NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|342187153|sp|P22219|]
View 

RecName: Full=Serine/threonine-protein kinase VPS15; AltName: Full=Golgi-retention defective mutant protein 8; AltName: Full=Vacuolar protein sorting-associated protein 15

Protein Classification

VPS15 family serine/threonine-protein kinase( domain architecture ID 12991011)

VPS15 family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Saccharomyces cerevisiae VPS15 that is required for cytoplasm to vacuole transport (Cvt) and autophagy as a part of the autophagy-specific VPS34 PI3-kinase complex I; contains WD40 repeats and may contain HEAT repeats

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
26-304 2.25e-153

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: 465.57  E-value: 2.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   26 EVHYVSQLNSSRFLKTCKALDPNGEIVIKVFIKPKDQYSLRPFLQRIRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQHL 105
Cdd:cd13980     1 DYLYDKSLGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLLELPNVLPFQKVIETDKAAYLIRQYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFiKPVYLPEDNPGEFLF 185
Cdd:cd13980    81 KYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASF-KPTYLPEDNPADFSY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 YFDTSKRRTCYLAPERFNSKLYQDGKS--NNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREflME 263
Cdd:cd13980   160 FFDTSRRRTCYIAPERFVDALTLDAESerRDGELTPAMDIFSLGCVIAELFTEGRPLFDLSQLLAYRKGEFSPEQV--LE 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 342187153  264 EMNSTDLRNLVLDMIQLDPSKRLSCDELLNKYRGIFFPDYF 304
Cdd:cd13980   238 KIEDPNIRELILHMIQRDPSKRLSAEDYLKKYRGKVFPEYF 278
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1080-1312 1.18e-09

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: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 61.20  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1080 PNSITSSAVSPgETPYLITGSDQGVIKIWNLKeiivGEVYSSSLTyDCSSTVTQITMIPNFDAFAVSSKDGQIIVLKVNh 1159
Cdd:cd00200     9 TGGVTCVAFSP-DGKLLATGSGDGTIKVWDLE----TGELLRTLK-GHTGPVRDVAASADGTYLASGSSDKTIRLWDLE- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1160 yqqesevkflNCECIRKinLKNFGKNEYAVrmrAFVNeEKSLLVALTNLSRVIIFDIRTLERLQIIENsprH-GAVSSIC 1238
Cdd:cd00200    82 ----------TGECVRT--LTGHTSYVSSV---AFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRG---HtDWVNSVA 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153 1239 IDEECCVLILGTTRGIIDIWDIRFNVLIRswSFGDH-APITHVevcQFYGKNSVIVVGGSSKTfLTIWNFVKGHC 1312
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVA--TLTGHtGEVNSV---AFSPDGEKLLSSSSDGT-IKLWDLSTGKC 211
 
Name Accession Description Interval E-value
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
26-304 2.25e-153

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: 465.57  E-value: 2.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   26 EVHYVSQLNSSRFLKTCKALDPNGEIVIKVFIKPKDQYSLRPFLQRIRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQHL 105
Cdd:cd13980     1 DYLYDKSLGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLLELPNVLPFQKVIETDKAAYLIRQYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFiKPVYLPEDNPGEFLF 185
Cdd:cd13980    81 KYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASF-KPTYLPEDNPADFSY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 YFDTSKRRTCYLAPERFNSKLYQDGKS--NNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREflME 263
Cdd:cd13980   160 FFDTSRRRTCYIAPERFVDALTLDAESerRDGELTPAMDIFSLGCVIAELFTEGRPLFDLSQLLAYRKGEFSPEQV--LE 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 342187153  264 EMNSTDLRNLVLDMIQLDPSKRLSCDELLNKYRGIFFPDYF 304
Cdd:cd13980   238 KIEDPNIRELILHMIQRDPSKRLSAEDYLKKYRGKVFPEYF 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
42-293 3.25e-29

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 118.02  E-value: 3.25e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153     42 CKALD-PNGEIV-IKVFIKPKDQYSLRPFLQRIRAQSfKLGQlPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPY 118
Cdd:smart00220   16 YLARDkKTGKLVaIKVIKKKKIKKDRERILREIKILK-KLKH-PNIVRLYDVFEDEDKLYLVMEYCEGgDLFDLLKKRGR 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPvylpednpgeflfyfdTSKRRTC- 195
Cdd:smart00220   94 LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFglARQLDP----------------GEKLTTFv 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    196 ----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF----NLSQLFKYKSNSydvNREFLMEEMN- 266
Cdd:smart00220  158 gtpeYMAPEVLLGKGY----------GKAVDIWSLGVILYELLT-GKPPFpgddQLLELFKKIGKP---KPPFPPPEWDi 223
                           250       260
                    ....*....|....*....|....*..
gi 342187153    267 STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:smart00220  224 SPEAKDLIRKLLVKDPEKRLTAEEALQ 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
50-292 1.42e-13

