS----TAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMA-RMYFA-ETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtt 727
Cdd:cd05039     79 TEYMAKGSLVDYLRSRGRAVITRKdQLGFAlDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK-------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyEGHIEKDAREFLDKqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFfgdtPEElfgqVISDEINWP 806
Cdd:cd05039    151 ---EASSNQDGGKLPIK-------WTAPEALREKKFSTKSDVWSFGILLWEiYSFGRVPY----PRI----PLKDVVPHV 212
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  807 EKD---EAP---PPDAQDLITLLLRQNPLER 831
Cdd:cd05039    213 EKGyrmEAPegcPPEVYKVMKNCWELDPAKR 243
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
572-831 9.76e-12

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: 68.14  E-value: 9.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVR-HKESrqrfAMKKINKQNLilrNQIQQAFVERDILTFA----ENpFVVSM-YCSfeTRRH 645
Cdd:cd14063      1 ELEIKEVIGKGRFGRVHRGRwHGDV----AIKLLNIDYL---NEEQLEAFKEEVAAYKntrhDN-LVLFMgACM--DPPH 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNmGPLPVDMARMY-FA-ETVLALEYLHNYGIVHRDLKPDNLLVTSmGHIKLTDFGLSKVglm 723
Cdd:cd14063     71 LAIVTSLCKGRTLYSLIHE-RKEKFDFNKTVqIAqQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSL--- 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttnlyEGHIEKDAREFLDKQVCGTPEYIAPEVI--LRQG--------YGKPVDWWAMGIILYEFLVGCVPFFGDTPEE 793
Cdd:cd14063    146 -------SGLLQPGRREDTLVIPNGWLCYLAPEIIraLSPDldfeeslpFTKASDVYAFGTVWYELLAGRWPFKEQPAES 218
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1988312908  794 LFGQVISDEiNWPEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd14063    219 IIWQVGCGK-KQSLSQLDIGREVKDILMQCWAYDPEKR 255
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
578-793 1.06e-11

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 68.54  E-value: 1.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYfvRHKESRQRFAMKKI---NKQNlilrnqiqqaFV-ERDI--LTFAENPFVVSMY-----CSFETRRHL 646
Cdd:cd14054      2 LIGQGRYGTVW--KGSLDERPVAVKVFparHRQN----------FQnEKDIyeLPLMEHSNILRFIgaderPTADGRMEY 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGD-CATLMKN------MGPLPVDMAR-MYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS 718
Cdd:cd14054     70 LLVLEYAPKGSlCSYLRENtldwmsSCRMALSLTRgLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 kvglMSMTTNLYEGHIEKDAREFLDKQVcGTPEYIAPEVI-----LR--QGYGKPVDWWAMGIILYEFLVGCVPFF-GDT 790
Cdd:cd14054    150 ----MVLRGSSLVRGRPGAAENASISEV-GTLRYMAPEVLegavnLRdcESALKQVDVYALGLVLWEIAMRCSDLYpGES 224

                   ...
gi 1988312908  791 PEE 793
Cdd:cd14054    225 VPP 227
PDZ_SHANK1_3-like cd06746
PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and ...
1145-1227 1.07e-11

PDZ domain of SH3 and multiple ankyrin repeat domains protein 1 (SHANK1), SHANK2, SHANK3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SHANK1, SHANK2, SHANK3, and related domains. SHANK family proteins, SHANK1 (also known as somatostatin receptor-interacting protein, SSTR-interacting protein, SSTRIP), SHANK2 (also known as cortactin-binding protein 1, proline-rich synapse-associated protein 1), and SHANK3 (proline-rich synapse-associated protein 2) are synaptic scaffolding proteins which are highly enriched in the post-synaptic densities of excitatory synapses. They have been implicated in synaptic transmission, synapse formation, synaptic plasticity, and cytoskeletal remodeling, and are regulators of Cav1 calcium current and CREB target expression. Many protein ligands have been identified for the Shank PDZ domain, such as GKAP (also known as SAPAP), betaPIX (a guanine nucleotide exchange factor used by Rho GTPase family members Rac1 and Cdc42), alpha-latrotoxin, neuroligin, group I metabotropic glutamate receptors (mGluRs), and L-type calcium channels. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SHANK-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta- strand F.


Pssm-ID: 467228 [Multi-domain]  Cd Length: 101  Bit Score: 63.38  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1145 IVIHSSGKNYGFTIRAIRV-----------------YVGDsdiytvhhivwnVEEGSPACQAGLKAGDLITHINGEPVHG 1207
Cdd:cd06746      9 VVLQKGDKGFGFVLRGAKAvgpileftptpafpalqYLES------------VDPGGVADKAGLKKGDFLLEINGEDVVK 76
                           90       100
                   ....*....|....*....|
gi 1988312908 1208 LVHTEVIELLLKSGNKVSIT 1227
Cdd:cd06746     77 ASHEQVVNLIRQSGNTLVLK 96
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
573-797 1.20e-11

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: 67.67  E-value: 1.20e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMK--KINKQNLILRNqiqqafvERDIL-TFAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd14017      2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKveSKSQPKQVLKM-------EVAVLkKLQGKPHFCRLIGCGRTERYNYIV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVeGGDCATLMKNMGPlpvdmaRMYFAETVL--------ALEYLHNYGIVHRDLKPDNLLV----TSMGHIKLTDFGL 717
Cdd:cd14017     75 MTLL-GPNLAELRRSQPR------GKFSVSTTLrlgiqilkAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SKVGLMSmttnlyEGHIEKDARE---FLdkqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:cd14017    148 ARQYTNK------DGEVERPPRNaagFR-----GTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLKDKEE 216

                   ...
gi 1988312908  795 FGQ 797
Cdd:cd14017    217 VGK 219
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
579-788 1.59e-11

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: 67.08  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQnliLRNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGD 657
Cdd:cd05041      3 IGRGNFGDVYRGVLKPDNTEVAVKTCRET---LPPDLKRKFLqEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLMKNMGP-LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyeghiEK 736
Cdd:cd05041     80 LLTFLRKKGArLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR---------------EE 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  737 DAREFLD----KQVcgtP-EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFG 788
Cdd:cd05041    145 EDGEYTVsdglKQI---PiKWTAPEALNYGRYTSESDVWSFGILLWEiFSLGATPYPG 199
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
570-783 1.74e-11

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 67.61  E-value: 1.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHK----ESRQRFAMKKINKQNLilrNQIQQAFVERDILTFAENPFVVSM--YCSFETR 643
Cdd:cd05081      3 ERHLKYISQLGKGNFGSVELCRYDplgdNTGALVAVKQLQHSGP---DQQRDFQREIQILKALHSDFIVKYrgVSYGPGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGGDCAT-LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVgl 722
Cdd:cd05081     80 RSLRLVMEYLPSGCLRDfLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKL-- 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908  723 msmttnlyeghIEKDAREFLDKQVCGTPEY-IAPEVILRQGYGKPVDWWAMGIILYEFLVGC 783
Cdd:cd05081    158 -----------LPLDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGVVLYELFTYC 208
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
570-846 2.01e-11

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 67.57  E-value: 2.01e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKESRQRFAMK--------KINKQNLILRNqiqqafverdiltFAENPFVVSMYCSF- 640
Cdd:cd14132     17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKvlkpvkkkKIKREIKILQN-------------LRGGPNIVKLLDVVk 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  641 -ETRRHLCMVMEYVEGGDCATLMKNMGPLPVdmaRMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH-IKLTDFGLS 718
Cdd:cd14132     84 dPQSKTPSLIFEYVNNTDFKTLYPTLTDYDI---RYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 KvglmsmttnLYEGHIEKDARefldkqvCGTPEYIAPEVILR-QGYGKPVDWWAMGIILYEFLVGCVPFF--GDTPEEL- 794
Cdd:cd14132    161 E---------FYHPGQEYNVR-------VASRYYKGPELLVDyQYYDYSLDMWSLGCMLASMIFRKEPFFhgHDNYDQLv 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  795 -----------------FGQVISDEIN----------W-----PEKDEAPPPDAQDLITLLLRQNPLERLgTggAYEVKQ 842
Cdd:cd14132    225 kiakvlgtddlyayldkYGIELPPRLNdilgrhskkpWerfvnSENQHLVTPEALDLLDKLLRYDHQERI-T--AKEAMQ 301

                   ....
gi 1988312908  843 HRFF 846
Cdd:cd14132    302 HPYF 305
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
573-786 2.32e-11

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


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 67.73  E-value: 2.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVY-FVRHKESRQRFAMKKIN-----KQNLILRNQIQQAFVERDiltfAENPFV-VSMYCSFETRRH 645
Cdd:cd14214     15 YEIVGDLGEGTFGKVVeCLDHARGKSQVALKIIRnvgkyREAARLEINVLKKIKEKD----KENKFLcVLMSDWFNFHGH 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVeGGDCATLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH-------------- 709
Cdd:cd14214     91 MCIAFELL-GKNTFEFLKenNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEFdtlynesksceeks 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  710 -----IKLTDFGlskvglmSMTTNlYEGHiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCV 784
Cdd:cd14214    170 vkntsIRVADFG-------SATFD-HEHH----------TTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFT 231

                   ..
gi 1988312908  785 PF 786
Cdd:cd14214    232 LF 233
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
579-833 3.41e-11

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 66.14  E-value: 3.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVY--FVRHKESRQRFAMKkinkqnlILRNQIQQAFVERDILTFA------ENPFVVSMY--CSFETrrhLCM 648
Cdd:cd05116      3 LGSGNFGTVKkgYYQMKKVVKTVAVK-------ILKNEANDPALKDELLREAnvmqqlDNPYIVRMIgiCEAES---WML 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  649 VMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTN 728
Cdd:cd05116     73 VMEMAELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKA--LRADEN 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  729 LYEGhiekdarefldkQVCGT-P-EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGdtpeeLFGQVISDEINW 805
Cdd:cd05116    151 YYKA------------QTHGKwPvKWYAPECMNYYKFSSKSDVWSFGVLMWEaFSYGQKPYKG-----MKGNEVTQMIEK 213
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1988312908  806 PEKDEAP---PPDAQDLITLLLRQNPLERLG 833
Cdd:cd05116    214 GERMECPagcPPEMYDLMKLCWTYDVDERPG 244
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
673-832 6.69e-11

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: 65.98  E-value: 6.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  673 ARMYFAETVLALEYLHNYGIVHRDLKPDNLLV----TSMGHIKLTDFGLSkvgLMSMTTNL---YEGHiekdareFLDKQ 745
Cdd:cd14018    140 ARVMILQLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGCC---LADDSIGLqlpFSSW-------YVDRG 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  746 vcGTPEYIAPEVI-LRQG------YGKpVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEiNWPEKDEAPPPDAQD 818
Cdd:cd14018    210 --GNACLMAPEVStAVPGpgvvinYSK-ADAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQES-QLPALPSAVPPDVRQ 285
                          170
                   ....*....|....
gi 1988312908  819 LITLLLRQNPLERL 832
Cdd:cd14018    286 VVKDLLQRDPNKRV 299
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
621-846 6.88e-11

