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Conserved domains on  [gi|15233564|ref|NP_194667|]
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protein kinase family protein / WD-40 repeat family protein [Arabidopsis thaliana]

Protein Classification

STKc_Vps15 and WD40 domain-containing protein (domain architecture ID 12991011)

STKc_Vps15 and WD40 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
16-303 1.51e-166

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


:

Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 501.01  E-value: 1.51e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   16 YYLHDLPssynlvlkevLGRGRFLKSIQCKHDEGLVVVKVYFKRGDSIDLREYERRLVKIKDVFLslEHPHVWPFQFWQE 95
Cdd:cd13980    1 DYLYDKS----------LGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLL--ELPNVLPFQKVIE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   96 TDKAAYLVRQYFYSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPTY 175
Cdd:cd13980   69 TDKAAYLIRQYVKYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPTY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  176 IPYDDPSDFSFFFDTRGQRLCYLAPERFYEHGGETQ--VAQDAPLKPSMDIFAVGCVIAELFLEGQPLFELAQLLAYRRG 253
Cdd:cd13980  149 LPEDNPADFSYFFDTSRRRTCYIAPERFVDALTLDAesERRDGELTPAMDIFSLGCVIAELFTEGRPLFDLSQLLAYRKG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15233564  254 QHDPSQHLEKIPDPGIRKMILHMIQLEPEARLSAEDYLQNYVGVVFPNYF 303
Cdd:cd13980  229 EFSPEQVLEKIEDPNIRELILHMIQRDPSKRLSAEDYLKKYRGKVFPEYF 278
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1071-1325 1.89e-17

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 356469 [Multi-domain]  Cd Length: 289  Bit Score: 84.31  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1071 GVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWDSRKLEkdisfrsrLTYHLEGSRGMCTTM-LRNSTQVVVGAS 1149
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE--------CVRTLTGHTSYVSSVaFSPDGRILSSSS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1150 -DGVIHMFSidhisrglgnvVEKYSGIVDIK--KKDVKEGALvsllnytadSLSGPMVMYSTQNCGIHLWDTRSDLDAWT 1226
Cdd:cd00200  113 rDKTIKVWD-----------VETGKCLTTLRghTDWVNSVAF---------SPDGTFVASSSQDGTIKLWDLRTGKCVAT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1227 LKAnpEEGYVSSLVTSPCGNWFVSGSSRGVLTLWDLRFRVPVNSWQY---PIicpiekMCLCFLPPSvsvsttmkpliYV 1303
Cdd:cd00200  173 LTG--HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhenGV------NSVAFSPDG-----------YL 233
                        250       260
                 ....*....|....*....|....*
gi 15233564 1304 AAGCNE---VSLWNAEGGSCHQVLR 1325
Cdd:cd00200  234 LASGSEdgtIRVWDLRTGECVQTLS 258
 
Name Accession Description Interval E-value
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
16-303 1.51e-166

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 501.01  E-value: 1.51e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   16 YYLHDLPssynlvlkevLGRGRFLKSIQCKHDEGLVVVKVYFKRGDSIDLREYERRLVKIKDVFLslEHPHVWPFQFWQE 95
Cdd:cd13980    1 DYLYDKS----------LGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLL--ELPNVLPFQKVIE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   96 TDKAAYLVRQYFYSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPTY 175
Cdd:cd13980   69 TDKAAYLIRQYVKYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPTY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  176 IPYDDPSDFSFFFDTRGQRLCYLAPERFYEHGGETQ--VAQDAPLKPSMDIFAVGCVIAELFLEGQPLFELAQLLAYRRG 253
Cdd:cd13980  149 LPEDNPADFSYFFDTSRRRTCYIAPERFVDALTLDAesERRDGELTPAMDIFSLGCVIAELFTEGRPLFDLSQLLAYRKG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15233564  254 QHDPSQHLEKIPDPGIRKMILHMIQLEPEARLSAEDYLQNYVGVVFPNYF 303
Cdd:cd13980  229 EFSPEQVLEKIEDPNIRELILHMIQRDPSKRLSAEDYLKKYRGKVFPEYF 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
29-292 8.00e-30

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 119.56  E-value: 8.00e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564      29 LKEVLGRGRFLKSIQCKH--DEGLVVVKVyFKRGDSIDLREYERRLVKIkdvFLSLEHPHVWPFQFWQETDKAAYLVRQY 106
Cdd:smart00220    3 ILEKLGEGSFGKVYLARDkkTGKLVAIKV-IKKKKIKKDRERILREIKI---LKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564     107 F-YSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF--ASFkptyipYDDPSD 183
Cdd:smart00220   79 CeGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFglARQ------LDPGEK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564     184 FSFFFDTRgqrlCYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELfLEGQPLF--ELAQLLAYRR---GQHDPS 258
Cdd:smart00220  153 LTTFVGTP----EYMAPE----------VLLGKGYGKAVDIWSLGVILYEL-LTGKPPFpgDDQLLELFKKigkPKPPFP 217
                           250       260       270
                    ....*....|....*....|....*....|....
gi 15233564     259 QHLEKIPDPGIRkMILHMIQLEPEARLSAEDYLQ 292
Cdd:smart00220  218 PPEWDISPEAKD-LIRKLLVKDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
27-292 6.50e-25

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 105.40  E-value: 6.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564     27 LVLKEVLGRGRFLKSIQCKHDE--GLVVVKVYFKRGDSIDLREYERRLVKIkdvFLSLEHPHVWPFQFWQETDKAAYLVR 104
Cdd:pfam00069    1 YEVLEKLGEGSFGTVYKAKHKDtgKIVAIKKIKKEKIKKKKEKNVLREIKI---LKKLSHPNIVRLYDVFEDKDHLYLVL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564    105 QYF-YSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF--ASFkptyipYDDP 181
Cdd:pfam00069   78 EYVeGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFglAKQ------LSSG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564    182 SDFSFFFDTRGqrlcYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELfLEGQPLFELA-----QLLAYRRGQHD 256
Cdd:pfam00069  152 SKLTTFVGTPW----YMAPE----------VLGGNPYGPKVDVWSLGCILYEL-LTGKPPFPGIngddiYELILDQLERI 216
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 15233564    257 PSQ----HLEKIPDPGIrKMILHMIQLEPEARLSAEDYLQ 292
Cdd:pfam00069  217 PEDfsspFPSSLSEEAK-DLLKKLLKKDPSKRLTATQALQ 255
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
24-402 3.19e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 88.65  E-value: 3.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   24 SYNLVlkEVLGRGRFLKSIQCKHDEgLVVVKVYFKrgDSIDLREYERRLVKIKDVFLSLEHPHVWP-FQFWQETDKAAYL 102
Cdd:COG0515    1 SYRIL--RKLGEGSFGEVYLARDRK-LVALKVLAK--KLESKSKEVERFLREIQILASLNHPPNIVkLYDFFQDEGSLYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  103 VRQYF----YSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSW-NWLYLADFASFKpTYIP 177
Cdd:COG0515   76 VMEYVdggsLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAK-LLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  178 YDDPSDFSFFFDTRGQRLCYLAPERFyehggetQVAQDAPLKPSMDIFAVGCVIAELfLEGQPLFELAQL---------- 247
Cdd:COG0515  155 PGSTSSIPALPSTSVGTPGYMAPEVL-------LGLSLAYASSSSDIWSLGITLYEL-LTGLPPFEGEKNssatsqtlki 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  248 ---LAYRRGQHDPSQHLEKIPDPGIRKMILHMIQLEPEARLSAEDYLQNYVGVVFPNYFSPFLHTLYccWNPLPSDMRVA 324
Cdd:COG0515  227 ileLPTPSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLK--PDDSAPLRLSL 304
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233564  325 TCQGIFQEILKKMMENKSGDEIGVDSPVTSNPMNASTVQETFANHKLNSSKDLIRNTVNSKDEIFYSISDALKKNRHP 402
Cdd:COG0515  305 PPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSSSSRQQ 382
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1071-1325 1.89e-17

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 84.31  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1071 GVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWDSRKLEkdisfrsrLTYHLEGSRGMCTTM-LRNSTQVVVGAS 1149
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE--------CVRTLTGHTSYVSSVaFSPDGRILSSSS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1150 -DGVIHMFSidhisrglgnvVEKYSGIVDIK--KKDVKEGALvsllnytadSLSGPMVMYSTQNCGIHLWDTRSDLDAWT 1226
Cdd:cd00200  113 rDKTIKVWD-----------VETGKCLTTLRghTDWVNSVAF---------SPDGTFVASSSQDGTIKLWDLRTGKCVAT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1227 LKAnpEEGYVSSLVTSPCGNWFVSGSSRGVLTLWDLRFRVPVNSWQY---PIicpiekMCLCFLPPSvsvsttmkpliYV 1303
Cdd:cd00200  173 LTG--HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhenGV------NSVAFSPDG-----------YL 233
                        250       260
                 ....*....|....*....|....*
gi 15233564 1304 AAGCNE---VSLWNAEGGSCHQVLR 1325
Cdd:cd00200  234 LASGSEdgtIRVWDLRTGECVQTLS 258
WD40 COG2319
WD40 repeat [General function prediction only];
1071-1271 7.73e-09

WD40 repeat [General function prediction only];