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 75.05  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   50 EIVIKVFikpKDQYSLRP-FLQRIRAQSFKLGQL--PHVLNYSKLIETNRAGYMIRQHLK-NNLYDRLSLRPYLQDIELK 125
Cdd:COG0515    34 PVALKVL---RPELAADPeARERFRREARALARLnhPNIVRVYDVGEEDGRPYLVMEYVEgESLADLLRRRGPLPPAEAL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  126 FIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEDN-----PGeflfyfdtskrrtcYLA 198
Cdd:COG0515   111 RILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFgiARALGGATLTQTGtvvgtPG--------------YMA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSklyqdgksnnGRLTKEMDIFSLGCVIAEIFAeGRPIFNLsqlfkykSNSYDVNREFLMEEMN---------STD 269
Cdd:COG0515   177 PEQARG----------EPVDPRSDVYSLGVTLYELLT-GRPPFDG-------DSPAELLRAHLREPPPppselrpdlPPA 238
                         250       260
                  ....*....|....*....|....
gi 342187153  270 LRNLVLDMIQLDPSKRL-SCDELL 292
Cdd:COG0515   239 LDAIVLRALAKDPEERYqSAAELA 262
Pkinase pfam00069
Protein kinase domain;
42-293 6.77e-13

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 69.58  E-value: 6.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    42 CKALDPNGEIVIKVFIKPKDQYSlrpFLQRIRA--QSFKLGQLPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPY 118
Cdd:pfam00069   18 AKHRDTGKIVAIKKIKKEKIKKK---KDKNILReiKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGgSLFDLLSEKGA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   119 LQDIELKFIAFQLLNALKdihnlnivhGDIKTENILVTSWnwciltdfaafikpvylpednpgeflfyfdtskrrtcYLA 198
Cdd:pfam00069   95 FSEREAKFIMKQILEGLE---------SGSSLTTFVGTPW-------------------------------------YMA 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   199 PERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIFnlsQLFKYKSNSYDVNREFLMEEMN----STDLRNLV 274
Cdd:pfam00069  129 PEVLGGNPY----------GPKVDVWSLGCILYELLT-GKPPF---PGINGNEIYELIIDQPYAFPELpsnlSEEAKDLL 194
                          250
                   ....*....|....*....
gi 342187153   275 LDMIQLDPSKRLSCDELLN 293
Cdd:pfam00069  195 KKLLKKDPSKRLTATQALQ 213
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1080-1312 1.18e-09

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: 61.20  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1080 PNSITSSAVSPgETPYLITGSDQGVIKIWNLKeiivGEVYSSSLTyDCSSTVTQITMIPNFDAFAVSSKDGQIIVLKVNh 1159
Cdd:cd00200     9 TGGVTCVAFSP-DGKLLATGSGDGTIKVWDLE----TGELLRTLK-GHTGPVRDVAASADGTYLASGSSDKTIRLWDLE- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1160 yqqesevkflNCECIRKinLKNFGKNEYAVrmrAFVNeEKSLLVALTNLSRVIIFDIRTLERLQIIENsprH-GAVSSIC 1238
Cdd:cd00200    82 ----------TGECVRT--LTGHTSYVSSV---AFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRG---HtDWVNSVA 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153 1239 IDEECCVLILGTTRGIIDIWDIRFNVLIRswSFGDH-APITHVevcQFYGKNSVIVVGGSSKTfLTIWNFVKGHC 1312
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVA--TLTGHtGEVNSV---AFSPDGEKLLSSSSDGT-IKLWDLSTGKC 211
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
109-154 2.45e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 53.71  E-value: 2.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENIL 154
Cdd:PHA03390   96 LFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVL 141
WD40 COG2319
WD40 repeat [General function prediction only];
1069-1261 1.40e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.06  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1069 GKLIATLmENEPNSITSSAVSP-GETpyLITGSDQGVIKIWNLKEiivGEVySSSLTYDcSSTVTQITMIPNFDAFAVSS 1147
Cdd:COG2319   236 GKLLRTL-TGHSGSVRSVAFSPdGRL--LASGSADGTVRLWDLAT---GEL-LRTLTGH-SGGVNSVAFSPDGKLLASGS 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1148 KDGQIIVLKVNHYQQesevkflncecirkinLKNFGKNEYAVRMRAFVNEEKSLLVALTNlSRVIIFDIRTLERLQIIEN 1227
Cdd:COG2319   308 DDGTVRLWDLATGKL----------------LRTLTGHTGAVRSVAFSPDGKTLASGSDD-GTVRLWDLATGELLRTLTG 370
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 342187153 1228 sprH-GAVSSICIDEECCVLILGTTRGIIDIWDIR 1261
Cdd:COG2319   371 ---HtGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
 
Name Accession Description Interval E-value
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
26-304 2.25e-153

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: 465.57  E-value: 2.25e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   26 EVHYVSQLNSSRFLKTCKALDPNGEIVIKVFIKPKDQYSLRPFLQRIRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQHL 105
Cdd:cd13980     1 DYLYDKSLGSTRFLKVARARHDEGLVVVKVFVKPDPALPLRSYKQRLEEIRDRLLELPNVLPFQKVIETDKAAYLIRQYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFiKPVYLPEDNPGEFLF 185
Cdd:cd13980    81 KYNLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASF-KPTYLPEDNPADFSY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 YFDTSKRRTCYLAPERFNSKLYQDGKS--NNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREflME 263
Cdd:cd13980   160 FFDTSRRRTCYIAPERFVDALTLDAESerRDGELTPAMDIFSLGCVIAELFTEGRPLFDLSQLLAYRKGEFSPEQV--LE 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 342187153  264 EMNSTDLRNLVLDMIQLDPSKRLSCDELLNKYRGIFFPDYF 304
Cdd:cd13980   238 KIEDPNIRELILHMIQRDPSKRLSAEDYLKKYRGKVFPEYF 278
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
42-293 3.25e-29