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: 65.48  E-value: 6.88e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  621 ERDILTFAENPFVVSMYCSFET----RRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYG--IVH 694
Cdd:cd14032     50 EAEMLKGLQHPNIVRFYDFWEScakgKRCIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIH 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  695 RDLKPDNLLVTS-MGHIKLTDFGLSKVglmsmttnlyeghiekdAREFLDKQVCGTPEYIAPEvILRQGYGKPVDWWAMG 773
Cdd:cd14032    130 RDLKCDNIFITGpTGSVKIGDLGLATL-----------------KRASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFG 191
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  774 IILYEFLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPPPDAQDLITLLLRQNPLERlgtggaYEVK---QHRFF 846
Cdd:cd14032    192 MCMLEMATSEYPYSECQNAAQIYRKVTCGIKPASFEKVTDPEIKEIIGECICKNKEER------YEIKdllSHAFF 261
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
571-786 6.90e-11

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 65.27  E-value: 6.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKeSRQRFAMKKINKQNLILRNQIQQAFVERDIltfaENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05114      4 SELTFMKELGSGLFGVVRLGKWR-AQYKVAIKAIREGAMSEEDFIEEAKVMMKL----THPKLVQLYGVCTQQKPIYIVT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGdCAT--LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglmsmttn 728
Cdd:cd05114     79 EFMENG-CLLnyLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGM----------- 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  729 lyeghiekdAREFLDKQV---CGTP---EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPF 786
Cdd:cd05114    147 ---------TRYVLDDQYtssSGAKfpvKWSPPEVFNYSKFSSKSDVWSFGVLMWEvFTEGKMPF 202
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
571-786 8.62e-11

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: 64.78  E-value: 8.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQrFAMKKINKQNLILRNQIQQAFVerdiLTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05059      4 SELTFLKELGSGQFGVVHLGKWRGKID-VAIKMIKEGSMSEDDFIEEAKV----MMKLSHPKLVQLYGVCTKQRPIFIVT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGDCATLMK------NMGPLpVDMARmyfaETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLskvglms 724
Cdd:cd05059     79 EYMANGCLLNYLRerrgkfQTEQL-LEMCK----DVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGL------- 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  725 mttnlyeghiekdAREFLDKQVC---GTP---EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPF 786
Cdd:cd05059    147 -------------ARYVLDDEYTssvGTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWEvFSEGKMPY 202
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
582-831 9.03e-11

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: 65.10  E-value: 9.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQAFVErDILTF------AENPFVVSMYCSFETRRHLCMVMEYveg 655
Cdd:cd13992     17 VKKVGVYGGRTVAIKHITFSRTEKRTILQELNQLKELVHD-NLNKFigicinPPNIAVVTEYCTRGSLQDVLLNREI--- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 gdcatlmkNMGplpvDMARMYFA-ETVLALEYLHN-YGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvGLMSMTTNLYE-G 732
Cdd:cd13992     93 --------KMD----WMFKSSFIkDIVKGMNYLHSsSIGYHGRLKSSNCLVDSRWVVKLTDFGLR--NLLEEQTNHQLdE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HIEKdareflDKQVCGTPEYIAPEVILRQGYGKPvDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEINWP------ 806
Cdd:cd13992    159 DAQH------KKLLWTAPELLRGSLLEVRGTQKG-DVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKPFrpelav 231
                          250       260
                   ....*....|....*....|....*...
gi 1988312908  807 EKDEAPPpdaqDLITLLLR---QNPLER 831
Cdd:cd13992    232 LLDEFPP----RLVLLVKQcwaENPEKR 255
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
578-840 1.21e-10

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: 64.59  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYfvRHKESRQRFAMKKINKQN--LILRNQIQqafverdILTFAENPFVVSMYCSFETRRHLcmVMEYVEG 655
Cdd:cd14068      1 LLGDGGFGSVY--RAVYRGEDVAVKIFNKHTsfRLLRQELV-------VLSHLHHPSLVALLAAGTAPRML--VMELAPK 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDC-ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH-----IKLTDFGLSKVgLMSMTTnl 729
Cdd:cd14068     70 GSLdALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPncaiiAKIADYGIAQY-CCRMGI-- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  730 yeghiekdarefldKQVCGTPEYIAPEVIlrQG---YGKPVDWWAMGIILYEFLVGcvpffgdtpeelfGQVISDEINWP 806
Cdd:cd14068    147 --------------KTSEGTPGFRAPEVA--RGnviYNQQADVYSFGLLLYDILTC-------------GERIVEGLKFP 197
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  807 -EKDE----------------APPPDAQDLITLLLRQNPLERLGTGGAYEV 840
Cdd:cd14068    198 nEFDElaiqgklpdpvkeygcAPWPGVEALIKDCLKENPQCRPTSAQVFDI 248
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
621-825 1.23e-10

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 65.34  E-value: 1.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  621 ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNM----------------GPLPVDMARMYF---AETV 681
Cdd:cd05096     69 EVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHhlddkeengndavppaHCLPAISYSSLLhvaLQIA 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  682 LALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNLYEG-HIEKDAREFLDKQvcgtpeYIAPEVILR 760
Cdd:cd05096    149 SGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSR--------NLYAGdYYRIQGRAVLPIR------WMAWECILM 214
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  761 QGYGKPVDWWAMGIILYEFLVGCvpffgdtPEELFGQVISDEI--NWPE--KDEA-------PPPDAQDLITLLLR 825
Cdd:cd05096    215 GKFTTASDVWAFGVTLWEILMLC-------KEQPYGELTDEQVieNAGEffRDQGrqvylfrPPPCPQGLYELMLQ 283
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
576-783 1.40e-10

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 64.95  E-value: 1.40e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVRHK----ESRQRFAMKKINKQNLilRNQIQQAFVERDILT--FAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd05079      9 IRDLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESG--GNHIADLKKEIEILRnlYHENIVKYKGICTEDGGNGIKLI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCAT-LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttn 728
Cdd:cd05079     87 MEFLPSGSLKEyLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKA-------- 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  729 lyeghIEKDAREFLDKQVCGTPEY-IAPEVILRQGYGKPVDWWAMGIILYEFLVGC 783
Cdd:cd05079    159 -----IETDKEYYTVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELLTYC 209
PDZ2_L-delphilin-like cd06744
PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 ...
1145-1226 1.52e-10

PDZ domain 2 of delphilin (L-delphilin isoform), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 2 of delphilin (also known as glutamate receptor, ionotropic, delta 2-interacting protein 1, L-delphilin). Delphilin, a postsynaptic protein which it is selectively expressed at cerebellar Purkinje cells, links the glutamate receptor delta 2 subunit (GluRdelta2) with the actin cytoskeleton and various signaling molecules. Two alternatively spliced isoforms of delphilin have been characterized: L-delphilin has two PDZ domains, PDZ1 and PDZ2, and S-delphilin has a single PDZ domain (PDZ2). These two isoforms are differently palmitoylated and may be involved in controlling GluRdelta2 signaling in Purkinje cells. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This delphilin-like family PDZ2 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F


Pssm-ID: 467226 [Multi-domain]  Cd Length: 75  Bit Score: 59.21  E-value: 1.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1145 IVIHSSGKNYGFTIRAirvyvgdsdiytvHHIVW--NVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGN 1222
Cdd:cd06744      2 VRVYRGNGSFGFTLRG-------------HAPVYieSVDPGSAAERAGLKPGDRILFLNGLDVRNCSHDKVVSLLQGSGS 68

                   ....
gi 1988312908 1223 KVSI 1226
Cdd:cd06744     69 MPTL 72
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
578-792 1.78e-10

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: 64.38  E-value: 1.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKEsrqRFAMKKI----NKQNLILRNQIQqafveRDILTFAEN--PFVVSMYCSFETRRHLCMVME 651
Cdd:cd13998      2 VIGKGRFGEVWKASLKN---EPVAVKIfssrDKQSWFREKEIY-----RTPMLKHENilQFIAADERDTALRTELWLVTA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  652 YVEGGDCATLMKNMGPLPVDMARMyfAETVL-ALEYLHNY---------GIVHRDLKPDNLLVTSMGHIKLTDFGLSkvg 721
Cdd:cd13998     74 FHPNGSL*DYLSLHTIDWVSLCRL--ALSVArGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLA--- 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  722 lMSMTTNLYEGHIEKDARefldkqvCGTPEYIAPEVI------LRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPE 792
Cdd:cd13998    149 -VRLSPSTGEEDNANNGQ-------VGTKRYMAPEVLegainlRDFESFKRVDIYAMGLVLWEMASRCTDLFGIVEE 217
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
684-788 1.80e-10

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 64.22  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  684 LEYLHNYGIVHRDLKPDNLLVTSMG-----HIKLTDFGLSKvglmsmtTNLYEGHIekdarefldkQVCGTPEYIAPEVI 758
Cdd:cd14067    127 LAYLHKKNIIFCDLKSDNILVWSLDvqehiNIKLSDYGISR-------QSFHEGAL----------GVEGTPGYQAPEIR 189
                           90       100       110
                   ....*....|....*....|....*....|
gi 1988312908  759 LRQGYGKPVDWWAMGIILYEFLVGCVPFFG 788
Cdd:cd14067    190 PRIVYDEKVDMFSYGMVLYELLSGQRPSLG 219
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
621-783 2.04e-10

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 64.63  E-value: 2.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  621 ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGP----------LPVDMARMYFAETVLA--LEYLH 688
Cdd:cd05095     69 EIKIMSRLKDPNIIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPegqlalpsnaLTVSYSDLRFMAAQIAsgMKYLS 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  689 NYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNLYEGHIEK-DAREFLDKQvcgtpeYIAPEVILRQGYGKPV 767
Cdd:cd05095    149 SLNFVHRDLATRNCLVGKNYTIKIADFGMSR--------NLYSGDYYRiQGRAVLPIR------WMSWESILLGKFTTAS 214
                          170
                   ....*....|....*.
gi 1988312908  768 DWWAMGIILYEFLVGC 783
Cdd:cd05095    215 DVWAFGVTLWETLTFC 230
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
576-786 2.11e-10

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: 63.88  E-value: 2.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYFVR-HKEsrqrfAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVsMYCSFETRRHLCMVMEYVE 654
Cdd:cd14150      5 LKRIGTGSFGTVFRGKwHGD-----VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GgdcATLMKNMGPLP--------VDMARmyfaETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMT 726
Cdd:cd14150     79 G---SSLYRHLHVTEtrfdtmqlIDVAR----QTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSG 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1988312908  727 TNLYEghiekdarefldkQVCGTPEYIAPEVILRQG---YGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14150    152 SQQVE-------------QPSGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPY 201
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
579-840 2.31e-10

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 64.26  E-value: 2.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAV-----YFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd05094     13 LGEGAFGKVflaecYNLSPTKDKMLVAVKTLKDPTLAARKDFQR---EAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGP---LPVD-----------MARMYFAETVLA--LEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGL 717
Cdd:cd05094     90 KHGDLNKFLRAHGPdamILVDgqprqakgelgLSQMLHIATQIAsgMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGM 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SKvGLMSMTTNLYEGHIEKDARefldkqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELFG 796
Cdd:cd05094    170 SR-DVYSTDYYRVGGHTMLPIR------------WMPPESIMYRKFTTESDVWSFGVILWEiFTYGKQPWFQLSNTEVIE 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1988312908  797 QVISDEInwPEKDEAPPPDAQDLITLLLRQNPLERLGTGGAYEV 840
Cdd:cd05094    237 CITQGRV--LERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKI 278
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
573-787 2.83e-10