Pssm-ID: 225201 [Multi-domain]  Cd Length: 466  Bit Score: 59.72  E-value: 7.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1071 GVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWDSRKLEKdisfRSRLTYHLEGSRGMCTTMLRNSTQVVVGAS- 1149
Cdd:COG2319  274 SSLLRTLSGHSSSVLSVAFSPDGKLLASGSSDGTVRLWDLETGKL----LSSLTLKGHEGPVSSLSFSPDGSLLVSGGSd 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1150 DGVIHMFSIDhisrgLGNVVEKYSGIVDIKKKDVKEGALVSLLNYTADSlsgpmvmystqncgIHLWDTRSDLDAWTLKA 1229
Cdd:COG2319  350 DGTIRLWDLR-----TGKPLKTLEGHSNVLSVSFSPDGRVVSSGSTDGT--------------VRLWDLSTGSLLRNLDG 410
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15233564 1230 NPeeGYVSSLVTSPCGNWFVSGSSRGVLTLWDLRFRVPVNSW 1271
Cdd:COG2319  411 HT--SRVTSLDFSPDGKSLASGSSDNTIRLWDLKTSLKSVSF 450
WD40 pfam00400
WD domain, G-beta repeat;
1071-1109 1.46e-08

WD domain, G-beta repeat;


Pssm-ID: 334060 [Multi-domain]  Cd Length: 39  Bit Score: 51.59  E-value: 1.46e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 15233564   1071 GVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWD 1109
Cdd:pfam00400    1 GKLLKTLEGHSSSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1071-1109 1.70e-08

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 51.54  E-value: 1.70e-08
                            10        20        30
                    ....*....|....*....|....*....|....*....
gi 15233564    1071 GVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWD 1109
Cdd:smart00320    2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
68-288 1.33e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 52.59  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564    68 YERRLVKikdvflSLEHPHVWPFQFWQETDKAAYLVRQYFYSNLHDRLSTRPF-LSLVEKKWLAFQLLLAVKQCHEKDIC 146
Cdd:PHA03211  209 HEARLLR------RLSHPAVLALLDVRVVGGLTCLVLPKYRSDLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHGEGII 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   147 HGDIKCENVLLTSWNWLYLADF--ASF----KPTYIPYddpsDFSFFFDTRgqrlcylAPErfyehggetqVAQDAPLKP 220
Cdd:PHA03211  283 HRDIKTENVLVNGPEDICLGDFgaACFargsWSTPFHY----GIAGTVDTN-------APE----------VLAGDPYTP 341
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   221 SMDIFAVGCVIAELFLEGQPLFELAQllAYRRGQHDpsQHLEKIpdpgIRKMILHMIQL--EPEARLSAE 288
Cdd:PHA03211  342 SVDIWSAGLVIFEAAVHTASLFSASR--GDERRPYD--AQILRI----IRQAQVHVDEFpqHAGSRLVSQ 403
 
Name Accession Description Interval E-value
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
16-303 1.51e-166

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 501.01  E-value: 1.51e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   16 YYLHDLPssynlvlkevLGRGRFLKSIQCKHDEGLVVVKVYFKRGDSIDLREYERRLVKIKDVFLslEHPHVWPFQFWQE 95
Cdd:cd13980    1 DYLYDKS----------LGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLL--ELPNVLPFQKVIE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   96 TDKAAYLVRQYFYSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPTY 175
Cdd:cd13980   69 TDKAAYLIRQYVKYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPTY 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  176 IPYDDPSDFSFFFDTRGQRLCYLAPERFYEHGGETQ--VAQDAPLKPSMDIFAVGCVIAELFLEGQPLFELAQLLAYRRG 253
Cdd:cd13980  149 LPEDNPADFSYFFDTSRRRTCYIAPERFVDALTLDAesERRDGELTPAMDIFSLGCVIAELFTEGRPLFDLSQLLAYRKG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 15233564  254 QHDPSQHLEKIPDPGIRKMILHMIQLEPEARLSAEDYLQNYVGVVFPNYF 303
Cdd:cd13980  229 EFSPEQVLEKIEDPNIRELILHMIQRDPSKRLSAEDYLKKYRGKVFPEYF 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
29-292 8.00e-30

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 119.56  E-value: 8.00e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564      29 LKEVLGRGRFLKSIQCKH--DEGLVVVKVyFKRGDSIDLREYERRLVKIkdvFLSLEHPHVWPFQFWQETDKAAYLVRQY 106
Cdd:smart00220    3 ILEKLGEGSFGKVYLARDkkTGKLVAIKV-IKKKKIKKDRERILREIKI---LKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564     107 F-YSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF--ASFkptyipYDDPSD 183
Cdd:smart00220   79 CeGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFglARQ------LDPGEK 152
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564     184 FSFFFDTRgqrlCYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELfLEGQPLF--ELAQLLAYRR---GQHDPS 258
Cdd:smart00220  153 LTTFVGTP----EYMAPE----------VLLGKGYGKAVDIWSLGVILYEL-LTGKPPFpgDDQLLELFKKigkPKPPFP 217
                           250       260       270
                    ....*....|....*....|....*....|....
gi 15233564     259 QHLEKIPDPGIRkMILHMIQLEPEARLSAEDYLQ 292
Cdd:smart00220  218 PPEWDISPEAKD-LIRKLLVKDPEKRLTAEEALQ 250
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
33-293 1.02e-29

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: 118.14  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   33 LGRGRFLKSIQCKH--DEGLVVVKVYFKRgdsiDLREYERRLVKIKDVFLSLEHPHVWPFQFWQETDKAAYLVRQYF-YS 109
Cdd:cd00180    1 LGKGSFGKVYKARDkeTGKKVAVKVIPKE----KLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCeGG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  110 NLHDRLSTRP-FLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKptyiPYDDPSDFSFFF 188
Cdd:cd00180   77 SLKDLLKENKgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAK----DLDSDDSLLKTT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  189 DTrGQRLCYLAPERFYEHGGETQVaqdaplkpsmDIFAVGCVIAELflegqplfelaqllayrrgqhdpsqhlekipdPG 268
Cdd:cd00180  153 GG-TTPPYYAPPELLGGRYYGPKV----------DIWSLGVILYEL--------------------------------EE 189
                        250       260
                 ....*....|....*....|....*
gi 15233564  269 IRKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd00180  190 LKDLIRRMLQYDPKKRPSAKELLEH 214
Pkinase pfam00069
Protein kinase domain;
27-292 6.50e-25

Protein kinase domain;


Pssm-ID: 333812 [Multi-domain]  Cd Length: 259  Bit Score: 105.40  E-value: 6.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564     27 LVLKEVLGRGRFLKSIQCKHDE--GLVVVKVYFKRGDSIDLREYERRLVKIkdvFLSLEHPHVWPFQFWQETDKAAYLVR 104
Cdd:pfam00069    1 YEVLEKLGEGSFGTVYKAKHKDtgKIVAIKKIKKEKIKKKKEKNVLREIKI---LKKLSHPNIVRLYDVFEDKDHLYLVL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564    105 QYF-YSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF--ASFkptyipYDDP 181
Cdd:pfam00069   78 EYVeGGSLFDLLSEKGVFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILIDEDGNLKITDFglAKQ------LSSG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564    182 SDFSFFFDTRGqrlcYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELfLEGQPLFELA-----QLLAYRRGQHD 256
Cdd:pfam00069  152 SKLTTFVGTPW----YMAPE----------VLGGNPYGPKVDVWSLGCILYEL-LTGKPPFPGIngddiYELILDQLERI 216
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 15233564    257 PSQ----HLEKIPDPGIrKMILHMIQLEPEARLSAEDYLQ 292
Cdd:pfam00069  217 PEDfsspFPSSLSEEAK-DLLKKLLKKDPSKRLTATQALQ 255
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
25-292 1.48e-22

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: 98.81  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   25 YNLVlkEVLGRGRFlkSI----QCKHDEGLVVVKV----YFKRGDSIDLREYERRLVKikdvflSLEHPHVWP-FQFwQE 95
Cdd:cd14014    2 YRLV--RLLGRGGM--GEvyraRDTLLGRPVAIKVlrpeLAEDEEFRERFLREARALA------RLSHPNIVRvYDV-GE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   96 TDKAAYLVRQYFYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF--ASFK 172
Cdd:cd14014   71 DDGRPYIVMEYVEGgSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFgiARAL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  173 PTyipyDDPSDFSFFFDTRGqrlcYLAPERfyehggetqvAQDAPLKPSMDIFAVGCVIAELfLEGQPLFELAQL--LAY 250
Cdd:cd14014  151 GD----SGLTQTGSVLGTPA----YMAPEQ----------ARGGPVDPRSDIYSLGVVLYEL-LTGRPPFDGDSPaaVLA 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15233564  251 RRGQHDPSQHLEKIPD--PGIRKMILHMIQLEPEARL-SAEDYLQ 292
Cdd:cd14014  212 KHLQEAPPPPSPLNPDvpPALDAIILRALAKDPEERPqSAAELLA 256
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
31-292 7.65e-22