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 118.02  E-value: 3.25e-29
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153     42 CKALD-PNGEIV-IKVFIKPKDQYSLRPFLQRIRAQSfKLGQlPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPY 118
Cdd:smart00220   16 YLARDkKTGKLVaIKVIKKKKIKKDRERILREIKILK-KLKH-PNIVRLYDVFEDEDKLYLVMEYCEGgDLFDLLKKRGR 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPvylpednpgeflfyfdTSKRRTC- 195
Cdd:smart00220   94 LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFglARQLDP----------------GEKLTTFv 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    196 ----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF----NLSQLFKYKSNSydvNREFLMEEMN- 266
Cdd:smart00220  158 gtpeYMAPEVLLGKGY----------GKAVDIWSLGVILYELLT-GKPPFpgddQLLELFKKIGKP---KPPFPPPEWDi 223
                           250       260
                    ....*....|....*....|....*..
gi 342187153    267 STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:smart00220  224 SPEAKDLIRKLLVKDPEKRLTAEEALQ 250
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
33-293 2.91e-27

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: 111.21  E-value: 2.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   33 LNSSRFLKTCKALDPNG--EIVIKVFIKPKDQYSLRPFLQRIRAQSfKLgQLPHVLNYSKLIETNRAGYMIRQHLKN-NL 109
Cdd:cd00180     1 LGKGSFGKVYKARDKETgkKVAVKVIPKEKLKKLLEELLREIEILK-KL-NHPNIVKLYDVFETENFLYLVMEYCEGgSL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  110 YDRL-SLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIkpvylpeDNPGEFLFY 186
Cdd:cd00180    79 KDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFglAKDL-------DSDDSLLKT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  187 FDTSkRRTCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIfaegrpifnlsqlfkyksnsydvnreflmeemn 266
Cdd:cd00180   152 TGGT-TPPYYAPPELLGGRYY----------GPKVDIWSLGVILYEL--------------------------------- 187
                         250       260
                  ....*....|....*....|....*..
gi 342187153  267 sTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd00180   188 -EELKDLIRRMLQYDPKKRPSAKELLE 213
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
83-293 6.55e-21

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: 94.08  E-value: 6.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLK-NNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC 161
Cdd:cd05117    59 PNIVKLYEVFEDDKNLYLVMELCTgGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPD 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 I---LTDF--AAFIKpvylpednpgeflfyfDTSKRRTC-----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIA 231
Cdd:cd05117   139 SpikIIDFglAKIFE----------------EGEKLKTVcgtpyYVAPEVLKGKGY----------GKKCDIWSLG-VIL 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153  232 EIFAEGRPIF---NLSQLF-KYKSNSYDVNReflmEEMN--STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd05117   192 YILLCGYPPFygeTEQELFeKILKGKYSFDS----PEWKnvSEEAKDLIKRLLVVDPKKRLTAAEALN 255
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
42-293 1.96e-20

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: 93.15  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   42 CKALDpNGEIV-IKVF-IKPKDQYSLRPFLQRIRAqsfkLGQLPHVlNYSKLIETNRAG---YMIRQHLKNNLYDRLSLR 116
Cdd:cd07833    20 CRNKA-TGEIVaIKKFkESEDDEDVKKTALREVKV----LRQLRHE-NIVNLKEAFRRKgrlYLVFEYVERTLLELLEAS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  117 PYLQDIEL-KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNPgeflfYFDTSKRRtC 195
Cdd:cd07833    94 PGGLPPDAvRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDF-GFARALTARPASP-----LTDYVATR-W 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 YLAPERFNsklyqdGKSNNGrltKEMDIFSLGCVIAEIFAeGRPIF----NLSQLFK---------------YKSNSY-- 254
Cdd:cd07833   167 YRAPELLV------GDTNYG---KPVDVWAIGCIMAELLD-GEPLFpgdsDIDQLYLiqkclgplppshqelFSSNPRfa 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 342187153  255 -----DVNREFLMEEMNSTDLRNLVLDMIQ----LDPSKRLSCDELLN 293
Cdd:cd07833   237 gvafpEPSQPESLERRYPGKVSSPALDFLKaclrMDPKERLTCDELLQ 284
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
30-293 2.35e-20

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: 91.91  E-value: 2.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   30 VSQLNSSRFLKTCKALDPN-GEIVIKVFIKPKDQYSLRP-----FLQRIRaqsfKLGQLPHVLNYSKLIETNRAG--YMI 101
Cdd:cd05118     4 LRKIGEGAFGTVWLARDKVtGEKVAIKKIKNDFRHPKAAlreikLLKHLN----DVEGHPNIVKLLDVFEHRGGNhlCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  102 RQHLKNNLYDRLSLRPY-LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFAafikpvylpedn 179
Cdd:cd05118    80 FELMGMNLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLkLADFG------------ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  180 pgefLFYFDTSKRRTC------YLAPErfnsKLYQDgksnnGRLTKEMDIFSLGCVIAEIFaEGRPIF----NLSQLFKy 249
Cdd:cd05118   148 ----LARSFTSPPYTPyvatrwYRAPE----VLLGA-----KPYGSSIDIWSLGCILAELL-TGRPLFpgdsEVDQLAK- 212
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 342187153  250 ksnsydvnrefLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd05118   213 -----------IVRLLGTPEALDLLSKMLKYDPAKRITASQALA 245
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
30-293 6.37e-20