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: 64.65  E-value: 2.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKI-NKQNLilRNQIQqafVERDILTF-----AENPF-VVSMYCSFETRRH 645
Cdd:cd14226     15 YEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIkNKKAF--LNQAQ---IEVRLLELmnkhdTENKYyIVRLKRHFMFRNH 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVME------YveggdcaTLMKNMGPLPVDMARMY-FAETVL-ALEYLH--NYGIVHRDLKPDNLLVTS--MGHIKLT 713
Cdd:cd14226     90 LCLVFEllsynlY-------DLLRNTNFRGVSLNLTRkFAQQLCtALLFLStpELSIIHCDLKPENILLCNpkRSAIKII 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  714 DFGLSkvglMSMTTNLYEgHIEKdarEFldkqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVGcVPFF 787
Cdd:cd14226    163 DFGSS----CQLGQRIYQ-YIQS---RF----------YRSPEVLLGLPYDLAIDMWSLGCILVEMHTG-EPLF 217
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
579-786 2.88e-10

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: 63.32  E-value: 2.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYfvRHKESRQRFAMKKINKQNLILRNQIQQAFVERDILTFAENPFVVSMY-CSFETRRHLCMVMEYVEGGD 657
Cdd:cd14064      1 IGSGSFGKVY--KGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVgACLDDPSQFAIVTQYVSGGS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  658 CATLM----KNMGP-----LPVDMARmyfaetvlALEYLHNYG--IVHRDLKPDNLLVTSMGHIKLTDFGLSKVgLMSMT 726
Cdd:cd14064     79 LFSLLheqkRVIDLqskliIAVDVAK--------GMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRF-LQSLD 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908  727 tnlyeghiekdaREFLDKQVcGTPEYIAPEVILRQG-YGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14064    150 ------------EDNMTKQP-GNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
567-786 3.09e-10

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: 63.36  E-value: 3.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  567 KPRESDFetIKLISNGAYGAVYFVRHKeSRQRFAMKKINKQNLILRNQIQQAfverDILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd05113      2 DPKDLTF--LKELGTGQFGVVKYGKWR-GQYDVAIKMIKEGSMSEDEFIEEA----KVMMNLSHEKLVQLYGVCTKQRPI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNM--GPLPVDMARMYFaETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSkvglms 724
Cdd:cd05113     75 FIITEYMANGCLLNYLREMrkRFQTQQLLEMCK-DVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLS------ 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  725 mttnlyeghiekdaREFLDKQVCGT-----P-EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPF 786
Cdd:cd05113    148 --------------RYVLDDEYTSSvgskfPvRWSPPEVLMYSKFSSKSDVWAFGVLMWEvYSLGKMPY 202
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
636-786 3.10e-10

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 63.54  E-value: 3.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  636 MYCSFETRRHLCMVMEYVEGGDC-----ATLMKNMGPLPVDMARmyfaETVLALEYLHNYGIVHRDLKPDNLLVTSMGHI 710
Cdd:cd14151     68 LFMGYSTKPQLAIVTQWCEGSSLyhhlhIIETKFEMIKLIDIAR----QTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTV 143
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  711 KLTDFGLSKVGLMSMTTNLYEghiekdarefldkQVCGTPEYIAPEVILRQG---YGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14151    144 KIGDFGLATVKSRWSGSHQFE-------------QLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPY 209
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
577-798 3.27e-10

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 63.10  E-value: 3.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKEsRQRFAMKKINKQnliLRNQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05085      2 ELLGKGNFGEVYKGTLKD-KTPVAVKTCKED---LPQELKIKFLsEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCAT-LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyeghi 734
Cdd:cd05085     78 GDFLSfLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSR--------------- 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  735 EKDAREFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELFGQV 798
Cdd:cd05085    143 QEDDGVYSSSGLKQIPiKWTAPEALNYGRYSSESDVWSFGILLWEtFSLGVCPYPGMTNQQAREQV 208
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
621-783 4.23e-10

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 63.46  E-value: 4.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  621 ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDC----------ATLMKNMGPLPVDMARMYFAETVLA--LEYLH 688
Cdd:cd05097     67 EIKIMSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLnqflsqreieSTFTHANNIPSVSIANLLYMAVQIAsgMKYLA 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  689 NYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNLYEGHIEK-DAREFLDKQvcgtpeYIAPEVILRQGYGKPV 767
Cdd:cd05097    147 SLNFVHRDLATRNCLVGNHYTIKIADFGMSR--------NLYSGDYYRiQGRAVLPIR------WMAWESILLGKFTTAS 212
                          170
                   ....*....|....*.
gi 1988312908  768 DWWAMGIILYEFLVGC 783
Cdd:cd05097    213 DVWAFGVTLWEMFTLC 228
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
579-716 4.39e-10

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: 59.76  E-value: 4.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPF--VVSMYCSFETRRHLCMVMEYVEGG 656
Cdd:cd13968      1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLES---EMDILRRLKGLElnIPKVLVTEDVDGPNILLMELVKGG 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 DCATLMKNMGPLPVDMARMYFaETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFG 716
Cdd:cd13968     78 TLIAYTQEEELDEKDVESIMY-QLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
568-832 4.94e-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: 63.13  E-value: 4.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PREsDFETIKLISNGAYGAVYF-----VRHKESRQRFAMKKINkQNLILRNQIQqaFV-ERDILTFAENPFVVSMYCSFE 641
Cdd:cd05032      4 PRE-KITLIRELGQGSFGMVYEglakgVVKGEPETRVAIKTVN-ENASMRERIE--FLnEASVMKEFNCHHVVRLLGVVS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 TRRHLCMVMEYVEGGDCATLMK--------NMGPLPVDMARMY--FAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIK 711
Cdd:cd05032     80 TGQPTLVVMELMAKGDLKSYLRsrrpeaenNPGLGPPTLQKFIqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  712 LTDFGlskvglmsMTTNLYE-GHIEKDAREFLdkqvcgtP-EYIAPEViLRQGYGKPV-DWWAMGIILYEFL-VGCVPFF 787
Cdd:cd05032    160 IGDFG--------MTRDIYEtDYYRKGGKGLL-------PvRWMAPES-LKDGVFTTKsDVWSFGVVLWEMAtLAEQPYQ 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908  788 GDTPEELFGQVISDEInwPEKDEAPPPDAQDLITLLLRQNPLERL 832
Cdd:cd05032    224 GLSNEEVLKFVIDGGH--LDLPENCPDKLLELMRMCWQYNPKMRP 266
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
568-831 8.13e-10

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 62.48  E-value: 8.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESdFETIKLISNGAYGAVYFVRHKES-----RQRFAMKKINKQNlilRNQIQQAF-VERDILTFAENPFVVSMY--CS 639
Cdd:cd05046      3 PRSN-LQEITTLGRGEFGEVFLAKAKGIeeeggETLVLVKALQKTK---DENLQSEFrRELDMFRKLSHKNVVRLLglCR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  640 fETRRHlCMVMEYVEGGDCATLMK-------NMGPLPVDM-ARMYFAETV-LALEYLHNYGIVHRDLKPDNLLVTSMGHI 710
Cdd:cd05046     79 -EAEPH-YMILEYTDLGDLKQFLRatkskdeKLKPPPLSTkQKVALCTQIaLGMDHLSNARFVHRDLAARNCLVSSQREV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  711 KLTDFGLSKvglmsmttnlyeghiEKDARE-FLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFG 788
Cdd:cd05046    157 KVSLLSLSK---------------DVYNSEyYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEvFTQGELPFYG 221
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1988312908  789 DTPEELFGQVISDEINWPEKDEAPppdaQDLITLLLR---QNPLER 831
Cdd:cd05046    222 LSDEEVLNRLQAGKLELPVPEGCP----SRLYKLMTRcwaVNPKDR 263
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
573-786 8.67e-10

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 62.95  E-value: 8.67e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVY-FVRHKESRQRFAMK---KINKQNLILRNQIQqaFVERDILTFAENPF-VVSMYCSFETRRHLC 647
Cdd:cd14213     14 YEIVDTLGEGAFGKVVeCIDHKMGGMHVAVKivkNVDRYREAARSEIQ--VLEHLNTTDPNSTFrCVQMLEWFDHHGHVC 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVeGGDCATLMK--NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGH---------------- 709
Cdd:cd14213     92 IVFELL-GLSTYDFIKenSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYvvkynpkmkrdertlk 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  710 ---IKLTDFGlskvglmSMTTNlYEGHiekdarefldKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14213    171 npdIKVVDFG-------SATYD-DEHH----------STLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVF 232
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
578-786 9.33e-10

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: 62.52  E-value: 9.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  578 LISNGAYGAVYFVRHKEsrQRFAMKKINKQNLILRNQIQQAFvERDILTFA----ENpfVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd14158     22 KLGEGGFGVVFKGYIND--KNVAVKKLAAMVDISTEDLTKQF-EQEIQVMAkcqhEN--LVELLGYSCDGPQLCLVYTYM 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGG---DCATLMKNMGPLPVDMaRMYFAE-TVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGlmsmttnl 729
Cdd:cd14158     97 PNGsllDRLACLNDTPPLSWHM-RCKIAQgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARAS-------- 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  730 yeghiEKDAREFLDKQVCGTPEYIAPEViLRQGYGKPVDWWAMGIILYEFLVGCVPF 786
Cdd:cd14158    168 -----EKFSQTIMTERIVGTTAYMAPEA-LRGEITPKSDIFSFGVVLLEIITGLPPV 218
PDZ_tamalin_CYTIP-like cd06713
PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ ...
1154-1228 1.06e-09

PDZ domain of tamalin, cytohesin-1-interacting protein (CYTIP), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of tamalin, cytohesin-1-interacting protein, and related domains. Tamalin (trafficking regulator and scaffold protein tamalin, also known as general receptor for phosphoinositides 1-associated scaffold protein, GRASP) functions to link receptors, including group 1 metabotropic glutamate receptors (mGluRs), to neuronal proteins. The tamalin PDZ domain binds the C-terminal domains of group I mGluRs; it also binds potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 (HCN2), neurotrophin-3 (NT3) TrkCT1-truncated receptor, SAP90/PSD-95-associated protein, and tamalin itself. CYTIP (cytohesin-1-interacting protein, also known as Pleckstrin homology Sec7 and coiled-coil domain-binding protein) sequesters cytohesin-1 in the cytoplasm, limiting its interaction with beta2 integrins; cytohesin-1 binds the CYTIP coiled coil domain. The CYTIP PDZ domain can bind the C-terminal peptide of protocadherin alpha-1 (PCDHA1), indicating a possible interaction between the two. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This tamalin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467197 [Multi-domain]  Cd Length: 91  Bit Score: 57.25  E-value: 1.06e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908 1154 YGFTIRAIRVYVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKVSITT 1228
Cdd:cd06713     16 FGFEIQTYGLHHKNSNEVEMCTYVCRVHEDSPAYLAGLTAGDVILSVNGVSVEGASHQEIVELIRSSGNTLRLET 90
PDZ_rhophilin-like cd06712
PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density ...
1154-1227 1.11e-09