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: 97.39  E-value: 7.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   31 EVLGRGRFLKSIQCKHDEG--LVVVKVYFKRGDSIDLREYERRLVKikdVFLSLEHPHVWPFQFWQETDKAAYLVRQYFY 108
Cdd:cd07833    7 GVVGEGAYGVVLKCRNKATgeIVAIKKFKESEDDEDVKKTALREVK---VLRQLRHENIVNLKEAFRRKGRLYLVFEYVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  109 SNLHDRLSTRPF-LSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLAD--FASF--KPTYIPYDDpsd 183
Cdd:cd07833   84 RTLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDfgFARAltARPASPLTD--- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  184 fsfFFDTRgqrlCYLAPErfyehggetQVAQDAPLKPSMDIFAVGCVIAELfLEGQPLF----ELAQLLAYRR--GQHDP 257
Cdd:cd07833  161 ---YVATR----WYRAPE---------LLVGDTNYGKPVDVWAIGCIMAEL-LDGEPLFpgdsDIDQLYLIQKclGPLPP 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233564  258 SQ----------HLEKIPDPGIRKMILH----------------MIQLEPEARLSAEDYLQ 292
Cdd:cd07833  224 SHqelfssnprfAGVAFPEPSQPESLERrypgkvsspaldflkaCLRMDPKERLTCDELLQ 284
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
32-292 2.73e-21

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: 94.61  E-value: 2.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   32 VLGRGRFLKSIQCK-HDEG-LVVVKVY--FKRGDSIDLREYE-----------RRLVKIKDVFlslEHPHvwpfqfwqet 96
Cdd:cd05118    6 KIGEGAFGTVWLARdKVTGeKVAIKKIknDFRHPKAALREIKllkhlndveghPNIVKLLDVF---EHRG---------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   97 DKAAYLVRQYFYSNLHD--RLSTRPF-LSLVekKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNW-LYLADFASFK 172
Cdd:cd05118   73 GNHLCLVFELMGMNLYEliKDYPRGLpLDLI--KSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLAR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  173 ptyiPYDDPsdfsfFFDTRGQRLCYLAPERFYehggetqvaQDAPLKPSMDIFAVGCVIAELFLeGQPLFelaqllayrr 252
Cdd:cd05118  151 ----SFTSP-----PYTPYVATRWYRAPEVLL---------GAKPYGSSIDIWSLGCILAELLT-GRPLF---------- 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15233564  253 GQHDPSQHLEKIPDP-GIRKM---ILHMIQLEPEARLSAEDYLQ 292
Cdd:cd05118  202 PGDSEVDQLAKIVRLlGTPEAldlLSKMLKYDPAKRITASQALA 245
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
73-293 2.37e-18

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: 86.77  E-value: 2.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   73 VKIKDVFLslehphvwpfqfwqeTDKAAYLVRQYFYSNLHDRLSTRPF-LSLVEKKWLAFQLLLAVKQCHEKDICHGDIK 151
Cdd:cd07829   61 VKLLDVIH---------------TENKLYLVFEYCDQDLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  152 CENVLLTSWNWLYLADF---ASFKPTYIPYDDPSdfsfffdtrgQRLCYLAPE-----RFYEhggetqvaqdaplkPSMD 223
Cdd:cd07829  126 PQNLLINRDGVLKLADFglaRAFGIPLRTYTHEV----------VTLWYRAPEillgsKHYS--------------TAVD 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  224 IFAVGCVIAELfLEGQPLF----ELAQLL------------------AYRRGQHD----PSQHLEK-IP--DPGIRKMIL 274
Cdd:cd07829  182 IWSVGCIFAEL-ITGKPLFpgdsEIDQLFkifqilgtpteeswpgvtKLPDYKPTfpkwPKNDLEKvLPrlDPEGIDLLS 260
                        250
                 ....*....|....*....
gi 15233564  275 HMIQLEPEARLSAEDYLQN 293
Cdd:cd07829  261 KMLQYNPAKRISAKEALKH 279
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
24-402 3.19e-18

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 88.65  E-value: 3.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   24 SYNLVlkEVLGRGRFLKSIQCKHDEgLVVVKVYFKrgDSIDLREYERRLVKIKDVFLSLEHPHVWP-FQFWQETDKAAYL 102
Cdd:COG0515    1 SYRIL--RKLGEGSFGEVYLARDRK-LVALKVLAK--KLESKSKEVERFLREIQILASLNHPPNIVkLYDFFQDEGSLYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  103 VRQYF----YSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSW-NWLYLADFASFKpTYIP 177
Cdd:COG0515   76 VMEYVdggsLEDLLKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDgRVVKLIDFGLAK-LLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  178 YDDPSDFSFFFDTRGQRLCYLAPERFyehggetQVAQDAPLKPSMDIFAVGCVIAELfLEGQPLFELAQL---------- 247
Cdd:COG0515  155 PGSTSSIPALPSTSVGTPGYMAPEVL-------LGLSLAYASSSSDIWSLGITLYEL-LTGLPPFEGEKNssatsqtlki 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  248 ---LAYRRGQHDPSQHLEKIPDPGIRKMILHMIQLEPEARLSAEDYLQNYVGVVFPNYFSPFLHTLYccWNPLPSDMRVA 324
Cdd:COG0515  227 ileLPTPSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLK--PDDSAPLRLSL 304
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233564  325 TCQGIFQEILKKMMENKSGDEIGVDSPVTSNPMNASTVQETFANHKLNSSKDLIRNTVNSKDEIFYSISDALKKNRHP 402
Cdd:COG0515  305 PPSLEALISSLNSLAISGSDLKLDDSNFSKELAPNGVSSSPHNSSSLLLSTASSKRSSLPKISARSSPSSLSSSSRQQ 382
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
28-292 4.19e-18

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: 85.61  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   28 VLKEVLGRGRFLKSIQCKH--DEGLVVVKVYFKRGDSIDLREYERRLVKIkdvFLSLEHPHVWPFQFWQETDKAAYLVRQ 105
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHkkTGEEYAVKIIDKKKLKSEDEEMLRREIEI---LKRLDHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  106 YFYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNW---LYLADF--ASFkptyipYD 179
Cdd:cd05117   80 LCTGgELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPdspIKIIDFglAKI------FE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  180 DPSDFSFFFDTRGqrlcYLAPErfyehggetqVAQDAPLKPSMDIFAVGcVIAELFLEGQPLFE---LAQLL-AYRRGQH 255
Cdd:cd05117  154 EGEKLKTVCGTPY----YVAPE----------VLKGKGYGKKCDIWSLG-VILYILLCGYPPFYgetEQELFeKILKGKY 218
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 15233564  256 D-PSQHLEKIPDPGiRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd05117  219 SfDSPEWKNVSEEA-KDLIKRLLVVDPKKRLTAAEALN 255
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1071-1325 1.89e-17

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 84.31  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1071 GVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWDSRKLEkdisfrsrLTYHLEGSRGMCTTM-LRNSTQVVVGAS 1149
Cdd:cd00200   41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE--------CVRTLTGHTSYVSSVaFSPDGRILSSSS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1150 -DGVIHMFSidhisrglgnvVEKYSGIVDIK--KKDVKEGALvsllnytadSLSGPMVMYSTQNCGIHLWDTRSDLDAWT 1226
Cdd:cd00200  113 rDKTIKVWD-----------VETGKCLTTLRghTDWVNSVAF---------SPDGTFVASSSQDGTIKLWDLRTGKCVAT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1227 LKAnpEEGYVSSLVTSPCGNWFVSGSSRGVLTLWDLRFRVPVNSWQY---PIicpiekMCLCFLPPSvsvsttmkpliYV 1303
Cdd:cd00200  173 LTG--HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGhenGV------NSVAFSPDG-----------YL 233
                        250       260
                 ....*....|....*....|....*
gi 15233564 1304 AAGCNE---VSLWNAEGGSCHQVLR 1325
Cdd:cd00200  234 LASGSEdgtIRVWDLRTGECVQTLS 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
26-292 5.66e-17

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: 82.18  E-value: 5.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   26 NLVLKEVLGRGRFLK-----SIQCKHdegLVVVKVYFKRGDSIDLREYERRLVKIkdvFLSLEHPHVwpFQFWQ--ETDK 98
Cdd:cd14003    1 NYELGKTLGEGSFGKvklarHKLTGE---KVAIKIIDKSKLKEEIEEKIKREIEI---MKLLNHPNI--IKLYEviETEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   99 AAYLVRQYFYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFAsfkptyip 177
Cdd:cd14003   73 KIYLVMEYASGgELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFG-------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  178 yddpsdFSFFFdTRGQRL-------CYLAPE----RFYeHGgetqvaqdaplkPSMDIFAVGcVIaeLF--LEGQPLFE- 243
Cdd:cd14003  145 ------LSNEF-RGGSLLktfcgtpAYAAPEvllgRKY-DG------------PKADVWSLG-VI--LYamLTGYLPFDd 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15233564  244 --LAQLLAY-RRGQHDPSQHLekipDPGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14003  202 dnDSKLFRKiLKGKYPIPSHL----SPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
50-291 1.25e-16

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: 81.58  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   50 LVVVKVYFKRGDSIDLREYERRLVKIKDVFLSLEHPHVW----PFQfwqeTDKAAYLVRQYFYS--NLHDRLSTRPFLSL 123
Cdd:cd13994   22 LYAVKEYRRRDDESKRKDYVKRLTSEYIISSKLHHPNIVkvldLCQ----DLHGKWCLVMEYCPggDLFTLIEKADSLSL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  124 VEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASfkptyipyddpSD-FSFFFDTR---GQRLC--- 196
Cdd:cd13994   98 EEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGT-----------AEvFGMPAEKEspmSAGLCgse 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  197 -YLAPERFYEhggetqvaqdAPLKP-SMDIFAVGCVIAELFLEGQPlFELAQL--LAY------RRGQHDPSQHLEKIPD 266
Cdd:cd13994  167 pYMAPEVFTS----------GSYDGrAVDVWSCGIVLFALFTGRFP-WRSAKKsdSAYkayeksGDFTNGPYEPIENLLP 235
                        250       260
                 ....*....|....*....|....*
gi 15233564  267 PGIRKMILHMIQLEPEARLSAEDYL 291
Cdd:cd13994  236 SECRRLIYRMLHPDPEKRITIDEAL 260
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
33-292 3.01e-16