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: 91.04  E-value: 6.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   30 VSQLNSSRFLKTCKALD-PNGEIV-IKVFIKPKDQYSLRPFLQRiRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQHLKN 107
Cdd:cd14003     5 GKTLGEGSFGKVKLARHkLTGEKVaIKIIDKSKLKEEIEEKIKR-EIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  108 -NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwNWCI-LTDF--AAFIKpvylpednPGEF 183
Cdd:cd14003    84 gELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDK-NGNLkIIDFglSNEFR--------GGSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  184 LfyfDTSKRRTCYLAPERFNSKLYqDGksnngrltKEMDIFSLGcVIAEIFAEGRPIF---NLSQLFKyksnsYDVNREF 260
Cdd:cd14003   155 L---KTFCGTPAYAAPEVLLGRKY-DG--------PKADVWSLG-VILYAMLTGYLPFdddNDSKLFR-----KILKGKY 216
                         250       260       270
                  ....*....|....*....|....*....|...
gi 342187153  261 LMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14003   217 PIPSHLSPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
99-288 1.83e-17

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: 83.72  E-value: 1.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 YMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPvylpe 177
Cdd:cd05123    69 YLVLDYVPGgELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDF-GLAKE----- 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  178 dnpgeflFYFDTSKRRT-C----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIFnlsqlfkYKSN 252
Cdd:cd05123   143 -------LSSDGDRTYTfCgtpeYLAPEVLLGKGY----------GKAVDWWSLGVLLYEMLT-GKPPF-------YAEN 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 342187153  253 SYDVNREFLMEEMN-----STDLRNLVLDMIQLDPSKRLSC 288
Cdd:cd05123   198 RKEIYEKILKSPLKfpeyvSPEAKSLISGLLQKDPTKRLGS 238
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
28-292 2.64e-17

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 83.20  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   28 HYVSQLNSSRFLKTCKALDP-NGEI-VIKvfikpkdqYSLRPF---------LQRIRAQSfKLGQLPHVLNYSKLIETNR 96
Cdd:cd13997     3 HELEQIGSGSFSEVFKVRSKvDGCLyAVK--------KSKKPFrgpkeraraLREVEAHA-ALGQHPNIVRYYSSWEEGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   97 AGYMIRQHLKN----NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKP 172
Cdd:cd13997    74 HLYIQMELCENgslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  173 VYLPEDNPGEflfyfdtskrrTCYLAPERFNSKLYQDGKSnngrltkemDIFSLGCVIAEIfAEGRPifnlsqlFKYKSN 252
Cdd:cd13997   154 ETSGDVEEGD-----------SRYLAPELLNENYTHLPKA---------DIFSLGVTVYEA-ATGEP-------LPRNGQ 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 342187153  253 SYDVNRE----FLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd13997   206 QWQQLRQgklpLPPGLVLSQELTRLLKVMLDPDPTRRPTADQLL 249
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
125-290 8.82e-17

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: 82.26  E-value: 8.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEDNPGEFLFYFDTSKRRTC------- 195
Cdd:cd05581   104 RFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFgtAKVLGPDSSPESTKGDADSQIAYNQARAAsfvgtae 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 YLAPERFnsklyqdgksNNGRLTKEMDIFSLGCVIAEIFAeGRPIFnlsqlfkYKSNSYD-----VNREFLMEEMNSTDL 270
Cdd:cd05581   184 YVSPELL----------NEKPAGKSSDLWALGCIIYQMLT-GKPPF-------RGSNEYLtfqkiVKLEYEFPENFPPDA 245
                         170       180
                  ....*....|....*....|
gi 342187153  271 RNLVLDMIQLDPSKRLSCDE 290
Cdd:cd05581   246 KDLIQKLLVLDPSKRLGVNE 265
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
43-292 3.95e-16

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: 79.94  E-value: 3.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   43 KALDPNG--EIVIKVfikPKDQYSLRP-FLQRIRAQSFKLGQL--PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLR 116
Cdd:cd14014    18 RARDTLLgrPVAIKV---LRPELAEDEeFRERFLREARALARLshPNIVRVYDVGEDDGRPYIVMEYVEGgSLADLLRER 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  117 PYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEdnPGEFLFYFDtskrrt 194
Cdd:cd14014    95 GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFgiARALGDSGLTQ--TGSVLGTPA------ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 cYLAPERFnsklyqdgksNNGRLTKEMDIFSLGCVIAEIfAEGRPIFNLSQLFK--YKSNSYDVNREflmEEMN---STD 269
Cdd:cd14014   167 -YMAPEQA----------RGGPVDPRSDIYSLGVVLYEL-LTGRPPFDGDSPAAvlAKHLQEAPPPP---SPLNpdvPPA 231
                         250       260
                  ....*....|....*....|....
gi 342187153  270 LRNLVLDMIQLDPSKRL-SCDELL 292
Cdd:cd14014   232 LDAIILRALAKDPEERPqSAAELL 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
130-293 3.96e-16