PDZ domain of rhophilin-1, rhophilin-2, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of rhophilin-1, rhophilin-2, and related domains. Rhophilin-1 (RHPN1, also known as GTP-Rho-binding protein 1) and rhophilin-2 (RHPN2, also known as GTP-Rho-binding protein 2) are Rho-GTP binding proteins involved in cytoskeletal dynamics. Rhophilin-2 inhibits RhoA's activity to induce F-actin stress fibers. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This rhophilin-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467196 [Multi-domain]  Cd Length: 78  Bit Score: 56.82  E-value: 1.11e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908 1154 YGFTIRairvyvGDSDIytvhhIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNK-VSIT 1227
Cdd:cd06712     13 FGFTLR------GDSPV-----QVASVDPGSCAAEAGLKEGDYIVSVGGVDCKWSKHSEVVKLLKSAGEEgLELQ 76
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
573-787 1.18e-09

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: 62.49  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKKINKqnlILRNQIQQAFVERDI--LTFAENPFVVSMY-----CSFETRRH 645
Cdd:cd07859      2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIND---VFEHVSDATRILREIklLRLLRHPDIVEIKhimlpPSRREFKD 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGgDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSM 725
Cdd:cd07859     79 IYVVFELMES-DLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDT 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  726 TTNLyeghiekdareFLDKQVcGTPEYIAPEVI--LRQGYGKPVDWWAMGIILYEFLVGcVPFF 787
Cdd:cd07859    158 PTAI-----------FWTDYV-ATRWYRAPELCgsFFSKYTPAIDIWSIGCIFAEVLTG-KPLF 208
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
576-793 1.18e-09

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 61.71  E-value: 1.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  576 IKLISNGAYGAVYF--VRHKESRQRFAMKKINKQNLILRNQIQQAF-VERDILTFAENPFVVSMYCSFETRRHLCMVMEY 652
Cdd:cd05049     10 KRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPDARKDFeREAELLTNLQHENIVKFYGVCTEGDPLLMVFEY 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  653 VEGGDCATLMKNMGPLPVDMARMYFAETVL--------------ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS 718
Cdd:cd05049     90 MEHGDLNKFLRSHGPDAAFLASEDSAPGELtlsqllhiavqiasGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMS 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  719 KvglMSMTTNLY--EGHIEKDARefldkqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEE 793
Cdd:cd05049    170 R---DIYSTDYYrvGGHTMLPIR------------WMPPESILYRKFTTESDVWSFGVVLWEiFTYGKQPWFQLSNTE 232
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
638-780 1.59e-09

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: 61.57  E-value: 1.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  638 CSFETRRHLCMVMEYVEGGDCAT-LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFG 716
Cdd:cd14205     74 CYSAGRRNLRLIMEYLPYGSLRDyLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFG 153
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  717 LSKVglmsmttnlyeghIEKDAREFLDKQVCGTPEY-IAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd14205    154 LTKV-------------LPQDKEYYKVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYELF 205
PDZ_6 pfam17820
PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.
1176-1224 1.60e-09

PDZ domain; This entry represents the PDZ domain from a wide variety of proteins.


Pssm-ID: 436067 [Multi-domain]  Cd Length: 54  Bit Score: 55.61  E-value: 1.60e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908 1176 IVWNVEEGSPACQAGLKAGDLITHINGEPVHGLvhTEVIELLLKSGNKV 1224
Cdd:pfam17820    1 VVTAVVPGSPAERAGLRVGDVILAVNGKPVRSL--EDVARLLQGSAGES 47
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
638-799 1.82e-09

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: 61.45  E-value: 1.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  638 CSFETRRHLCMVMEYVEGGdcaTLMKNMGPLPVDMAR-MYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDF 715
Cdd:cd05080     75 CSEQGGKSLQLIMEYVPLG---SLRDYLPKHSIGLAQlLLFAQQICeGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDF 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  716 GLSKvglmsmttNLYEGHIEKDAREFLDKQVCgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFfgDTPEELF 795
Cdd:cd05080    152 GLAK--------AVPEGHEYYRVREDGDSPVF----WYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSS--QSPPTKF 217

                   ....
gi 1988312908  796 GQVI 799
Cdd:cd05080    218 LEMI 221
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
569-825 1.85e-09

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 61.58  E-value: 1.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVYF-------------VRHKESRQRFAmKKINKQNLilrnqiQQAFVerdiLTFAENPFVVS 635
Cdd:cd05108      5 KETEFKKIKVLGSGAFGTVYKglwipegekvkipVAIKELREATS-PKANKEIL------DEAYV----MASVDNPHVCR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  636 MY--CSFETRRHLCMVMEYveGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLT 713
Cdd:cd05108     74 LLgiCLTSTVQLITQLMPF--GCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKIT 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  714 DFGLSKVglmsMTTNLYEGHIEKDArefldkqvcgTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTP 791
Cdd:cd05108    152 DFGLAKL----LGAEEKEYHAEGGK----------VPiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPA 217
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1988312908  792 EElfgqvISDEINWPEKDEAPPPDAQDLITLLLR 825
Cdd:cd05108    218 SE-----ISSILEKGERLPQPPICTIDVYMIMVK 246
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
582-824 1.88e-09

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 61.12  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVyfvrhKESRQRFAMKKINKQNLILRNQIQQA-----FVERDILTFAENPFVVSM--YCSFETrrhLCMVMEYVE 654
Cdd:cd05115     15 GNFGCV-----KKGVYKMRKKQIDVAIKVLKQGNEKAvrdemMREAQIMHQLDNPYIVRMigVCEAEA---LMLVMEMAS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCAT-LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglMSMTTNLYEgh 733
Cdd:cd05115     87 GGPLNKfLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKA--LGADDSYYK-- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 iekdAREFLDKQVcgtpEYIAPEVILRQGYGKPVDWWAMGIILYEFLVgcvpfFGDTP-EELFGQVISDEINWPEKDEAP 812
Cdd:cd05115    163 ----ARSAGKWPL----KWYAPECINFRKFSSRSDVWSYGVTMWEAFS-----YGQKPyKKMKGPEVMSFIEQGKRMDCP 229
                          250
                   ....*....|..
gi 1988312908  813 PPDAQDLITLLL 824
Cdd:cd05115    230 AECPPEMYALMS 241
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
569-831 2.07e-09

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: 60.90  E-value: 2.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVY---FVRHKESRQRFAMK--KINKQNLILRNQIQQAFVERDIltfaENPFVVSM--YCSFE 641
Cdd:cd05056      4 QREDITLGRCIGEGQFGDVYqgvYMSPENEKIAVAVKtcKNCTSPSVREKFLQEAYIMRQF----DHPHIVKLigVITEN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 TrrhLCMVMEYVEGGDC-ATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKv 720
Cdd:cd05056     80 P---VWIVMELAPLGELrSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSR- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  721 glmsmttnlyegHIEKDarEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTPEELFGQV 798
Cdd:cd05056    156 ------------YMEDE--SYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRI 221
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1988312908  799 isDEINWPEKDEAPPPDAQDLITLLLRQNPLER 831
Cdd:cd05056    222 --ENGERLPMPPNCPPTLYSLMTKCWAYDPSKR 252
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
568-843 2.41e-09

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 61.00  E-value: 2.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PReSDFETIKLISNGAYGAVYFVRHKE--SRQRFAMK--KINKQNLILrnQIQQAFvERDILTFAE--NPFVVSMYCSFE 641
Cdd:cd05050      3 PR-NNIEYVRDIGQGAFGRVFQARAPGllPYEPFTMVavKMLKEEASA--DMQADF-QREAALMAEfdHPNIVKLLGVCA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 TRRHLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVL----------------------ALEYLHNYGIVHRDLKP 699
Cdd:cd05050     79 VGKPMCLLFEYMAYGDLNEFLRHRSPRAQCSLSHSTSSARKcglnplplscteqlciakqvaaGMAYLSERKFVHRDLAT 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  700 DNLLVTSMGHIKLTDFGLSKvglmsmttNLYEGHIEK-DAREFLDKQvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYE 778
Cdd:cd05050    159 RNCLVGENMVVKIADFGLSR--------NIYSADYYKaSENDAIPIR------WMPPESIFYNRYTTESDVWAYGVVLWE 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  779 -FLVGCVPFFGDTPEELFGQVISDEI-NWPEKdeaPPPDAQDLITLLLRQNPLERLGTGGAYEVKQH 843
Cdd:cd05050    225 iFSYGMQPYYGMAHEEVIYYVRDGNVlSCPDN---CPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
568-831 2.57e-09

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 60.67  E-value: 2.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESdFETIKLISNGAYGAVYFVRHKeSRQRFAMKKINKQNLilrnQIQQAFVERDILTFAENPFVVSMYcSFETRRHLC 647
Cdd:cd05067      5 PRET-LKLVERLGAGQFGEVWMGYYN-GHTKVAIKSLKQGSM----SPDAFLAEANLMKQLQHQRLVRLY-AVVTQEPIY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMGPLP------VDMArmyfAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVg 721
Cdd:cd05067     78 IITEYMENGSLVDFLKTPSGIKltinklLDMA----AQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARL- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttnlyeghIEKDarEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTPEELFgQVI 799
Cdd:cd05067    153 ------------IEDN--EYTAREGAKFPiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVI-QNL 217
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1988312908  800 SDEINWPEKDEApPPDAQDLITLLLRQNPLER 831
Cdd:cd05067    218 ERGYRMPRPDNC-PEELYQLMRLCWKERPEDR 248
PHA03247 PHA03247
large tegument protein UL36; Provisional
1814-2192 3.32e-09

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 3.32e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1814 SGPQASKTELPSPESAQSPSPSGDVRASVPpvlPSSSGKKNDTTSARELSPSSLKMNKSyllePWFLPPSRGlqnsPAVS 1893
Cdd:PHA03247  2629 PSPSPAANEPDPHPPPTVPPPERPRDDPAP---GRVSRPRRARRLGRAAQASSPPQRPR----RRAARPTVG----SLTS 2697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1894 LPDPEFKRDRKGPHPTARSPGTVMESNPQQREGSSPKHQ----------------DHTTDPKLLTCLGQNLHSPDLAR-- 1955
Cdd:PHA03247  2698 LADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPaapappavpagpatpgGPARPARPPTTAGPPAPAPPAAPaa 2777
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1956 ---PRCPLPPEASPSREKPGLRESSERGPPTARSERSAARADTCREPSMELCFPETAKTSDNSKNllsvgrthPDFYTQT 2032
Cdd:PHA03247  2778 gppRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPP--------PGPPPPS 2849
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2033 QAMEKAWAPGgktnhkdGPGEARPPPRDnsslhSAGIPCEKELGKVRRGVEPKPEALLARRSLQPPGIESEKSEKLSSFP 2112
Cdd:PHA03247  2850 LPLGGSVAPG-------GDVRRRPPSRS-----PAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2113 SLQKDgAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSP---SHASGREPGAK---PSTAEPSSSPQDPPKPV 2186
Cdd:PHA03247  2918 QPQPQ-PPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPwlgALVPGRVAVPRfrvPQPAPSREAPASSTPPL 2996