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: 79.83  E-value: 3.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   33 LGRGRF--LKSIQCKHDEGLVVVKVYFKRgdsiDLREYE-----RRLVKIKdvfLSLEHPHVWPFQFWQETDKAAYLVRQ 105
Cdd:cd14007    8 LGKGKFgnVYLAREKKSGFIVALKVISKS----QLQKSGlehqlRREIEIQ---SHLRHPNILRLYGYFEDKKRIYLILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  106 Y-FYSNLHDRLSTRPFLSlvEKKwlA----FQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFasfkpTYIPYDD 180
Cdd:cd14007   81 YaPNGELYKELKKQKRFD--EKE--AakyiYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADF-----GWSVHAP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  181 PSDFSFFFDTrgqrLCYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAElFLEGQPLFE-LAQLLAYRRGQhdpSQ 259
Cdd:cd14007  152 SNRRKTFCGT----LDYLPPE----------MVEGKEYDYKVDIWSLGVLCYE-LLVGKPPFEsKSHQETYKRIQ---NV 213
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15233564  260 HLeKIPD---PGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14007  214 DI-KFPSsvsPEAKDLISKLLQKDPSKRLSLEQVLN 248
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
126-293 7.03e-16

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: 79.15  E-value: 7.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  126 KKWLAfQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKptYIPYDDPSDFSfffDTRGQRLCYLAPErfye 205
Cdd:cd14080  105 RIWFR-QLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFAR--LCPDDDGDVLS---KTFCGSAAYAAPE---- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  206 hggetqVAQDAPLKPSM-DIFAVGCViaeLF--LEGQPLFE---LAQLL--AYRRGQHDPSqHLEKIpDPGIRKMILHMI 277
Cdd:cd14080  175 ------ILQGIPYDPKKyDIWSLGVI---LYimLCGSMPFDdsnIKKMLkdQQNRKVRFPS-SVKKL-SPECKDLIDQLL 243
                        170
                 ....*....|....*.
gi 15233564  278 QLEPEARLSAEDYLQN 293
Cdd:cd14080  244 EPDPTKRATIEEILNH 259
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
25-292 1.20e-15

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: 78.73  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   25 YNLVlkEVLGRGRF---LKSIQcKHDEGLVVVKV----YFKRGDSIDLREYE--RRL------VKIKDVFLslEHPHVwp 89
Cdd:cd07830    1 YKVI--KQLGDGTFgsvYLARN-KETGELVAIKKmkkkFYSWEECMNLREVKslRKLnehpniVKLKEVFR--ENDEL-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   90 fqfwqetdkaaYLVRQYFYSNLHDRLSTR---PFLSLVEKKWLaFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLA 166
Cdd:cd07830   74 -----------YFVFEYMEGNLYQLMKDRkgkPFSESVIRSII-YQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIA 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  167 DF------ASfKPTYIPYddpsdfsffFDTRgqrlCYLAPE-----RFYehggetqvaqDAPLkpsmDIFAVGCVIAELF 235
Cdd:cd07830  142 DFglareiRS-RPPYTDY---------VSTR----WYRAPEillrsTSY----------SSPV----DIWALGCIMAELY 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  236 LeGQPLF----ELAQL--------------------LAYRRG-------QHDPSQHLEKIPDPGIrKMILHMIQLEPEAR 284
Cdd:cd07830  194 T-LRPLFpgssEIDQLykicsvlgtptkqdwpegykLASKLGfrfpqfaPTSLHQLIPNASPEAI-DLIKDMLRWDPKKR 271

                 ....*...
gi 15233564  285 LSAEDYLQ 292
Cdd:cd07830  272 PTASQALQ 279
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
33-292 2.70e-14

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: 75.10  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   33 LGRGRFLKSIQCKHDEG--LVVVKVYFKRGDS-----IDLREYerRLVKikdvflSLEHPHVWPFQFWQETDKAAYLVRQ 105
Cdd:cd07847    9 IGEGSYGVVFKCRNRETgqIVAIKKFVESEDDpvikkIALREI--RMLK------QLKHPNLVNLIEVFRRKRKLHLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  106 YFYSNLHDRLSTRPF-LSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFAsFKPTYIPYDDpsDF 184
Cdd:cd07847   81 YCDHTVLNELEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFG-FARILTGPGD--DY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  185 SFFFDTRgqrlCYLAPERFYehgGETQVAqdaplkPSMDIFAVGCVIAELfLEGQPLF----ELAQLLAYRR--GQHDPs 258
Cdd:cd07847  158 TDYVATR----WYRAPELLV---GDTQYG------PPVDVWAIGCVFAEL-LTGQPLWpgksDVDQLYLIRKtlGDLIP- 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233564  259 QHLE-----------KIPDPGIRKMI------------------LHMiqlEPEARLSAEDYLQ 292
Cdd:cd07847  223 RHQQifstnqffkglSIPEPETREPLeskfpnisspalsflkgcLQM---DPTERLSCEELLE 282
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
32-252 4.37e-14

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: 74.26  E-value: 4.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   32 VLGRGRFLKSIQCKHDEG--LVVVKVYFKRGDSIDLREYERRLVKIkdvFLSLEHPHVWPFQFWQETDKAAYLVRQYFYS 109
Cdd:cd07848    8 VVGEGAYGVVLKCRHKETkeIVAIKKFKDSEENEEVKETTLRELKM---LRTLKQENIVELKEAFRRRGKLYLVFEYVEK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  110 NLHDRLSTRPFLSLVEK-KWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPtyIPYDDPSDFSFFF 188
Cdd:cd07848   85 NMLELLEEMPNGVPPEKvRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARN--LSEGSNANYTEYV 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15233564  189 DTRgqrlCYLAPERFYehggetqvaqDAPLKPSMDIFAVGCVIAELFlEGQPLF----ELAQLLAYRR 252
Cdd:cd07848  163 ATR----WYRSPELLL----------GAPYGKAVDMWSVGCILGELS-DGQPLFpgesEIDQLFTIQK 215
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
72-248 5.46e-14

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 73.90  E-value: 5.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   72 LVKIKDVFlslehPHvwpfqfwqetDKAAYLVRQYFYSNLHDRL--STRPfLSLVEKKWLAFQLLLAVKQCHEKDICHGD 149
Cdd:cd07832   62 VVKLRDVF-----PH----------GTGFVLVFEYMLSSLSEVLrdEERP-LTEAQVKRYMRMLLKGVAYMHANRIMHRD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  150 IKCENVLLTSWNWLYLADFA---SFKPtyipyDDPSDFSFFFDTRgqrlCYLAPERFYEhggetqvAQDapLKPSMDIFA 226
Cdd:cd07832  126 LKPANLLISSTGVLKIADFGlarLFSE-----EDPRLYSHQVATR----WYRAPELLYG-------SRK--YDEGVDLWA 187
                        170       180
                 ....*....|....*....|....*.
gi 15233564  227 VGCVIAELfLEGQPLF----ELAQLL 248
Cdd:cd07832  188 VGCIFAEL-LNGSPLFpgenDIEQLA 212
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
101-292 5.89e-14

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: 74.14  E-value: 5.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  101 YLVRQYF---YSNLHDRLSTRpfLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKptyiP 177
Cdd:cd07840   80 YMVFEYMdhdLTGLLDNPEVK--FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR----P 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  178 YDDPSDFSFffdT-RGQRLCYLAPERFYehgGETQvaqdapLKPSMDIFAVGCVIAELFLeGQPLFelaqllayrRGQHD 256
Cdd:cd07840  154 YTKENNADY---TnRVITLWYRPPELLL---GATR------YGPEVDMWSVGCILAELFT-GKPIF---------QGKTE 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233564  257 PSQhLEKI------PD----PGIRKM-------------------------------ILHMIQLEPEARLSAEDYLQ 292
Cdd:cd07840  212 LEQ-LEKIfelcgsPTeenwPGVSDLpwfenlkpkkpykrrlrevfknvidpsaldlLDKLLTLDPKKRISADQALQ 287
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
31-293 7.33e-14

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: 72.88  E-value: 7.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   31 EVLGRGRFLKSI--QCKHDEGLVVVKVYFKRGDSIDLREYERRLVKIkdvfLS-LEHPHVWPFqfwqetdKAAYLVRQYF 107
Cdd:cd08215    6 RVIGKGSFGSAYlvRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKL----LSkLKHPNIVKY-------YESFEENGKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  108 Y--------SNLHDRLSTR-----PFLslvEK---KWLAfQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF--- 168
Cdd:cd08215   75 CivmeyadgGDLAQKIKKQkkkgqPFP---EEqilDWFV-QICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFgis 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  169 ------ASFKPTYI--PYddpsdfsfffdtrgqrlcYLAPErfyehggetqVAQDAPL-KPSmDIFAVGCVIAELfLEGQ 239
Cdd:cd08215  151 kvlestTDLAKTVVgtPY------------------YLSPE----------LCENKPYnYKS-DIWALGCVLYEL-CTLK 200
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233564  240 PLFELAQL--LAYR--RGQHDPsqhlekIP---DPGIRKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd08215  201 HPFEANNLpaLVYKivKGQYPP------IPsqySSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
22-242 8.90e-14