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: 79.81  E-value: 3.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYlpeDNPGEFLfyfdtskrRTC-----YLAPERFNS 204
Cdd:cd08215   111 QICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFG--ISKVL---ESTTDLA--------KTVvgtpyYLSPELCEN 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 KLYqDGKSnngrltkemDIFSLGCVIAEIfAEGRPIF---NLSQLFkYKSnsydVNREFL-MEEMNSTDLRNLVLDMIQL 280
Cdd:cd08215   178 KPY-NYKS---------DIWALGCVLYEL-CTLKHPFeanNLPALV-YKI----VKGQYPpIPSQYSSELRDLVNSMLQK 241
                         170
                  ....*....|...
gi 342187153  281 DPSKRLSCDELLN 293
Cdd:cd08215   242 DPEKRPSANEILS 254
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
83-293 3.21e-15

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: 77.91  E-value: 3.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPY-LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC 161
Cdd:cd07829    58 PNIVKLLDVIHTENKLYLVFEYCDQDLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 ILTDF---AAFIKPVylpednpgeflfyfdtsKRRT------CYLAPE-RFNSKLYqdgksnngrlTKEMDIFSLGCVIA 231
Cdd:cd07829   138 KLADFglaRAFGIPL-----------------RTYThevvtlWYRAPEiLLGSKHY----------STAVDIWSVGCIFA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  232 EIfAEGRPIF----NLSQLFK--------------------YKSNSYDVNREFLMEEM---NSTDLRNLVLDMIQLDPSK 284
Cdd:cd07829   191 EL-ITGKPLFpgdsEIDQLFKifqilgtpteeswpgvtklpDYKPTFPKWPKNDLEKVlprLDPEGIDLLSKMLQYNPAK 269

                  ....*....
gi 342187153  285 RLSCDELLN 293
Cdd:cd07829   270 RISAKEALK 278
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
38-293 5.58e-15

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


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 76.66  E-value: 5.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   38 FLKTCKALDPNGEIVIKVFIKpkdqyslrpflQRIRAQSF----KLGQLP---HVL---------NYSKLI---ETNRAG 98
Cdd:cd14004    15 QVNLAIYKSKGKEVVIKFIFK-----------ERILVDTWvrdrKLGTVPleiHILdtlnkrshpNIVKLLdffEDDEFY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 Y--MIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKpvy 174
Cdd:cd14004    84 YlvMEKHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFgsAAYIK--- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  175 lpednPGEflfyFDTSKRRTCYLAPERFNSKLYqdgksnngrLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSY 254
Cdd:cd14004   161 -----SGP----FDTFVGTIDYAAPEVLRGNPY---------GGKEQDIWALGVLLYTLVFKENPFYNIEEILEADLRIP 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 342187153  255 dvnreFLMEEmnstDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14004   223 -----YAVSE----DLIDLISRMLNRDVGDRPTIEELLT 252
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
48-293 1.01e-14

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: 76.42  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   48 NGEIV-IKVFIKP---KDQY-SLRP--FLQRIRAQsfklgqlPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLR--PY 118
Cdd:cd07830    23 TGELVaIKKMKKKfysWEECmNLREvkSLRKLNEH-------PNIVKLKEVFRENDELYFVFEYMEGNLYQLMKDRkgKP 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFI--KPVYLPednpgeflfYFDTskRrt 194
Cdd:cd07830    96 FSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFglAREIrsRPPYTD---------YVST--R-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 CYLAPErfnsKLYQDGKSNNgrltkEMDIFSLGCVIAEIFAeGRPIFN----LSQLFKYKS------NSYDVNREFLMEE 264
Cdd:cd07830   163 WYRAPE----ILLRSTSYSS-----PVDIWALGCIMAELYT-LRPLFPgsseIDQLYKICSvlgtptKQDWPEGYKLASK 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 342187153  265 MN------------------STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd07830   233 LGfrfpqfaptslhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQ 279
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
33-292 1.13e-14

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 75.77  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   33 LNSSRFLKTCKA-LDPNGEIVIKVFIKPKDQYSLRPFLQRIRaqsfKLGQLPHVlNYSKLIetnraGY--------MIRQ 103
Cdd:cd14066     1 IGSGGFGTVYKGvLENGTVVAVKRLNEMNCAASKKEFLTELE----MLGRLRHP-NLVRLL-----GYclesdeklLVYE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  104 HLKN-NLYDRLSLRPYLQDIELKF---IAFQLLNALKDIHN---LNIVHGDIKTENILVTSWNWCILTDFAAFIKPvylp 176
Cdd:cd14066    71 YMPNgSLEDRLHCHKGSPPLPWPQrlkIAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLI---- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  177 edNPGEFLFYFDTSKRRTCYLAPERFNSklyqdgksnnGRLTKEMDIFSLGCVIAEIFAeGRPIF----------NLSQL 246
Cdd:cd14066   147 --PPSESVSKTSAVKGTIGYLAPEYIRT----------GRVSTKSDVYSFGVVLLELLT-GKPAVdenrenasrkDLVEW 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 342187153  247 FkyKSNSYDVNREFLMEEM--NSTDLRNLVLDMIQL-------DPSKRLSCDELL 292
Cdd:cd14066   214 V--ESKGKEELEDILDKRLvdDDGVEEEEVEALLRLallctrsDPSLRPSMKEVV 266
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
119-293 2.20e-14