                   ....*.
gi 1988312908 2187 AAHSES 2192
Cdd:PHA03247  2997 TGHSLS 3002
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
579-787 4.76e-09

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 59.98  E-value: 4.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVR-----HKESRQRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd05092     13 LGEGAFGKVFLAEchnllPEQDKMLVAVKALKEATESARQDFQR---EAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPL-------------PVDMARMYFAETVLA--LEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLS 718
Cdd:cd05092     90 RHGDLNRFLRSHGPDakildggegqapgQLTLGQMLQIASQIAsgMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  719 KvglMSMTTNLYEghieKDAREFLDKQvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFF 787
Cdd:cd05092    170 R---DIYSTDYYR----VGGRTMLPIR------WMPPESILYRKFTTESDIWSFGVVLWEiFTYGKQPWY 226
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
645-802 4.79e-09

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: 59.98  E-value: 4.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  645 HLCMVMEYVEGGDCATLMKN-MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSmGHIKLTDFGLSKVglm 723
Cdd:cd14152     70 HLAIITSFCKGRTLYSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGI--- 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttnlyEGHIEKDAREFLDKQVCGTPEYIAPEVILRQGYG---------KPVDWWAMGIILYEFLVGCVPFFGDTPEEL 794
Cdd:cd14152    146 -------SGVVQEGRRENELKLPHDWLCYLAPEIVREMTPGkdedclpfsKAADVYAFGTIWYELQARDWPLKNQPAEAL 218

                   ....*...
gi 1988312908  795 FGQVISDE 802
Cdd:cd14152    219 IWQIGSGE 226
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
643-719 5.08e-09

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: 57.66  E-value: 5.08e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1988312908  643 RRHLCMVMEYVEGGDCATLMKNmGPLPVDMARMyfAETVLALeyLHNYGIVHRDLKPDNLLVTSmGHIKLTDFGLSK 719
Cdd:COG3642     28 PDDADLVMEYIEGETLADLLEE-GELPPELLRE--LGRLLAR--LHRAGIVHGDLTTSNILVDD-GGVYLIDFGLAR 98
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
569-825 5.14e-09

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 60.04  E-value: 5.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  569 RESDFETIKLISNGAYGAVY---FVRHKESRQRFAMKKINKQNLILRNQiQQAFVERDILTFAENPFVVSMY--CSFETR 643
Cdd:cd05109      5 KETELKKVKVLGSGAFGTVYkgiWIPDGENVKIPVAIKVLRENTSPKAN-KEILDEAYVMAGVGSPYVCRLLgiCLTSTV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYveGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglm 723
Cdd:cd05109     84 QLVTQLMPY--GCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARL--- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  724 smttnlyeghIEKDAREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVgcvpfFGDTPEELF-GQVISDE 802
Cdd:cd05109    159 ----------LDIDETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMT-----FGAKPYDGIpAREIPDL 223
                          250       260
                   ....*....|....*....|...
gi 1988312908  803 INWPEKDEAPPPDAQDLITLLLR 825
Cdd:cd05109    224 LEKGERLPQPPICTIDVYMIMVK 246
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
613-813 5.17e-09

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 60.03  E-value: 5.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  613 NQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGD---------------CATLMKNMGPLPVDMAR-MY 676
Cdd:cd05090     52 NEFQQ---EASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDlheflimrsphsdvgCSSDEDGTVKSSLDHGDfLH 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  677 FAETVLA-LEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNLYEGHIEKdarefLDKQVCGTPEYIAP 755
Cdd:cd05090    129 IAIQIAAgMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSR--------EIYSSDYYR-----VQNKSLLPIRWMPP 195
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  756 EVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELFGQVISDEInWPEKDEAPP 813
Cdd:cd05090    196 EAIMYGKFSSDSDIWSFGVVLWEiFSFGLQPYYGFSNQEVIEMVRKRQL-LPCSEDCPP 253
PDZ5_MAGI-1_3-like cd06735
PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, ...
1144-1224 5.56e-09

PDZ domain 5 of membrane-associated guanylate kinase inverted 1 (MAGI-1), MAGI-2, and MAGI-3, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain 5 of MAGI1, 2, 3 (MAGI is also known as Membrane-associated guanylate kinase, WW and PDZ domain-containing protein) and related domains. MAGI proteins have been implicated in the control of cell migration and invasion through altering the activity of phosphatase and tensin homolog (PTEN) and modulating Akt signaling. Four MAGI proteins have been identified (MAGI1-3 and MAGIX). MAGI1-3 have 6 PDZ domains and bind to the C-terminus of PTEN via their PDZ2 domain. MAGIX has a single PDZ domain that is related to MAGI1-3 PDZ domain 5, and belongs to this MAGI1,2,3-like family. Other binding partners for MAGI1 include JAM4, C-terminal tail of high risk HPV-18 E6, megalin, TRAF6, Kir4.1 (basolateral K+ channel subunit), and cadherin 23; for MAGI2, include DASM1, dendrin, axin, beta- and delta-catenin, neuroligin, hyperpolarization-activated cation channels, beta1-adrenergic receptors, NMDA receptor, and TARPs; and for MAGI3 includes LPA2. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This MAGI family PDZ5 domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged as beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467217 [Multi-domain]  Cd Length: 84  Bit Score: 55.28  E-value: 5.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1144 PIVIHSSGKNYGFTIRAIRVYvGDSDIYtvhhiVWNVEEGSPACQAG-LKAGDLITHINGEPVHGLVHTEVIELLLKSGN 1222
Cdd:cd06735      3 SVELERGPKGFGFSIRGGREY-NNMPLY-----VLRLAEDGPAQRDGrLRVGDQILEINGESTQGMTHAQAIELIRSGGS 76

                   ..
gi 1988312908 1223 KV 1224
Cdd:cd06735     77 VV 78
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
579-780 5.77e-09

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: 59.45  E-value: 5.77e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKeSRQRFAMKKINKQNlILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGG-- 656
Cdd:cd14156      1 IGSGFFSKVYKVTHG-ATGKVMVVKIYKND-VDQHKIVR---EISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGcl 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  657 -------DCATLMKNMGPLPVDMARmyfaetvlALEYLHNYGIVHRDLKPDNLLV--TSMG-HIKLTDFGLSKVgLMSMT 726
Cdd:cd14156     76 eellareELPLSWREKVELACDISR--------GMVYLHSKNIYHRDLNSKNCLIrvTPRGrEAVVTDFGLARE-VGEMP 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  727 TNLYEGHIekdarefldkQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd14156    147 ANDPERKL----------SLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
644-783 7.09e-09

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 59.66  E-value: 7.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGGD-CATLMKNMGPLPVDMAR----------MYFAETVLA-LEYLHNYGIVHRDLKPDNLLVTSMGHIK 711
Cdd:cd05051     92 EPLCMIVEYMENGDlNQFLQKHEAETQGASATnsktlsygtlLYMATQIASgMKYLESLNFVHRDLATRNCLVGPNYTIK 171
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  712 LTDFGLSKvglmsmttNLYEGHIEK-DAREFLdkqvcgtP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLVGC 783
Cdd:cd05051    172 IADFGMSR--------NLYSGDYYRiEGRAVL-------PiRWMAWESILLGKFTTKSDVWAFGVTLWEILTLC 230
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
567-800 7.96e-09

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: 58.99  E-value: 7.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  567 KPREsDFETIKLISNGAYGAVYFVRHKESRqRFAMKKINKQNLILRNQIQQafvERDILTFAENPFVVSMYCSFETRRHL 646
Cdd:cd05148      3 RPRE-EFTLERKLGSGYFGEVWEGLWKNRV-RVAIKILKSDDLLKQQDFQK---EVQALKRLRHKHLISLFAVCSVGEPV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKNMGPLPVDMARM-YFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglms 724
Cdd:cd05148     78 YIITELMEKGSLLAFLRSPEGQVLPVASLiDMACQVAeGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARL---- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  725 mttnlyeghIEKDAREFLDKQVcgtP-EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELFGQVIS 800
Cdd:cd05148    154 ---------IKEDVYLSSDKKI---PyKWTAPEAASHGTFSTKSDVWSFGILLYEmFTYGQVPYPGMNNHEVYDQITA 219
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
636-786 8.33e-09

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: 59.27  E-value: 8.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  636 MYCSFETRRHLCMVMEYVEGgdcATLMKNMGPLP--------VDMARmyfaETVLALEYLHNYGIVHRDLKPDNLLVTSM 707
Cdd:cd14149     72 LFMGYMTKDNLAIVTQWCEG---SSLYKHLHVQEtkfqmfqlIDIAR----QTAQGMDYLHAKNIIHRDMKSNNIFLHEG 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  708 GHIKLTDFGLSKVGLMSMTTNLYEghiekdarefldkQVCGTPEYIAPEVILRQG---YGKPVDWWAMGIILYEFLVGCV 784
Cdd:cd14149    145 LTVKIGDFGLATVKSRWSGSQQVE-------------QPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTGEL 211

                   ..
gi 1988312908  785 PF 786
Cdd:cd14149    212 PY 213
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
573-782 9.27e-09

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 59.77  E-value: 9.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  573 FETIKLISNGAYGAVYFVRHKESRQRFAMKkinkqnlILRNQ---IQQAFVERDILT--FAENP----FVVSMYCsFETR 643
Cdd:cd14211      1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIK-------ILKNHpsyARQGQIEVSILSrlSQENAdefnFVRAYEC-FQHK 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  644 RHLCMVMEYVEGGDCATLMKN-MGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMG----HIKLTDFGLS 718
Cdd:cd14211     73 NHTCLVFEMLEQNLYDFLKQNkFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGSA 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  719 KvglmsmttnlyegHIEkdarefldKQVCGT----PEYIAPEVILRQGYGKPVDWWAMGIILYEFLVG 782
Cdd:cd14211    153 S-------------HVS--------KAVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLG 199
PDZ_ZASP52-like cd23068
PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), ...
1176-1227 1.03e-08

PDZ domain of Drosophila melanogaster PDZ and LIM domain protein Zasp52 (also known as Zasp), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of Drosophila melanogaster Zasp52 and related domains. Drosophila melanogaster Zasp52 (also known as Z band alternatively spliced PDZ-motif protein or Zasp) colocalizes with integrins at myotendinous junctions and with alpha-actinin at Z-disks and is required for muscle attachment as well as Z-disk assembly and maintenance. The Zasp52 actin-binding site includes the extended PDZ domain and the ZM region. The Zasp52-PDZ domain is required for myofibril assembly. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This Zasp52-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467281 [Multi-domain]  Cd Length: 82  Bit Score: 54.07  E-value: 1.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908 1176 IVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKVSIT 1227
Cdd:cd23068     28 SIQKVNPGSPADKAGLRRGDVILRINGTDTSNLTHKQAQDLIKRAGNDLQLT 79
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
579-780 1.06e-08