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: 73.31  E-value: 8.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   22 PSSYNLVLKEVLGRGRFLKSIQCKHDEGLVVV---KVYF-KRGDSidlREYE--RRL-----VKIKDVFLSLEhphvwpf 90
Cdd:cd14137    1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVaikKVLQdKRYKN---RELQimRRLkhpniVKLKYFFYSSG------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   91 qfwqETDKAAYL--VRQYFYSNLHDRLST----RPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNW-L 163
Cdd:cd14137   71 ----EKKDEVYLnlVMEYMPETLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGvL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  164 YLADFASFKP--------TYIPyddpsdfsfffdTRgqrlCYLAPE-----RFYEHggetqvaqdaplkpSMDIFAVGCV 230
Cdd:cd14137  147 KLCDFGSAKRlvpgepnvSYIC------------SR----YYRAPElifgaTDYTT--------------AIDIWSAGCV 196
                        250
                 ....*....|..
gi 15233564  231 IAELFLeGQPLF 242
Cdd:cd14137  197 LAELLL-GQPLF 207
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
81-292 2.59e-13

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: 71.66  E-value: 2.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   81 SLEHPHVWPFQFWQETDKAAYLVRQYFYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTS 159
Cdd:cd14084   67 KLSHPCIIKIEDFFDAEDDYYIVLELMEGgELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSS 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  160 WN---WLYLADFASFKptyipyddPSDFSFFFDTRGQRLCYLAPERFYEHGGEtqvaqdaPLKPSMDIFAVGCViaeLF- 235
Cdd:cd14084  147 QEeecLIKITDFGLSK--------ILGETSLMKTLCGTPTYLAPEVLRSFGTE-------GYTRAVDCWSLGVI---LFi 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233564  236 -LEGQPLF-------ELAQLLAYRRGQHDPsQHLEKIPDPGiRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14084  209 cLSGYPPFseeytqmSLKEQILSGKYTFIP-KAWKNVSEEA-KDLVKKMLVVDPSRRPSIEEALE 271
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
29-292 3.26e-13

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: 71.15  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   29 LKEVLGRGRFLKSIQC-KHDEG-LVVVKV------YFKRG-DSIDLREY--------ERRLVKIKDVFLSLEHphvwpfq 91
Cdd:cd14133    3 VLEVLGKGTFGQVVKCyDLLTGeEVALKIiknnkdYLDQSlDEIRLLELlnkkdkadKYHIVRLKDVFYFKNH------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   92 fwqetdkaAYLVRQYFYSNLHD--RLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWN--WLYLAD 167
Cdd:cd14133   76 --------LCIVFELLSQNLYEflKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIID 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  168 FASfkptyipyddpSDFSfffdtrGQRLCYLAPERFYEhggETQVAQDAPLKPSMDIFAVGCVIAELFLeGQPLFELA-- 245
Cdd:cd14133  148 FGS-----------SCFL------TQRLYSYIQSRYYR---APEVILGLPYDEKIDMWSLGCILAELYT-GEPLFPGAse 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15233564  246 -QLLAYRRG-QHDPSQHL---EKIPDPGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14133  207 vDQLARIIGtIGIPPAHMldqGKADDELFVDFLKKLLEIDPKERPTASQALS 258
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
32-284 5.67e-13

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: 70.53  E-value: 5.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   32 VLGRGRFLKSIQC--KHDEGLVVVKVYFKRGDSIDLREYERRLVKIKDVflsLEHPHVWPFQFWQETDKAAYLVRQYFYS 109
Cdd:cd08220    7 VVGRGAYGTVYLCrrKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSM---LHHPNIIEYYESFLEDKALMIVMEYAPG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  110 -NLHDRLSTRPFLSLVEKKWLAF--QLLLAVKQCHEKDICHGDIKCENVLLTS-WNWLYLADFAsfkptyipyddpsdFS 185
Cdd:cd08220   84 gTLFEYIQQRKGSLLSEEEILHFfvQILLALHHVHSKQILHRDLKTQNILLNKkRTVVKIGDFG--------------IS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  186 FFFDTRGQRL------CYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELfLEGQPLFELAQL----LAYRRGQH 255
Cdd:cd08220  150 KILSSKSKAYtvvgtpCYISPE----------LCEGKPYNQKSDIWALGCVLYEL-ASLKRAFEAANLpalvLKIMRGTF 218
                        250       260
                 ....*....|....*....|....*....
gi 15233564  256 DPsqhLEKIPDPGIRKMILHMIQLEPEAR 284
Cdd:cd08220  219 AP---ISDRYSEELRHLILSMLHLDPNKR 244
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
33-287 7.07e-13

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 69.85  E-value: 7.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   33 LGRGRFLKSIQCKH--DEGLVVVKVYFKRgdSIDLREYERRLVKIKDVFLSLEHPHV----WPFQfwqeTDKAAYLVRQY 106
Cdd:cd05123    1 LGKGSFGKVLLVRKkdTGKLYAMKVLRKK--EIIKRKEVEHTLNERNILERVNHPFIvklhYAFQ----TEEKLYLVLDY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  107 FYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPtyIPYDDPSDFS 185
Cdd:cd05123   75 VPGgELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKE--LSSDGDRTYT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  186 FffdtrgqrlC----YLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELfLEGQPLFElaqllayrrgQHDPSQHL 261
Cdd:cd05123  153 F---------CgtpeYLAPE----------VLLGKGYGKAVDWWSLGVLLYEM-LTGKPPFY----------AENRKEIY 202
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15233564  262 EKI-------PD---PGIRKMILHMIQLEPEARLSA 287
Cdd:cd05123  203 EKIlksplkfPEyvsPEAKSLISGLLQKDPTKRLGS 238
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
31-292 1.21e-12

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: 69.47  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   31 EVLGRGRFLKSIQCK-HDEG-LVVVK-VYFKRGDSIDLREYER--RLVKikdvflSLEHPHVwpfqfwqetdkaaylVRq 105
Cdd:cd06606    6 ELLGKGSFGSVYLALnLDTGeLMAVKeVELSGDSEEELEALEReiRILS------SLKHPNI---------------VR- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  106 YFYSNlHDRLSTRPFL---------SLVEKKW---------LAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLAD 167
Cdd:cd06606   64 YLGTE-RTENTLNIFLeyvpggslaSLLKKFGklpepvvrkYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLAD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  168 F-ASFKptyipYDDPSDFSFFFDTRGQRLcYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELFLEGQPLFELAQ 246
Cdd:cd06606  143 FgCAKR-----LAEIATGEGTKSLRGTPY-WMAPE----------VIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGN 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15233564  247 LLA--YRRGQhdpSQHLEKIPD---PGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd06606  207 PVAalFKIGS---SGEPPPIPEhlsEEAKDFLRKCLQRDPKKRPTADELLQ 254
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
82-292 1.80e-12

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: 69.43  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   82 LEHPHVWPFQFWQETDKAAYLVRQYFYSNLHDRLST---RPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLT 158
Cdd:cd07836   55 LKHENIVRLHDVIHTENKLMLVFEYMDKDLKKYMDThgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLIN 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  159 SWNWLYLADFASFKPTYIPYDDpsdfsffFDTRGQRLCYLAPERFYehGGETqvaqdapLKPSMDIFAVGCVIAELFlEG 238
Cdd:cd07836  135 KRGELKLADFGLARAFGIPVNT-------FSNEVVTLWYRAPDVLL--GSRT-------YSTSIDIWSVGCIMAEMI-TG 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  239 QPLF-------------------------ELAQLLAYR----RGQHDPSQHLEKIPDPGIRKMILHMIQLEPEARLSAED 289
Cdd:cd07836  198 RPLFpgtnnedqllkifrimgtptestwpGISQLPEYKptfpRYPPQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHD 277

                 ...
gi 15233564  290 YLQ 292
Cdd:cd07836  278 ALQ 280
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
31-293 2.09e-12

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: 68.57  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   31 EVLGRGRFLKSIQCKHDEG--LVVVKVYFKRGDSIDLREYERRL------VKIKDVFLSLEHPHVWPFQFWQETDKAAYL 102
Cdd:cd14004    6 KEMGEGAYGQVNLAIYKSKgkEVVIKFIFKERILVDTWVRDRKLgtvpleIHILDTLNKRSHPNIVKLLDFFEDDEFYYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  103 VRQYFYS--NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASfkPTYIpydD 180
Cdd:cd14004   86 VMEKHGSgmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGS--AAYI---K 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  181 PSDFSFFFDTRGqrlcYLAPERFyehGGETQVAqdaplkPSMDIFAVGCVIAELFLEGQPLFELAQLLayrrgqhDPSQH 260
Cdd:cd14004  161 SGPFDTFVGTID----YAAPEVL---RGNPYGG------KEQDIWALGVLLYTLVFKENPFYNIEEIL-------EADLR 220
                        250       260       270
                 ....*....|....*....|....*....|...
gi 15233564  261 LEKIPDPGIRKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd14004  221 IPYAVSEDLIDLISRMLNRDVGDRPTIEELLTD 253
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
132-292 4.94e-12