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: 76.06  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEDNP--GEflfYFDTskRrt 194
Cdd:cd07852   104 LEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFglARSLSQLEEDDENPvlTD---YVAT--R-- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 CYLAPE-RFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF----NLSQLFKY-----KSNSYDV---NREF- 260
Cdd:cd07852   177 WYRAPEiLLGSTRY----------TKGVDMWSVGCILGEMLL-GKPLFpgtsTLNQLEKIievigRPSAEDIesiQSPFa 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 342187153  261 --LMEEMNSTDLRNLV----------LDMI----QLDPSKRLSCDELLN 293
Cdd:cd07852   246 atMLESLPPSRPKSLDelfpkaspdaLDLLkkllVFNPNKRLTAEEALR 294
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
106-293 3.73e-14

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: 74.05  E-value: 3.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikPVYLPEdnpgeflf 185
Cdd:cd14007    84 NGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGW---SVHAPS-------- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 yfdtSKRRT-----CYLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEiFAEGRPIFnlsqlfkyKSNSYD----- 255
Cdd:cd14007   153 ----NRRKTfcgtlDYLPPEMVEGKEY----------DYKVDIWSLGVLCYE-LLVGKPPF--------ESKSHQetykr 209
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 342187153  256 -VNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14007   210 iQNVDIKFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLN 248
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
100-292 5.14e-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: 74.46  E-value: 5.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  100 MIRQHLKNNLYdrlslrpyLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNW-CILTDF--AAFIKpvylp 176
Cdd:cd14137    92 VIRHYSKNKQT--------IPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGvLKLCDFgsAKRLV----- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  177 ednPGEflfyfdTSKRRTC---YLAPER-FNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF----------- 241
Cdd:cd14137   159 ---PGE------PNVSYICsryYRAPELiFGATDY----------TTAIDIWSAGCVLAELLL-GQPLFpgessvdqlve 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187153  242 --------NLSQLFKYKSNSYD--------VNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14137   219 iikvlgtpTREQIKAMNPNYTEfkfpqikpHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEAL 285
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
128-293 5.93e-14

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: 73.32  E-value: 5.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  128 AFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEdnpgeflfyFDTSKRRTCY-LAPERFNS 204
Cdd:cd06606   105 TRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFgcAKRLAEIATGE---------GTKSLRGTPYwMAPEVIRG 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 KLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQ----LFKY-KSNSYDVNREFLmeemnSTDLRNLVLDMIQ 279
Cdd:cd06606   176 EGY----------GRAADIWSLGCTVIEMATGKPPWSELGNpvaaLFKIgSSGEPPPIPEHL-----SEEAKDFLRKCLQ 240
                         170
                  ....*....|....
gi 342187153  280 LDPSKRLSCDELLN 293
Cdd:cd06606   241 RDPKKRPTADELLQ 254
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
124-293 6.45e-14

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 73.39  E-value: 6.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  124 LKFIAFQLLNALKDIHN-LNIVHGDIKTENILVTSWNWCILTDF--AAFIkpvylpEDNPGEFLFYFDTSKrrtcYLAPE 200
Cdd:cd06623   101 LAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFgiSKVL------ENTLDQCNTFVGTVT----YMSPE 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  201 RFNSKLYqdgkSNNGrltkemDIFSLGCVIAEiFAEGR-PIFNLSQL--FKYKSNSYDVNREFLMEEMNSTDLRNLVLDM 277
Cdd:cd06623   171 RIQGESY----SYAA------DIWSLGLTLLE-CALGKfPFLPPGQPsfFELMQAICDGPPPSLPAEEFSPEFRDFISAC 239
                         170
                  ....*....|....*.
gi 342187153  278 IQLDPSKRLSCDELLN 293
Cdd:cd06623   240 LQKDPKKRPSAAELLQ 255
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
129-293 7.04e-14

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: 73.50  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  129 FQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvylpednpgeFLFYFDTSKRRTC-------YLAPER 201
Cdd:cd13994   105 KQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEV-----------FGMPAEKESPMSAglcgsepYMAPEV 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  202 FNSKLYqdgksnNGRLtkeMDIFSLGCVIAEIFAeGRPIFNLS-------QLFKYKSNSYDVNREFLMEEMNsTDLRNLV 274
Cdd:cd13994   174 FTSGSY------DGRA---VDVWSCGIVLFALFT-GRFPWRSAkksdsayKAYEKSGDFTNGPYEPIENLLP-SECRRLI 242
                         170
                  ....*....|....*....
gi 342187153  275 LDMIQLDPSKRLSCDELLN 293
Cdd:cd13994   243 YRMLHPDPEKRITIDEALN 261
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
25-293 1.34e-13