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 59.31  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESR--QRFAMKKINKQNLILrnqiqQAFVERDILTFAENPFVVSMYCSF--ETRRHLCMVMEYVE 654
Cdd:cd07867     10 VGRGTYGHVYKAKRKDGKdeKEYALKQIEGTGISM-----SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GgDCATLMK-------NMGP--LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT----SMGHIKLTDFGLSKvg 721
Cdd:cd07867     85 H-DLWHIIKfhraskaNKKPmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFAR-- 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttnLYEGHIEKDARefLDKQVCgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFL 780
Cdd:cd07867    162 -------LFNSPLKPLAD--LDPVVV-TFWYRAPELLLgARHYTKAIDIWAIGCIFAELL 211
CtpA COG0793
C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, ...
1167-1227 1.10e-08

C-terminal processing protease CtpA/Prc, contains a PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440556 [Multi-domain]  Cd Length: 341  Bit Score: 59.50  E-value: 1.10e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1988312908 1167 DSDIYTVHHIVwnveEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLL-KSGNKVSIT 1227
Cdd:COG0793     69 EDGKVVVVSVI----PGSPAEKAGIKPGDIILAIDGKSVAGLTLDDAVKLLRgKAGTKVTLT 126
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
667-798 1.32e-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: 58.57  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  667 PLPVDMArmyfAETVLALEYL--HNYgiVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmSMTTNLYEGHIEkdAReFLDK 744
Cdd:cd05068    104 PQLIDMA----AQVASGMAYLesQNY--IHRDLAARNVLVGENNICKVADFGLARV---IKVEDEYEAREG--AK-FPIK 171
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1988312908  745 qvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTPEELFGQV 798
Cdd:cd05068    172 -------WTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQV 219
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
654-823 1.36e-08

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 59.64  E-value: 1.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMkNMGPLPVDMARMYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyeg 732
Cdd:cd05107    222 ERTRRDTLI-NESPALSYMDLVGFSYQVAnGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLAR------------- 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  733 HIEKDArEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPfFGDTP-EELFGQVI---------- 799
Cdd:cd05107    288 DIMRDS-NYISKGSTFLPlKWMAPESIFNNLYTTLSDVWSFGILLWEiFTLGGTP-YPELPmNEQFYNAIkrgyrmakpa 365
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1988312908  800 --SDEIN------WPEKDEAPPPDAQdLITLL 823
Cdd:cd05107    366 haSDEIYeimqkcWEEKFEIRPDFSQ-LVHLV 396
PDZ pfam00595
PDZ domain; PDZ domains are found in diverse signaling proteins.
1143-1227 1.50e-08

PDZ domain; PDZ domains are found in diverse signaling proteins.


Pssm-ID: 395476 [Multi-domain]  Cd Length: 81  Bit Score: 53.82  E-value: 1.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1143 QPIVIHSSGKNYGFTIrairvyVGDSDIYTVHHIVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGN 1222
Cdd:pfam00595    1 QVTLEKDGRGGLGFSL------KGGSDQGDPGIFVSEVLPGGAAEAGGLKVGDRILSINGQDVENMTHEEAVLALKGSGG 74

                   ....*
gi 1988312908 1223 KVSIT 1227
Cdd:pfam00595   75 KVTLT 79
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
646-786 1.53e-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: 58.35  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMGPLPVDMARM--YFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLM 723
Cdd:cd05083     73 LYIVMELMSKGNLVNFLRSRGRALVPVIQLlqFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSM 152
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  724 SMTTNLYeghiekdarefldkqvcgTPEYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPF 786
Cdd:cd05083    153 GVDNSRL------------------PVKWTAPEALKNKKFSSKSDVWSYGVLLWEvFSYGRAPY 198
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
568-825 2.11e-08

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: 57.73  E-value: 2.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESdFETIKLISNGAYGAVYFVRHKEsRQRFAMKKINKQNLILrnqiqQAFVER-DILTFAENPFVVSMYcSFETRRHL 646
Cdd:cd05073      9 PRES-LKLEKKLGAGQFGEVWMATYNK-HTKVAVKTMKPGSMSV-----EAFLAEaNVMKTLQHDKLVKLH-AVVTKEPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMK----NMGPLP--VDMArmyfAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKV 720
Cdd:cd05073     81 YIITEFMAKGSLLDFLKsdegSKQPLPklIDFS----AQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  721 glmsmttnlyeghIEKDarEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTPEELFgQV 798
Cdd:cd05073    157 -------------IEDN--EYTAREGAKFPiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVI-RA 220
                          250       260
                   ....*....|....*....|....*..
gi 1988312908  799 ISDEINWPEKDEAPppdaQDLITLLLR 825
Cdd:cd05073    221 LERGYRMPRPENCP----EELYNIMMR 243
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
668-831 3.10e-08

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 58.09  E-value: 3.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  668 LPVDMARM--YFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttNLYEG--HIEK-DAREFL 742
Cdd:cd14207    175 RPLTMEDLisYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLAR--------DIYKNpdYVRKgDARLPL 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  743 dkqvcgtpEYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPFFGDTPEELFGQVISDEINWPEKDEAPPPDAQDLIT 821
Cdd:cd14207    247 --------KWMAPESIFDKIYSTKSDVWSYGVLLWEiFSLGASPYPGVQIDEDFCSKLKEGIRMRAPEFATSEIYQIMLD 318
                          170
                   ....*....|
gi 1988312908  822 lLLRQNPLER 831
Cdd:cd14207    319 -CWQGDPNER 327
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
673-784 3.24e-08

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 57.12  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  673 ARMYFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMsmttnlyeghiekdarefLDKQVCGTPE 751
Cdd:cd13975    103 ERLQIALDVVeGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAM------------------MSGSIVGTPI 164
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1988312908  752 YIAPEViLRQGYGKPVDWWAMGIILYEFLVGCV 784
Cdd:cd13975    165 HMAPEL-FSGKYDNSVDVYAFGILFWYLCAGHV 196
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
579-780 3.42e-08

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 58.15  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAVYFVRHKESR--QRFAMKKINKQNLILrnqiqQAFVERDILTFAENPFVVSMYCSFETR--RHLCMVMEYVE 654
Cdd:cd07868     25 VGRGTYGHVYKAKRKDGKddKDYALKQIEGTGISM-----SACREIALLRELKHPNVISLQKVFLSHadRKVWLLFDYAE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GgDCATLMK-------NMGP--LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVT----SMGHIKLTDFGLSKvg 721
Cdd:cd07868    100 H-DLWHIIKfhraskaNKKPvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFAR-- 176
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttnLYEGHIEKDARefLDKQVCgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFL 780
Cdd:cd07868    177 -------LFNSPLKPLAD--LDPVVV-TFWYRAPELLLgARHYTKAIDIWAIGCIFAELL 226
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
591-785 3.59e-08

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 57.41  E-value: 3.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  591 RHKESRQRFAMKKINKQNlilRNQIQQAFVER-----DILTFAENPFVVSmYCSFETRRH--LCMVMEYVEggdcATLM- 662
Cdd:cd14001     23 RGGSSRSPWAVKKINSKC---DKGQRSLYQERlkeeaKILKSLNHPNIVG-FRAFTKSEDgsLCLAMEYGG----KSLNd 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  663 -------KNMGPLPVDMARMYFAETVLALEYLHNYG-IVHRDLKPDNLLVTS-MGHIKLTDFGLSkvglMSMTTNLyEGH 733
Cdd:cd14001     95 lieeryeAGLGPFPAATILKVALSIARALEYLHNEKkILHGDIKSGNVLIKGdFESVKLCDFGVS----LPLTENL-EVD 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1988312908  734 IEKDArefldkQVCGTPEYIAPEVILRqgyGKPV----DWWAMGIILYEFLVGCVP 785
Cdd:cd14001    170 SDPKA------QYVGTEPWKAKEALEE---GGVItdkaDIFAYGLVLWEMMTLSVP 216
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
621-842 3.61e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 57.36  E-value: 3.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  621 ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEGGDCATLMKNMGPLPVDMAR------------MYFAETVLA-LEYL 687
Cdd:cd05093     57 EAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEgnrpaeltqsqmLHIAQQIAAgMVYL 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  688 HNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglMSMTTNLYE--GHIEKDARefldkqvcgtpeYIAPEVILRQGYGK 765
Cdd:cd05093    137 ASQHFVHRDLATRNCLVGENLLVKIGDFGMSR---DVYSTDYYRvgGHTMLPIR------------WMPPESIMYRKFTT 201
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908  766 PVDWWAMGIILYE-FLVGCVPFFGDTPEELFGQVISDEInwPEKDEAPPPDAQDLITLLLRQNPLERLGTGGAYEVKQ 842
Cdd:cd05093    202 ESDVWSLGVVLWEiFTYGKQPWYQLSNNEVIECITQGRV--LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQ 277
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
572-786 3.96e-08

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: 56.91  E-value: 3.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  572 DFETIKLISNGAYGAVYFVRHKESRqrFAMKKINKqnlilrNQIQQAFV-ERDILT-FAENPFVVSMYCSFETRRHLCMV 649
Cdd:cd05082      7 ELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCIKN------DATAQAFLaEASVMTqLRHSNLVQLLGVIVEEKGGLYIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  650 MEYVEGGDCATLMKNMGPLPVDMARM-YFAETVL-ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmtt 727
Cdd:cd05082     79 TEYMAKGSLVDYLRSRGRSVLGGDCLlKFSLDVCeAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK-------- 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  728 nlyEGHIEKDAREFLDKqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPF 786
Cdd:cd05082    151 ---EASSTQDTGKLPVK-------WTAPEALREKKFSTKSDVWSFGILLWEiYSFGRVPY 200
cpPDZ_CPP-like cd06782
circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, ...
1176-1227 4.81e-08

circularly permuted PDZ domain of C-terminal processing peptidase (CPP), a serine protease, and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of CPP (also known as tail-specific protease, PRC protein, Protease Re, and Photosystem II D1 protein processing peptidase), and related domains. CPP belongs to the peptidase S41A family. It cleaves a C-terminal 11 residue peptide from the precursor form of penicillin-binding protein 3, and may have a role in protecting bacterium from thermal and osmotic stresses. In the plant chloroplast, the enzyme removes the C-terminal extension of the D1 polypeptide of photosystem II. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains and as well as those with circular permutations and domain swapping of beta-strands. The canonical PDZ domain contains six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2); arranged as A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F. This CPP-like PDZ domain is a circularly permuted PDZ domain which places beta-strand A on the C-terminus. Another permutation exists in the PDZ superfamily which places both beta-strands A and B on the C-terminus.