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: 67.71  E-value: 4.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  132 QLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPTyIPYDDPSDFSFFFDTRGQRLcYLAPE-----RFYEH 206
Cdd:cd06626  107 QLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKL-KNNTTTMAPGEVNSLVGTPA-YMAPEvitgnKGEGH 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  207 GGetqvaqdaplkpSMDIFAVGCVIAELFLEGQPLFELAQLLA--YRRGQHDPSQhlekIPDP------GIrKMILHMIQ 278
Cdd:cd06626  185 GR------------AADIWSLGCVVLEMATGKRPWSELDNEWAimYHVGMGHKPP----IPDSlqlspeGK-DFLSRCLE 247
                        170
                 ....*....|....
gi 15233564  279 LEPEARLSAEDYLQ 292
Cdd:cd06626  248 SDPKKRPTASELLD 261
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
25-292 7.82e-12

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


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 67.30  E-value: 7.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   25 YNLVLKevLGRGRF---LKsIQCKHDEGLVVVKVYFKRGDSID----LREYE--RRLVkikdvflslEHPHVWPFQ---F 92
Cdd:cd07831    1 YKILGK--IGEGTFsevLK-AQSRKTGKYYAIKCMKKHFKSLEqvnnLREIQalRRLS---------PHPNILRLIevlF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   93 WQETDKAAyLVRQYFYSNLHDRLSTR--PFLSLVEKKWLaFQLLLAVKQCHEKDICHGDIKCENVLLTSwNWLYLADFAS 170
Cdd:cd07831   69 DRKTGRLA-LVFELMDMNLYELIKGRkrPLPEKRVKNYM-YQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  171 FKPTYI--PYDDpsdfsfFFDTRgqrlCYLAPERFYEHGGETqvaqdaplkPSMDIFAVGCVIAELfLEGQPLF----EL 244
Cdd:cd07831  146 CRGIYSkpPYTE------YISTR----WYRAPECLLTDGYYG---------PKMDIWAVGCVFFEI-LSLFPLFpgtnEL 205
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233564  245 AQ--------------LLAYRRgqhdPSQHLE-KIP---DPGIRKMILH-----------MIQLEPEARLSAEDYLQ 292
Cdd:cd07831  206 DQiakihdvlgtpdaeVLKKFR----KSRHMNyNFPskkGTGLRKLLPNasaegldllkkLLAYDPDERITAKQALR 278
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
26-242 9.04e-12

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


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 67.24  E-value: 9.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   26 NLVLKEVLGRGRFLKSIQC--KHDEGLVVVKVYFKRgdSIdLREYERRLVKI-KDVFLSLEHPHV----WPFQFWQETdk 98
Cdd:cd05581    2 DFKFGKPLGEGSYSTVVLAkeKETGKEYAIKVLDKR--HI-IKEKKVKYVTIeKEVLSRLAHPGIvklyYTFQDESKL-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   99 aaYLVRQYfysnlhdrLSTRPFLSLVEK------KWLAF---QLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFA 169
Cdd:cd05581   77 --YFVLEY--------APNGDLLEYIRKygsldeKCTRFytaEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  170 S---FKPTYIPYDDPSDFSFFFDTRGQRLC-------YLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELFlEGQ 239
Cdd:cd05581  147 TakvLGPDSSPESTKGDADSQIAYNQARAAsfvgtaeYVSPE----------LLNEKPAGKSSDLWALGCIIYQML-TGK 215

                 ...
gi 15233564  240 PLF 242
Cdd:cd05581  216 PPF 218
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1067-1268 9.27e-12

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 67.36  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1067 WKPR-GVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWDSRKLEKDISFRSrltyHLEGsrGMCTTMLRNSTQVV 1145
Cdd:cd00200   78 WDLEtGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRG----HTDW--VNSVAFSPDGTFVA 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1146 VGASDGVIHMFSIDhisrgLGNVVEKYSGivdikkkdvKEGALVSLlnytADSLSGPMVMYSTQNCGIHLWDTRSdlDAW 1225
Cdd:cd00200  152 SSSQDGTIKLWDLR-----TGKCVATLTG---------HTGEVNSV----AFSPDGEKLLSSSSDGTIKLWDLST--GKC 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 15233564 1226 --TLKANpeEGYVSSLVTSPCGNWFVSGSSRGVLTLWDLRFRVPV 1268
Cdd:cd00200  212 lgTLRGH--ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECV 254
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-293 1.17e-11

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: 66.59  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   29 LKEVLGRGRFLKSI--QCKHDEGLVVVKVYFKRGdsidLREYERRLVKIKDVFLSLEHPHVWPFQFWQETDKAAYLVRQY 106
Cdd:cd14167    7 FREVLGTGAFSEVVlaEEKRTQKLVAIKCIAKKA----LEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  107 FYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNW---LYLADFASFKPTyipyDDPS 182
Cdd:cd14167   83 VSGgELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDEdskIMISDFGLSKIE----GSGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  183 DFSFFFDTRGqrlcYLAPErfyehggetqVAQDAPLKPSMDIFAVGcVIAELFLEGQP---------LFElaQLLayrRG 253
Cdd:cd14167  159 VMSTACGTPG----YVAPE----------VLAQKPYSKAVDCWSIG-VIAYILLCGYPpfydendakLFE--QIL---KA 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 15233564  254 QHD-PSQHLEKIPDPGiRKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd14167  219 EYEfDSPYWDDISDSA-KDFIQHLMEKDPEKRFTCEQALQH 258
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
95-295 2.27e-11

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: 66.81  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   95 ETDKAAYLVRQYFYSNLHdRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFA---SF 171
Cdd:cd07852   79 ENDKDIYLVFEYMETDLH-AVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGlarSL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  172 KPTYIPYDDPsDFSFFFDTRgqrlCYLAPE-----RFYEHGgetqvaqdaplkpsMDIFAVGCVIAELFLeGQPLF---- 242
Cdd:cd07852  158 SQLEEDDENP-VLTDYVATR----WYRAPEillgsTRYTKG--------------VDMWSVGCILGEMLL-GKPLFpgts 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  243 -------------------------ELAQLLAYRRGQHDPSQHLEKIPD--PGIRKMILHMIQLEPEARLSAEDYLQN-Y 294
Cdd:cd07852  218 tlnqlekiievigrpsaediesiqsPFAATMLESLPPSRPKSLDELFPKasPDALDLLKKLLVFNPNKRLTAEEALRHpY 297

                 .
gi 15233564  295 V 295
Cdd:cd07852  298 V 298
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
97-292 2.88e-11

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: 65.98  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   97 DKAA-YLVRQYFYsnlHDrlstrpFLSLVEKKWLAF----------QLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYL 165
Cdd:cd07864   87 DKGAfYLVFEYMD---HD------LMGLLESGLVHFsedhiksfmkQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKL 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  166 ADF--ASFkptyipYDdpSDFSFFFDTRGQRLCYLAPERFYehgGETQVAqdaplkPSMDIFAVGCVIAELFLEgQPLF- 242
Cdd:cd07864  158 ADFglARL------YN--SEESRPYTNKVITLWYRPPELLL---GEERYG------PAIDVWSCGCILGELFTK-KPIFq 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  243 ---ELAQLLAYRR--GQHDPS-------------------------QHLEKIPDPGIrKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd07864  220 anqELAQLELISRlcGSPCPAvwpdviklpyfntmkpkkqyrrrlrEEFSFIPTPAL-DLLDHMLTLDPSKRCTAEQALN 298
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1067-1261 3.78e-11

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 65.43  E-value: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1067 WK-PRGVLVAHLQEHRSAVNDIATSSDHSFFVSASDDSTVKVWDSRklekdiSFRSRLTYHLEGSRGMCTTMLRNSTQVV 1145
Cdd:cd00200  120 WDvETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLR------TGKCVATLTGHTGEVNSVAFSPDGEKLL 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564 1146 VGASDGVIHMFSIDhisrgLGNVVEKYSGivdikkkdvKEGALVSLlnytADSLSGPMVMYSTQNCGIHLWDTRSDLDAW 1225
Cdd:cd00200  194 SSSSDGTIKLWDLS-----TGKCLGTLRG---------HENGVNSV----AFSPDGYLLASGSEDGTIRVWDLRTGECVQ 255
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15233564 1226 TLKANPEEgyVSSLVTSPCGNWFVSGSSRGVLTLWD 1261
Cdd:cd00200  256 TLSGHTNS--VTSLAWSPDGKRLASGSADGTIRIWD 289
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
101-247 1.12e-10

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 64.31  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  101 YLVRQYFYSNLHDRLS--TRPFlSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPTYIPY 178
Cdd:cd07845   84 FLVMEYCEQDLASLLDnmPTPF-SESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLPA 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233564  179 DDPSdfsfffdTRGQRLCYLAPERFYehGGETQVAqdaplkpSMDIFAVGCVIAELfLEGQPLF----ELAQL 247
Cdd:cd07845  163 KPMT-------PKVVTLWYRAPELLL--GCTTYTT-------AIDMWAVGCILAEL-LAHKPLLpgksEIEQL 218
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
82-293 1.15e-10