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 73.24  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   25 EEVHYVSQLNSSRFLKTCKALDPNG---EIVIKVFikPKDQYSLRPFLQRIRAQSFKLGQL------PHVLNYSKLIETN 95
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYKAVPLRNtgkPVAIKVV--RKADLSSDNLKGSSRANILKEVQImkrlshPNIVKLLDFQESD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   96 RAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwnwcilTDFAAFIKPVY 174
Cdd:cd14096    79 EYYYIVLELADGgEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEP------IPFIPSIVKLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  175 LPEDNP-----GEF-------------LFYFDTSK-------RRTC----YLAPERFNSKLYqdgksnngrlTKEMDIFS 225
Cdd:cd14096   153 KADDDEtkvdeGEFipgvggggigivkLADFGLSKqvwdsntKTPCgtvgYTAPEVVKDERY----------SKKVDMWA 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187153  226 LGCVIAEIFAeGRPIF---NLSQLFKYKSNSydvNREFLM---EEMnSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14096   223 LGCVLYTLLC-GFPPFydeSIETLTEKISRG---DYTFLSpwwDEI-SKSAKDLISHLLTVDPAKRYDIDEFLA 291
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
79-293 1.36e-13

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: 72.98  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   79 LGQLPHVlNYSKLIE--TNRAG-------YMIRQHLKNNLyDRLSLRPYLQ--DIELKFIAFQLLNALKDIHNLNIVHGD 147
Cdd:cd07840    52 LQKLDHP-NVVRLKEivTSKGSakykgsiYMVFEYMDHDL-TGLLDNPEVKftESQIKCYMKQLLEGLQYLHSNGILHRD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  148 IKTENILVTSWNWCILTDF--AAFIKPvylpeDNPGEFlfyfdTSKRRTC-YLAPE-RFNSKLYqdgksnngrlTKEMDI 223
Cdd:cd07840   130 IKGSNILINNDGVLKLADFglARPYTK-----ENNADY-----TNRVITLwYRPPElLLGATRY----------GPEVDM 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  224 FSLGCVIAEIFaEGRPIFN----LSQL--------------------------FKYKSNSYDVNREFlMEEMNSTDLRNL 273
Cdd:cd07840   190 WSVGCILAELF-TGKPIFQgkteLEQLekifelcgspteenwpgvsdlpwfenLKPKKPYKRRLREV-FKNVIDPSALDL 267
                         250       260
                  ....*....|....*....|
gi 342187153  274 VLDMIQLDPSKRLSCDELLN 293
Cdd:cd07840   268 LDKLLTLDPKKRISADQALQ 287
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
50-292 1.42e-13

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 75.05  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   50 EIVIKVFikpKDQYSLRP-FLQRIRAQSFKLGQL--PHVLNYSKLIETNRAGYMIRQHLK-NNLYDRLSLRPYLQDIELK 125
Cdd:COG0515    34 PVALKVL---RPELAADPeARERFRREARALARLnhPNIVRVYDVGEEDGRPYLVMEYVEgESLADLLRRRGPLPPAEAL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  126 FIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEDN-----PGeflfyfdtskrrtcYLA 198
Cdd:COG0515   111 RILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFgiARALGGATLTQTGtvvgtPG--------------YMA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSklyqdgksnnGRLTKEMDIFSLGCVIAEIFAeGRPIFNLsqlfkykSNSYDVNREFLMEEMN---------STD 269
Cdd:COG0515   177 PEQARG----------EPVDPRSDVYSLGVTLYELLT-GRPPFDG-------DSPAELLRAHLREPPPppselrpdlPPA 238
                         250       260
                  ....*....|....*....|....
gi 342187153  270 LRNLVLDMIQLDPSKRL-SCDELL 292
Cdd:COG0515   239 LDAIVLRALAKDPEERYqSAAELA 262
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
42-293 1.82e-13

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: 72.46  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   42 CKALDPNGEIVIKVFIKPKDQYSLRPFLQR-IRAqsfkLGQLPHVlNYSKLIETNRAG---YMIRQHLKNNLYDRLSLRP 117
Cdd:cd07846    20 CRHKETGQIVAIKKFLESEDDKMVKKIAMReIKM----LKQLRHE-NLVNLIEVFRRKkrwYLVFEFVDHTVLDDLEKYP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  118 Y-LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVylpeDNPGEflFYFDTSKRRtCY 196
Cdd:cd07846    95 NgLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDF-GFARTL----AAPGE--VYTDYVATR-WY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  197 LAPERfnskLYQDGKSNngrltKEMDIFSLGCVIAEIFAeGRPIF----NLSQLFK----------YKSNSYDVNREFL- 261
Cdd:cd07846   167 RAPEL----LVGDTKYG-----KAVDVWAVGCLVTEMLT-GEPLFpgdsDIDQLYHiikclgnlipRHQELFQKNPLFAg 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 342187153  262 -----MEEMNSTDLR-----NLVLDM----IQLDPSKRLSCDELLN 293
Cdd:cd07846   237 vrlpeVKEVEPLERRypklsGVVIDLakkcLHIDPDKRPSCSELLH 282
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
119-293 2.47e-13