Pssm-ID: 467623 [Multi-domain]  Cd Length: 88  Bit Score: 52.49  E-value: 4.81e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1988312908 1176 IVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLL-KSGNKVSIT 1227
Cdd:cd06782     17 VVVSPIPGGPAEKAGIKPGDVIVAVDGESVRGMSLDEVVKLLRgPKGTKVKLT 69
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
579-825 5.75e-08

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 56.59  E-value: 5.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  579 ISNGAYGAV---YFVRHKESRQRFAMKKInKQNLILRNQiQQAFVERDILTFAENPFVVSMY--CSFETrrhLCMVMEYV 653
Cdd:cd05060      3 LGHGNFGSVrkgVYLMKSGKEVEVAVKTL-KQEHEKAGK-KEFLREASVMAQLDHPCIVRLIgvCKGEP---LMLVMELA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttnlyegh 733
Cdd:cd05060     78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRA------------- 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEKDAREFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLVgcvpfFGDTP-EELFGQVISDEINWPEKDEA 811
Cdd:cd05060    145 LGAGSDYYRATTAGRWPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFS-----YGAKPyGEMKGPEVIAMLESGERLPR 219
                          250
                   ....*....|....
gi 1988312908  812 PPPDAQDLITLLLR 825
Cdd:cd05060    220 PEECPQEIYSIMLS 233
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
582-793 6.46e-08

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 56.61  E-value: 6.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  582 GAYGAVYF-----VRHKESRQRFAMKKINKQNLIlrnQIQQAFV-ERDILTFAENPFVVSMYCSFETRRHLCMVMEYVEG 655
Cdd:cd05048     16 GAFGKVYKgellgPSSEESAISVAIKTLKENASP---KTQQDFRrEAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMAH 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  656 GDCATLMKNMGP-----------------LPVDMarMYFAETVLA-LEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGL 717
Cdd:cd05048     93 GDLHEFLVRHSPhsdvgvssdddgtasslDQSDF--LHIAIQIAAgMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  718 SKVGLMSmttnlyeghiekDAREFLDKQVcgTP-EYIAPEVILrqgYGK---PVDWWAMGIILYE-FLVGCVPFFGDTPE 792
Cdd:cd05048    171 SRDIYSS------------DYYRVQSKSL--LPvRWMPPEAIL---YGKfttESDVWSFGVVLWEiFSYGLQPYYGYSNQ 233

                   .
gi 1988312908  793 E 793
Cdd:cd05048    234 E 234
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
664-848 6.46e-08

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 56.56  E-value: 6.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  664 NMGPLPVDMA--RMYFAET-------VLALEYLHNY-GIVHRDLKPDNLLVTSMGHIKLTDFGLSkvGLMSMTTNLYEGH 733
Cdd:cd14011     98 NMPSPPPELQdyKLYDVEIkygllqiSEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFC--ISSEQATDQFPYF 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEKDAREFLDKQVcgTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFF-----GDTPEELFGQVISDEINwpeK 808
Cdd:cd14011    176 REYDPNLPPLAQP--NLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFdcvnnLLSYKKNSNQLRQLSLS---L 250
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1988312908  809 DEAPPPDAQDLITLLLRQNPLERLgtgGAYEVKQHRFFRS 848
Cdd:cd14011    251 LEKVPEELRDHVKTLLNVTPEVRP---DAEQLSKIPFFDD 287
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
683-826 7.25e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 57.60  E-value: 7.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  683 ALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTNLYEGhiekdarefldkqVCGTPEYIAPEVILRQG 762
Cdd:PHA03211   272 AIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARGSWSTPFHYG-------------IAGTVDTNAPEVLAGDP 338
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1988312908  763 YGKPVDWWAMGIILYEFLVGCVPFFgdtpeelfgqvisdeiNWPEKDEAPPPDAQdlITLLLRQ 826
Cdd:PHA03211   339 YTPSVDIWSAGLVIFEAAVHTASLF----------------SASRGDERRPYDAQ--ILRIIRQ 384
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
577-804 9.39e-08

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: 56.14  E-value: 9.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQR---FAMKKI-------NKQNLILRNQIQQAFVERDILTFAEnpfVVSMYcsfetrRHL 646
Cdd:cd05063     11 KVIGAGEFGEVFRGILKMPGRKevaVAIKTLkpgytekQRQDFLSEASIMGQFSHHNIIRLEG---VVTKF------KPA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  647 CMVMEYVEGGDCATLMKN----MGPLP-VDMARMYFAetvlALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVg 721
Cdd:cd05063     82 MIITEYMENGALDKYLRDhdgeFSSYQlVGMLRGIAA----GMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRV- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttnlyeghIEKDAREFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLVgcvpfFGDTPE-ELFGQVI 799
Cdd:cd05063    157 ------------LEDDPEGTYTTSGGKIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEVMS-----FGERPYwDMSNHEV 219

                   ....*
gi 1988312908  800 SDEIN 804
Cdd:cd05063    220 MKAIN 224
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
648-831 9.55e-08

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: 55.69  E-value: 9.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKN-MG-----PLPVDMArmyfAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVg 721
Cdd:cd14203     66 IVTEFMSKGSLLDFLKDgEGkylklPQLVDMA----AQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARL- 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  722 lmsmttnlyeghIEKDarEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTPEELFGQVi 799
Cdd:cd14203    141 ------------IEDN--EYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV- 205
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1988312908  800 SDEINWPEKDEApPPDAQDLITLLLRQNPLER 831
Cdd:cd14203    206 ERGYRMPCPPGC-PESLHELMCQCWRKDPEER 236
DegQ COG0265
Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational ...
1176-1227 1.07e-07

Periplasmic serine protease, S1-C subfamily, contain C-terminal PDZ domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440035 [Multi-domain]  Cd Length: 274  Bit Score: 55.93  E-value: 1.07e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1988312908 1176 IVWNVEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKVSIT 1227
Cdd:COG0265    204 LVARVEPGSPAAKAGLRPGDVILAVDGKPVTSARDLQRLLASLKPGDTVTLT 255
PDZ_2 pfam13180
PDZ domain;
1176-1227 1.51e-07

PDZ domain;


Pssm-ID: 433015 [Multi-domain]  Cd Length: 74  Bit Score: 50.73  E-value: 1.51e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1988312908 1176 IVWNVEEGSPACQAGLKAGDLITHINGEPVHGLvhTEVIELLL--KSGNKVSIT 1227
Cdd:pfam13180    9 VVVSVKSSGPAAKAGLKAGDVILSIDGRKINDL--TDLESALYghKPGDTVTLQ 60
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
571-786 1.60e-07

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: 54.96  E-value: 1.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  571 SDFETIKLISNGAYGAVYFVRHKESRQrFAMKKINKQNLILRNQIQQAfverDILTFAENPFVVSMYCSFETRRHLCMVM 650
Cdd:cd05112      4 SELTFVQEIGSGQFGLVHLGYWLNKDK-VAIKTIREGAMSEEDFIEEA----EVMMKLSHPKLVQLYGVCLEQAPICLVF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  651 EYVEGGdCAT--LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVGLMSMTTN 728
Cdd:cd05112     79 EFMEHG-CLSdyLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTS 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  729 lyeghieKDAREFLDKqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCVPF 786
Cdd:cd05112    158 -------STGTKFPVK-------WSSPEVFSFSRYSSKSDVWSFGVLMWEvFSEGKIPY 202
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
621-722 1.67e-07

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 57.27  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  621 ERDILTFAENPFVVSMYCsfETRR---HLCMVMEYVEGGDCATLMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDL 697
Cdd:NF033442   556 EAEVLGRLRHPRIVALVE--GPLEiggRTALLLEYAGEQTLAERLRKEGRLSLDLLERFGDDLLSAVVHLEGQGVWHRDI 633
                           90       100
                   ....*....|....*....|....*....
gi 1988312908  698 KPDNLLVTSMG----HIKLTDFGLSKVGL 722
Cdd:NF033442   634 KPDNIGIRPRPsrtlHLVLFDFSLAGAPA 662
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
568-798 1.74e-07

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: 55.07  E-value: 1.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  568 PRESdFETIKLISNGAYGAVYfVRHKESRQRFAMKKINKQNLILRNQIQQAfverDILTFAENPFVVSMYcSFETRRHLC 647
Cdd:cd05070      7 PRES-LQLIKRLGNGQFGEVW-MGTWNGNTKVAIKTLKPGTMSPESFLEEA----QIMKKLKHDKLVQLY-AVVSEEPIY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  648 MVMEYVEGGDCATLMKNMG------PLPVDMArmyfAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVg 721
Cdd:cd05070     80 IVTEYMSKGSLLDFLKDGEgralklPNLVDMA----AQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARL- 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1988312908  722 lmsmttnlyeghIEKDarEFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDTPEELFGQV 798
Cdd:cd05070    155 ------------IEDN--EYTARQGAKFPiKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 219
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
646-795 1.89e-07

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: 55.41  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  646 LCMVMEYVEGGDCATLMKNMGPLPV----DMAR-----MYFAETV-------LALEYLHNYGIVHRDLKPDNLLVTSMGH 709
Cdd:cd05101    105 LYVIVEYASKGNLREYLRARRPPGMeysyDINRvpeeqMTFKDLVsctyqlaRGMEYLASQKCIHRDLAARNVLVTENNV 184
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  710 IKLTDFGLSK----VGLMSMTTNlyeGHIEKdarefldkqvcgtpEYIAPEVILRQGYGKPVDWWAMGIILYE-FLVGCV 784
Cdd:cd05101    185 MKIADFGLARdinnIDYYKKTTN---GRLPV--------------KWMAPEALFDRVYTHQSDVWSFGVLMWEiFTLGGS 247
                          170
                   ....*....|.
gi 1988312908  785 PFFGDTPEELF 795
Cdd:cd05101    248 PYPGIPVEELF 258
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
577-824 1.89e-07

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 54.88  E-value: 1.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKE--SRQRFAMKKINKQNLILRnQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYVE 654
Cdd:cd05065     10 EVIGAGEFGEVCRGRLKLpgKREIFVAIKTLKSGYTEK-QRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFME 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  655 GGDCATLMK-NMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKvglmsmttnlyegH 733
Cdd:cd05065     89 NGALDSFLRqNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSR-------------F 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  734 IEKDARE--FLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEflvgcVPFFGDTPE-ELFGQvisDEINWPEKD 809
Cdd:cd05065    156 LEDDTSDptYTSSLGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWE-----VMSYGERPYwDMSNQ---DVINAIEQD 227
                          250
                   ....*....|....*..
gi 1988312908  810 E--APPPDAQDLITLLL 824
Cdd:cd05065    228 YrlPPPMDCPTALHQLM 244
PDZ_SYNPO2-like cd10820
PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related ...
1180-1226 1.93e-07

PDZ domain of synaptopodin 2 (SYNPO2), synaptopodin 2-like protein (SYNPO2L), and related domains; PDZ (PSD-95 (Postsynaptic density protein 95), Dlg (Discs large protein), and ZO-1 (Zonula occludens-1)) domain of SYNPO2, SYNPO2L, and related domains. SYNPO2 (also known as genethonin-2, myopodin) is a cytoskeleton adaptor protein. It participates in chaperone-assisted selective autophagy (CASA), a mechanism for the disposal of misfolded and damaged proteins and provides a link between the CASA chaperone complex and a membrane-tethering and fusion machinery that generates autophagosome membranes. The SYNPO2 PPxY motif binds CASA cochaperone BCL2-associated athanogene 3 (BAG3) and the SYNPO2 PDZ domain binds vacuolar protein sorting 18 homolog (VPS18). There are three isoforms of SYNPO2, which possess an amino-terminal PDZ domain (SYNPO2a, b, c); the short isoform SYNPO2d, lacks the PDZ domain. PDZ domains usually bind in a sequence-specific manner to short peptide sequences located at the C-terminal end of their partner proteins (known as PDZ binding motifs). The PDZ superfamily includes canonical PDZ domains as well as those with circular permutations and domain swapping mediated by beta-strands. This SYNPO2-like family domain is a canonical PDZ domain containing six beta-strands A-F and two alpha-helices (alpha-helix 1 and 2), arranged in the order: beta-strands A, B, C, alpha-helix 1, beta-strands D, E, alpha-helix 2 and beta-strand F.