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: 63.57  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   82 LEHPHVWPFQFWQETDKAAYLVRQYfYSN--LHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTS 159
Cdd:cd14071   56 LNHPHIIKLYQVMETKDMLYLVTEY-ASNgeIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  160 WNWLYLADFAsfkptyipyddpsdFSFFFdTRGQRL---C----YLAPERF--YEHGGetqvaqdaplkPSMDIFAVGCV 230
Cdd:cd14071  135 NMNIKIADFG--------------FSNFF-KPGELLktwCgsppYAAPEVFegKEYEG-----------PQLDIWSLGVV 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  231 I-----AELFLEGQPLFEL-AQLLAYR-RGQHDPSQHLEkipdpgirKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd14071  189 LyvlvcGALPFDGSTLQTLrDRVLSGRfRIPFFMSTDCE--------HLIRRMLVLDPSKRLTIEQIKKH 250
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
31-292 1.33e-10

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: 63.42  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   31 EVLGRGRFLKSIQC--KHDEGLVVVKVYFKRGDS-IDLREYERRLvkikDVFLSLEHPHVWPFQFWQETDKAAYLVRQYF 107
Cdd:cd14002    7 ELIGEGSFGKVYKGrrKYTGQVVALKFIPKRGKSeKELRNLRQEI----EILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  108 YSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKptyipyddpsdfSFF 187
Cdd:cd14002   83 QGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAR------------AMS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  188 FDT------RGQRLcYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELFLeGQP------LFELAQLLAyrrgqH 255
Cdd:cd14002  151 CNTlvltsiKGTPL-YMAPE----------LVQEQPYDHTADLWSLGCILYELFV-GQPpfytnsIYQLVQMIV-----K 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15233564  256 DPSQHLEKIpDPGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14002  214 DPVKWPSNM-SPEFKSFLQGLLNKDPSKRLSWPDLLE 249
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
28-242 1.46e-10

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: 64.19  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   28 VLKEVLGRGRF---LKSIQCKHDEgLVVVKV------YFKRG----------DSIDLREYERRLVKIKDVFLSleHPHVW 88
Cdd:cd14212    2 LVLDLLGQGTFgqvVKCQDLKTNK-LVAVKVlknkpaYFRQAmleiailtllNTKYDPEDKHHIVRLLDHFMH--HGHLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   89 pfqfwqetdkaayLVRQYFYSNLHDRLSTRPF--LSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWN--WLY 164
Cdd:cd14212   79 -------------IVFELLGVNLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDspEIK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  165 LADFAS--FKP----TYIpyddpsdfsfffdtrgQRLCYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELFLeG 238
Cdd:cd14212  146 LIDFGSacFENytlyTYI----------------QSRFYRSPE----------VLLGLPYSTAIDMWSLGCIAAELFL-G 198

                 ....
gi 15233564  239 QPLF 242
Cdd:cd14212  199 LPLF 202
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
81-293 1.84e-10

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: 63.03  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   81 SLEHPHVWPFQFWQETDKAAYLV----RQYFYSNLHDRlstRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVL 156
Cdd:cd14187   63 SLAHQHVVGFHGFFEDNDFVYVVlelcRRRSLLELHKR---RKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLF 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  157 LTSWNWLYLADFAsfKPTYIPYDdpsdfsfffDTRGQRLC----YLAPERFYEHGGETQVaqdaplkpsmDIFAVGCVIA 232
Cdd:cd14187  140 LNDDMEVKIGDFG--LATKVEYD---------GERKKTLCgtpnYIAPEVLSKKGHSFEV----------DIWSIGCIMY 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233564  233 ELfLEGQPLFELAQL----LAYRRGQHDPSQHLEKIPDPGIRKmilhMIQLEPEARLSAEDYLQN 293
Cdd:cd14187  199 TL-LVGKPPFETSCLketyLRIKKNEYSIPKHINPVAASLIQK----MLQTDPTARPTINELLND 258
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
33-292 2.41e-10

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: 62.29  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   33 LGRGRFLKSIQCKHD-EGLVV----VKVYFKRGDSIdLREYerrlvkikDVFLSLEHPHVWPFQFWQETDKAAYLVRQYF 107
Cdd:cd14006    1 LGRGRFGVVKRCIEKaTGREFaakfIPKRDKKKEAV-LREI--------SILNQLQHPRIIQLHEAYESPTELVLILELC 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  108 YS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSW--NWLYLADFASFKptyiPYDDPSDF 184
Cdd:cd14006   72 SGgELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRpsPQIKIIDFGLAR----KLNPGEEL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  185 SFFFDTrgqrLCYLAPErfyehggetqVAQDAPLKPSMDIFAVGcVIAELFLEGQPLF----ELAQLLAYRRGQHDPSQH 260
Cdd:cd14006  148 KEIFGT----PEFVAPE----------IVNGEPVSLATDMWSIG-VLTYVLLSGLSPFlgedDQETLANISACRVDFSEE 212
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15233564  261 LEKIPDPGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14006  213 YFSSVSQEAKDFIRKLLVKEPRKRPTAQEALQ 244
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
11-293 2.59e-10

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: 63.07  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   11 VSATEYYLHDLPssynlvlKEVLGRGRFLKSIQCKHDE-----GLVVVKVYFKRGDSIDLREYERRLVKIKDVFLSLE-H 84
Cdd:cd14181    3 AGAKEFYQKYDP-------KEVIGRGVSSVVRRCVHRHtgqefAVKIIEVTAERLSPEQLEEVRSSTLKEIHILRQVSgH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   85 PHVWPFQFWQETDKAAYLVRQYFY-SNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWL 163
Cdd:cd14181   76 PSIITLIDSYESSTFIFLVFDLMRrGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  164 YLADFAsFKPTYIPyddpsdfsfffDTRGQRLC----YLAPERFYEHGGETQVAQDAplkpSMDIFAVGCVIAELFLEGQ 239
Cdd:cd14181  156 KLSDFG-FSCHLEP-----------GEKLRELCgtpgYLAPEILKCSMDETHPGYGK----EVDLWACGVILFTLLAGSP 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15233564  240 PLFELAQLLAYR---RGQHDPSQHLEKIPDPGIRKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd14181  220 PFWHRRQMLMLRmimEGRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQH 276
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
29-293 2.79e-10

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: 62.57  E-value: 2.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   29 LKEVLGRGRF--LKSIQCKHDEGLVVVKVYFKRGDSIDLreYERRLVKIKDVFLSLEHPH-VWPFQFWQETDKAAYLVRQ 105
Cdd:cd14164    4 LGTTIGEGSFskVKLATSQKYCCKVAIKIVDRRRASPDF--VQKFLPRELSILRRVNHPNiVQMFECIEVANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  106 YFYSNLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWN-WLYLADFASFKPTyipyDDPSDF 184
Cdd:cd14164   82 AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFV----EDYPEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  185 SFFFdtRGQRlCYLAPErfyehggetqVAQDAPLKP-SMDIFAVGCVIAELFLEGQPLFE-LAQLLayrRGQHDPSQHLE 262
Cdd:cd14164  158 STTF--CGSR-AYTPPE----------VILGTPYDPkKYDVWSLGVVLYVMVTGTMPFDEtNVRRL---RLQQRGVLYPS 221
                        250       260       270
                 ....*....|....*....|....*....|...
gi 15233564  263 --KIPDPgIRKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd14164  222 gvALEEP-CRALIRTLLQFNPSTRPSIQQVAGN 253
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
31-294 2.79e-10

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: 62.70  E-value: 2.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   31 EVLGRGRFLKSIQCKH--DEGLVVVKVyFKRGDSIDLREYERRLVKikdVFLSLEHPHVWPFQFWQETDKAAYLVRQYF- 107
Cdd:cd13996   12 ELLGSGGFGSVYKVRNkvDGVTYAIKK-IRLTEKSSASEKVLREVK---ALAKLNHPNIVRYYTAWVEEPPLYIQMELCe 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  108 YSNLHDRLSTRPFLSLVEKK--WLAF-QLLLAVKQCHEKDICHGDIKCENVLLTSW-NWLYLADF----ASFKPTYIPYD 179
Cdd:cd13996   88 GGTLRDWIDRRNSSSKNDRKlaLELFkQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFglatSIGNQKRELNN 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  180 DPSDFSFFFDTRGQR---LCYLAPERfyEHGGE-TQvaqdaplkpSMDIFAVGCVIAELFLEGQPLFELAQLL-AYRRGQ 254
Cdd:cd13996  168 LNNNNNGNTSNNSVGigtPLYASPEQ--LDGENyNE---------KADIYSLGIILFEMLHPFKTAMERSTILtDLRNGI 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 15233564  255 HDPSQhleKIPDPGIRKMILHMIQLEPEARLSAEDYLQNY 294
Cdd:cd13996  237 LPESF---KAKHPKEADLIQSLLSKNPEERPSAEQLLRSL 273
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
29-292 2.82e-10

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: 62.82  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   29 LKEVLGRGRF---LKSIQCKHDEGLVVVKVYFKRGDSIDLREYERRLvkikDVFLSLEHPHVWPFQFWQETDKAAYLVRQ 105
Cdd:cd14086    5 LKEELGKGAFsvvRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREA----RICRLLKHPNIVRLHDSISEEGFHYLVFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  106 YFYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPTYIPYDDPSDF 184
Cdd:cd14086   81 LVTGgELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  185 SFFFDTRGqrlcYLAPErfyehggetqVAQDAPLKPSMDIFAVGcVIAELFLEGQPLFE-------LAQLLAyrrGQHD- 256
Cdd:cd14086  161 FGFAGTPG----YLSPE----------VLRKDPYGKPVDIWACG-VILYILLVGYPPFWdedqhrlYAQIKA---GAYDy 222
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 15233564  257 PSQHLEKIpDPGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14086  223 PSPEWDTV-TPEAKDLINQMLTVNPAKRITAAEALK 257
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
131-293 3.35e-10