Pssm-ID: 467264 [Multi-domain]  Cd Length: 78  Bit Score: 50.38  E-value: 1.93e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1988312908 1180 VEEGSPACQAGLKAGDLITHINGEPVHGLVHTEVIELLLKSGNKVSI 1226
Cdd:cd10820     29 IRKKSKAALAGLCEGDELLSINGKPCADLSHSEAMDLIDSSGDTLQL 75
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
570-825 2.85e-07

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 54.54  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  570 ESDFETIKLISNGAYGAVYFVRHKE---SRQRFAMKKInKQNLILRNQIQQAFVERDILTFAENPFV-----VSMYCSFE 641
Cdd:cd05074      8 EQQFTLGRMLGKGEFGSVREAQLKSedgSFQKVAVKML-KADIFSSSDIEEFLREAACMKEFDHPNVikligVSLRSRAK 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  642 TRRHLCMV-MEYVEGGDCAT--LMKNMGP----LPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTD 714
Cdd:cd05074     87 GRLPIPMViLPFMKHGDLHTflLMSRIGEepftLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVAD 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  715 FGLSKvglmsmttNLYEGHIEkdarefldKQVCGTP---EYIAPEVILRQGYGKPVDWWAMGIILYEFLV-GCVPFFGDT 790
Cdd:cd05074    167 FGLSK--------KIYSGDYY--------RQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVE 230
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1988312908  791 PEELFGQVISDeinwpEKDEAPPPDAQDLITLLLR 825
Cdd:cd05074    231 NSEIYNYLIKG-----NRLKQPPDCLEDVYELMCQ 260
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
577-780 3.71e-07

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 54.10  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  577 KLISNGAYGAVYFVRHKESRQR---FAMKKINKQnlILRNQIQQAFVERDILTFAENPFVVSMYCSFETRRHLCMVMEYV 653
Cdd:cd05066     10 KVIGAGEFGEVCSGRLKLPGKReipVAIKTLKAG--YTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYM 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908  654 EGGDCAT-LMKNMGPLPVDMARMYFAETVLALEYLHNYGIVHRDLKPDNLLVTSMGHIKLTDFGLSKVglmsmttnlyeg 732
Cdd:cd05066     88 ENGSLDAfLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRV------------ 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1988312908  733 hIEKDAREFLDKQVCGTP-EYIAPEVILRQGYGKPVDWWAMGIILYEFL 780
Cdd:cd05066    156 -LEDDPEAAYTTRGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEVM 203
PHA03247 PHA03247
large tegument protein UL36; Provisional
1897-2365 3.80e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 56.10  E-value: 3.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1897 PEFKR--DRKGPHPTARSPGTVMESNPQQREGSSPKHQ------DHTT----DPKLLTCLG--QNLHSPDLARPRCPLPP 1962
Cdd:PHA03247  2478 PVYRRpaEARFPFAAGAAPDPGGGGPPDPDAPPAPSRLapailpDEPVgepvHPRMLTWIRglEELASDDAGDPPPPLPP 2557
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1963 EASP---------SREKP-------GLRESSERGPP-TARSERSAARADTCREPSMELCFPETAKTSDNSKnllSVGRTH 2025
Cdd:PHA03247  2558 AAPPaapdrsvppPRPAPrpsepavTSRARRPDAPPqSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPP---PSPSPA 2634
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2026 PdfyTQTQAMEKAWAPGGKTNHKDGPGEARPPPRDNSSLHSAGIPCEKELGKVRRGVEPK--PEALLARRSLQPPGIESE 2103
Cdd:PHA03247  2635 A---NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTvgSLTSLADPPPPPPTPEPA 2711
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2104 KSEKLS-------------SFPSLQKDGAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSPSHASGREPGAKP 2170
Cdd:PHA03247  2712 PHALVSatplppgpaaarqASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASL 2791
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2171 STAEPSS-SPQDPPKPVAAHSESSSHKPRPGPDPGPPKTkhpdrSLSSQKPSVGATKGKEPATQSLGGSSREGKGHSKSG 2249
Cdd:PHA03247  2792 SESRESLpSPWDPADPPAAVLAPAAALPPAASPAGPLPP-----PTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRP 2866
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2250 PDVFPAT--------PGSQNKASDGIGQGEGGPSVPLHTDRAPLDAKPQPTSGGRPLEVLEKPVHLPR-PGHPGPSEPAD 2320
Cdd:PHA03247  2867 PSRSPAAkpaaparpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPpPPRPQPPLAPT 2946
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1988312908 2321 QKLSAVGEKqtlSPKHPKPSTVKDCPTLCKQTDNRQTDKSPSQPA 2365
Cdd:PHA03247  2947 TDPAGAGEP---SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREA 2988
PHA03247 PHA03247
large tegument protein UL36; Provisional
1816-2235 7.24e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 7.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1816 PQASKTELPSPESAQSPS-PSGDVRASVPPVLPSSSGKK----NDTTSARELSPSSLKMNKSYLLEPWFLPPSRGLQNSP 1890
Cdd:PHA03247  2561 PAAPDRSVPPPRPAPRPSePAVTSRARRPDAPPQSARPRapvdDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDP 2640
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1891 AVSLPDPEFKRDRKGPHPT-------ARSPG-TVMESNPQQR---------------------EGSSPKHQDHTTDPKLL 1941
Cdd:PHA03247  2641 HPPPTVPPPERPRDDPAPGrvsrprrARRLGrAAQASSPPQRprrraarptvgsltsladpppPPPTPEPAPHALVSATP 2720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1942 TCLG-QNLHSPDLARPRCPLPPEASPSREKPGLRESSERGPPTARSERSAARADTCREPSMELCFPETAKTSDNSKNLLS 2020
Cdd:PHA03247  2721 LPPGpAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPS 2800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2021 --------VGRTHPDFYTQTQAMEKAWAPGGKTNHKDGPGEARPPPRDNSSLHSAGIPCekelGKVRRGVEPKPEALL-- 2090
Cdd:PHA03247  2801 pwdpadppAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPG----GDVRRRPPSRSPAAKpa 2876
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2091 ------ARRSLQPPGIESEKSEKL--SSFPSLQKDGAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSPSHAS 2162
Cdd:PHA03247  2877 aparppVRRLARPAVSRSTESFALppDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPS 2956
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1988312908 2163 GREPGAKPSTAEPSSSP-----QDPPKPVAAHSESSSHkprpgpdpgpPKTKHPDRSLSSQKPSVGATKGKEPATQSL 2235
Cdd:PHA03247  2957 GAVPQPWLGALVPGRVAvprfrVPQPAPSREAPASSTP----------PLTGHSLSRVSSWASSLALHEETDPPPVSL 3024
PHA03247 PHA03247
large tegument protein UL36; Provisional
1722-2194 2.20e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 50.32  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1722 PGNPVRPTGGQQEPPPASESRAFVSSTHAAQMSAVSFVPLKALTGRVDSGTEKPGLVAPESPVRKspseyklEGRSVSCL 1801
Cdd:PHA03247  2605 RGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARR-------LGRAAQAS 2677
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1802 KPIEGTLDIALLS--GPQASKTELPSPESAQSPSPSGDVRASVPPVLPSSSGKKNDTTSARELSPSSlkMNKSYLLEPWF 1879
Cdd:PHA03247  2678 SPPQRPRRRAARPtvGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAV--PAGPATPGGPA 2755
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1880 LPPSRGLQNSPAVSLPdpefKRDRKGPHPTARSPGTVMESNPQQREGSSPKHQDHTTDPklltCLGQNLHSPDLARPRCP 1959
Cdd:PHA03247  2756 RPARPPTTAGPPAPAP----PAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA----VLAPAAALPPAASPAGP 2827
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 1960 LPP-----EASPSREKPGLRES-------------SERGPPTARSERSAARAdtcREPSMELCFPETAKTSDNSKNLLSV 2021
Cdd:PHA03247  2828 LPPptsaqPTAPPPPPGPPPPSlplggsvapggdvRRRPPSRSPAAKPAAPA---RPPVRRLARPAVSRSTESFALPPDQ 2904
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2022 GRTHPDFYTQTQAMEKAWAPGGKTNHKDGPGEARPPPRDNSSLHSAGIPCEKELGKVRRGVEPKPEALLARRSLQPPGIE 2101
Cdd:PHA03247  2905 PERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2102 SEKSEKlSSFPSLQKDGAKEPERKEQPLQRHPSSIPPPPLTAKDLSSPAARQHCSSPS---------HASGREPGAKPST 2172
Cdd:PHA03247  2985 SREAPA-SSTPPLTGHSLSRVSSWASSLALHEETDPPPVSLKQTLWPPDDTEDSDADSlfdsdsersDLEALDPLPPEPH 3063
                          490       500
                   ....*....|....*....|..
gi 1988312908 2173 aEPSSSPQDPPKPVAAHSESSS 2194
Cdd:PHA03247  3064 -DPFAHEPDPATPEAGARESPS 3084
PHA03247 PHA03247
large tegument protein UL36; Provisional
2138-2437 3.65e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.47  E-value: 3.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2138 PPPLTAKDLSSPAARQHCSSPSHA-SGREPGAKPSTAEPSSSPQdPPKPVAAHSESSSHKPRPGPDPGPPKTKHPDRSLS 2216
Cdd:PHA03247  2551 PPPPLPPAAPPAAPDRSVPPPRPApRPSEPAVTSRARRPDAPPQ-SARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPP 2629
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2217 SQKPSVGATKGKEPATQSLGGSSREGKGHSKSGPDVFPATPGSQNKASDGIgQGEGGPSVPLHTdrAPLDAKPQPTSGGR 2296
Cdd:PHA03247  2630 SPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPP-QRPRRRAARPTV--GSLTSLADPPPPPP 2706
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1988312908 2297 PLEvlekpvhlPRPGHPGPSEPADQKLSAVGEKQTLSPKHPKPSTVKDCPTLCKQTDNRQTDKSPSQPAANTDRRAEGKK 2376
Cdd:PHA03247  2707 TPE--------PAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1988312908 2377 CTEALYAPAEGDKLEAGLSFVHSENrlkGAERPAAGVGKGFPEARGKGPGPQKPPTEADKP 2437
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWD---PADPPAAVLAPAAALPPAASPAGPLPPPTSAQP 2836
 
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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