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: 62.17  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  131 FQLLLAVKQCHEKD-----ICHGDIKCENVLLTSWNWLYLADF---------ASFKPTYI--PYddpsdfsfffdtrgqr 194
Cdd:cd08217  112 TQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFglarvlshdSSFAKTYVgtPY---------------- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  195 lcYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELfLEGQPLF------ELAQLLayRRGQHDPsqhlekIPD-- 266
Cdd:cd08217  176 --YMSPE----------LLNEQSYDEKSDIWSLGCLIYEL-CALHPPFqaanqlELAKKI--KEGKFPR------IPSry 234
                        170       180
                 ....*....|....*....|....*...
gi 15233564  267 -PGIRKMILHMIQLEPEARLSAEDYLQN 293
Cdd:cd08217  235 sSELNEVIKSMLNVDPDKRPSVEELLQL 262
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
29-168 4.40e-10

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


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 61.93  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   29 LKEVLGRGRF--LKSIQCKHDEGLVVVKVYFKRGDSIDL------REYErrLVKIkdvflsLEHPHVwpFQFWQ--ETDK 98
Cdd:cd14162    4 VGKTLGHGSYavVKKAYSTKHKCKVAIKIVSKKKAPEDYlqkflpREIE--VIKG------LKHPNL--ICFYEaiETTS 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233564   99 AAYLVRQYFYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF 168
Cdd:cd14162   74 RVYIIMELAENgDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDF 144
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
33-292 4.55e-10

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: 61.89  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   33 LGRGRFLKSIQCKHDEG--LVVVKVYFKRGDSID--LREYERRLVKIKdvflSLEHPH------VWpfqfwqETDKAAYL 102
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTgqKVAIKIVNKEKLSKEsvLMKVEREIAIMK----LIEHPNvlklydVY------ENKKYLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  103 VRQYFYS-NLHDRLSTRPFLSlvEKKWLAF--QLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADF--ASFKPTyip 177
Cdd:cd14081   79 VLEYVSGgELFDYLVKKGRLT--EKEARKFfrQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFgmASLQPE--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  178 yddpsdfSFFFDTRGQRLCYLAPE----RFYeHGgetqvaqdaplKPSmDIFAVGcVIAELFLEGQPLFE---LAQLL-A 249
Cdd:cd14081  154 -------GSLLETSCGSPHYACPEvikgEKY-DG-----------RKA-DIWSCG-VILYALLVGALPFDddnLRQLLeK 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 15233564  250 YRRGQHDpsqhlekIPD---PGIRKMILHMIQLEPEARLSAEDYLQ 292
Cdd:cd14081  213 VKRGVFH-------IPHfisPDAQDLLRRMLEVNPEKRITIEEIKK 251
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
132-291 8.47e-10

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: 60.95  E-value: 8.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  132 QLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPtyIPYDDPSDFsFFFDTRGQRLCYLAPErfyehggetq 211
Cdd:cd14165  110 QLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKR--CLRDENGRI-VLSKTFCGSAAYAAPE---------- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  212 VAQDAPLKPSM-DIFAVGCVIAELFLEGQPLFE--LAQLLAYRRGQH---DPSQHLekipDPGIRKMILHMIQLEPEARL 285
Cdd:cd14165  177 VLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDsnVKKMLKIQKEHRvrfPRSKNL----TSECKDLIYRLLQPDVSQRL 252

                 ....*.
gi 15233564  286 SAEDYL 291
Cdd:cd14165  253 CIDEVL 258
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
31-242 1.13e-09

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 60.90  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   31 EVLGRGRFLKSIQCKHDEG--LVVVKVYFKRGDSIDLREYERRLVKIkdvFLSLEHPHVWPFQFWQETDKAAYLVRQYFY 108
Cdd:cd07846    7 GLVGEGSYGMVMKCRHKETgqIVAIKKFLESEDDKMVKKIAMREIKM---LKQLRHENLVNLIEVFRRKKRWYLVFEFVD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  109 SNLHDRLSTRPF---LSLVeKKWLaFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFASFKPTYIPYDDPSDfs 185
Cdd:cd07846   84 HTVLDDLEKYPNgldESRV-RKYL-FQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVYTD-- 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15233564  186 fFFDTRgqrlCYLAPErfyehggetQVAQDAPLKPSMDIFAVGCVIAELfLEGQPLF 242
Cdd:cd07846  160 -YVATR----WYRAPE---------LLVGDTKYGKAVDVWAVGCLVTEM-LTGEPLF 201
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
19-305 1.29e-09

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: 61.57  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   19 HDLPSSYNLVlkEVLGRGRFLKSIQCKH--DEGLVVVKVYFKRgdSIDLREYERRLVKIKDVFL-SLEHPHVWPFQFWQE 95
Cdd:cd05602    3 HAKPSDFHFL--KVIGKGSFGKVLLARHksDEKFYAVKVLQKK--AILKKKEEKHIMSERNVLLkNVKHPFLVGLHFSFQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   96 TDKAAYLVRQY------FYSNLHDRLSTRPflslvEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFA 169
Cdd:cd05602   79 TTDKLYFVLDYinggelFYHLQRERCFLEP-----RARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  170 SFKPTYIPYDDPSDFsfffdtrgqrlC----YLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAELFLEGQPLFELA 245
Cdd:cd05602  154 LCKENIEPNGTTSTF-----------CgtpeYLAPE----------VLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRN 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  246 QLLAYRRGQHDPSQHLEKIPDPGiRKMILHMIQLEPEARLSAEDYLQNYVGVVFpnyFSP 305
Cdd:cd05602  213 TAEMYDNILNKPLQLKPNITNSA-RHLLEGLLQKDRTKRLGAKDDFTEIKNHIF---FSP 268
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
81-292 1.63e-09

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: 60.37  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   81 SLEHPHVWP----FQFWQ-ETDKAAYLVRQYFYSNLHDRLS--TRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCE 153
Cdd:cd07838   57 SFEHPNVVRlldvCHGPRtDRELKLTLVFEHVDQDLATYLDkcPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQ 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  154 NVLLTSWNWLYLADFASFKpTYipyddpsDFSFFFDTRGQRLCYLAPErfyehggetqVAQDAPLKPSMDIFAVGCVIAE 233
Cdd:cd07838  137 NILVTSDGQVKLADFGLAR-IY-------SFEMALTSVVVTLWYRAPE----------VLLQSSYATPVDMWSVGCIFAE 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  234 LFLEgQPLF----ELAQL-----LAYRRGQHD------------PSQHLEKIPD--PGIRK----MILHMIQLEPEARLS 286
Cdd:cd07838  199 LFNR-RPLFrgssEADQLgkifdVIGLPSEEEwprnsalprssfPSYTPRPFKSfvPEIDEegldLLKKMLTFNPHKRIS 277

                 ....*.
gi 15233564  287 AEDYLQ 292
Cdd:cd07838  278 AFEALQ 283
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
33-289 1.72e-09

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: 60.26  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   33 LGRGRFLKSIQCK--HDEGLVVVKVyFKRGDSIDLREYERRLVKIKDVFLS----------LEHPHVW--------PFQf 92
Cdd:cd14008    1 LGRGSFGKVKLALdtETGQLYAIKI-FNKSRLRKRREGKNDRGKIKNALDDvrreiaimkkLDHPNIVrlyeviddPES- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   93 wqetDKAaYLVRQYF-YSNLHDRLSTRPFLSLVEKK-WLAF-QLLLAVKQCHEKDICHGDIKCENVLLTSWNWLYLADFA 169
Cdd:cd14008   79 ----DKL-YLVLEYCeGGPVMELDSGDRVPPLPEETaRKYFrDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  170 SfkptyipyddpsdfSFFFDTRGQRL-------CYLAPERFYEHGGETQVaqdaplKPSmDIFAVGCVIAeLFLEGQPLF 242
Cdd:cd14008  154 V--------------SEMFEDGNDTLqktagtpAFLAPELCDGDSKTYSG------KAA-DIWALGVTLY-CLVFGRLPF 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15233564  243 ELAQLLA-YRRGQHDP-SQHLEKIPDPGIRKMILHMIQLEPEARLSAED 289
Cdd:cd14008  212 NGDNILElYEAIQNQNdEFPIPPELSPELKDLLRRMLEKDPEKRITLKE 260
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
29-292 1.98e-09

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: 59.80  E-value: 1.98e-09
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                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564   29 LKEVLGRGRFLKSIQCKHDEG--LVVVKVYFKR---GDSIDLREYERRLvkikDVFLSLEHPHVWPFQFWQETDKAAYLV 103
Cdd:cd14098    4 IIDRLGSGTFAEVKKAVEVETgkMRAIKQIVKRkvaGNDKNLQLFQREI----NILKSLEHPGIVRLIDWYEDDQHIYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233564  104 RQYFYS-NLHDRLSTRPFLSLVEKKWLAFQLLLAVKQCHEKDICHGDIKCENVLLTSWN--WLYLADFASFKPTYIpydd 180