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: 71.82  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaafikpvylpedNPGEFLFYFDTSKRRT---- 194
Cdd:cd14008   105 LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDF------------GVSEMFEDGNDTLQKTagtp 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 CYLAPERFNSklyqDGKSNNGRLTkemDIFSLGCVIAeIFAEGRPIF---NLSQLFKYKSNSYDvnrEFLMEEMNSTDLR 271
Cdd:cd14008   173 AFLAPELCDG----DSKTYSGKAA---DIWALGVTLY-CLVFGRLPFngdNILELYEAIQNQND---EFPIPPELSPELK 241
                         170       180
                  ....*....|....*....|..
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14008   242 DLLRRMLEKDPEKRITLKEIKE 263
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
42-293 2.66e-13

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 72.02  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   42 CKALDpNGEIV-IKVFIKPKDQyslrPFLQRIRAQSFK-LGQLPHVlNYSKLIET---NRAGYMIRQHLKNNLYDRLSLR 116
Cdd:cd07847    20 CRNRE-TGQIVaIKKFVESEDD----PVIKKIALREIRmLKQLKHP-NLVNLIEVfrrKRKLHLVFEYCDHTVLNELEKN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  117 PY-LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNpgeflfYFDTSKRRtC 195
Cdd:cd07847    94 PRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDF-GFARILTGPGDD------YTDYVATR-W 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 YLAPERfnskLYQDGKSNngrltKEMDIFSLGCVIAEIFAeGRPIF----NLSQLFK---------------YKSNSY-- 254
Cdd:cd07847   166 YRAPEL----LVGDTQYG-----PPVDVWAIGCVFAELLT-GQPLWpgksDVDQLYLirktlgdliprhqqiFSTNQFfk 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 342187153  255 ----DVNREFLMEEMNSTDLRNLVLDMIQ----LDPSKRLSCDELLN 293
Cdd:cd07847   236 glsiPEPETREPLESKFPNISSPALSFLKgclqMDPTERLSCEELLE 282
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
58-293 2.67e-13

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 71.61  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   58 KPKDQYSLRPFLQRIRAQSfKLGQLPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSL-RPYLQDIEL-KFIAFQLLNA 134
Cdd:cd13993    41 KDGNDFQKLPQLREIDLHR-RVSRHPNIITLHDVFETEVAIYIVLEYCPNgDLFEAITEnRIYVGKTELiKNVFLQLIDA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  135 LKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFAAFIKPVYLPEDNPGeflfyfdtSKRrtcYLAPERFNSklyqDGKSN 213
Cdd:cd13993   120 VKHCHSLGIYHRDIKPENILLSQDEGTVkLCDFGLATTEKISMDFGVG--------SEF---YMAPECFDE----VGRSL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  214 NGRLTKEMDIFSLG-CVIAEIFA--------EGRPIFNlsqlfKYKSNSYDVNREFLMEemnSTDLRNLVLDMIQLDPSK 284
Cdd:cd13993   185 KGYPCAAGDIWSLGiILLNLTFGrnpwkiasESDPIFY-----DYYLNSPNLFDVILPM---SDDFYNLLRQIFTVNPNN 256

                  ....*....
gi 342187153  285 RLSCDELLN 293
Cdd:cd13993   257 RILLPELQL 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
127-293 3.53e-13

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


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 71.27  E-value: 3.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKpvylpednpGEFLFyfdTSKRRTCYLAPERFNS 204
Cdd:cd08530   108 IFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLgiSKVLK---------KNLAK---TQIGTPLYAAPEVWKG 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 KLYqDGKSnngrltkemDIFSLGCVIAEIfAEGRPIFN---LSQL-FKYKSNSYDVnreflMEEMNSTDLRNLVLDMIQL 280
Cdd:cd08530   176 RPY-DYKS---------DIWSLGCLLYEM-ATFRPPFEartMQELrYKVCRGKFPP-----IPPVYSQDLQQIIRSLLQV 239
                         170
                  ....*....|...
gi 342187153  281 DPSKRLSCDELLN 293
Cdd:cd08530   240 NPKKRPSCDKLLQ 252
Pkinase pfam00069
Protein kinase domain;
42-293 6.77e-13

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 69.58  E-value: 6.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    42 CKALDPNGEIVIKVFIKPKDQYSlrpFLQRIRA--QSFKLGQLPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPY 118
Cdd:pfam00069   18 AKHRDTGKIVAIKKIKKEKIKKK---KDKNILReiKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGgSLFDLLSEKGA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   119 LQDIELKFIAFQLLNALKdihnlnivhGDIKTENILVTSWnwciltdfaafikpvylpednpgeflfyfdtskrrtcYLA 198
Cdd:pfam00069   95 FSEREAKFIMKQILEGLE---------SGSSLTTFVGTPW-------------------------------------YMA 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   199 PERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIFnlsQLFKYKSNSYDVNREFLMEEMN----STDLRNLV 274
Cdd:pfam00069  129 PEVLGGNPY----------GPKVDVWSLGCILYELLT-GKPPF---PGINGNEIYELIIDQPYAFPELpsnlSEEAKDLL 194
                          250
                   ....*....|....*....
gi 342187153   275 LDMIQLDPSKRLSCDELLN 293
Cdd:pfam00069  195 KKLLKKDPSKRLTATQALQ 213
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
50-293 9.14e-13

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: 69.73  E-value: 9.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   50 EIVIKVFIKPK-DQYSLRPFLQRIraQSFKLGQLPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFI 127
Cdd:cd14071    27 EVAIKIIDKSQlDEENLKKIYREV--QIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNgEIFDYLAQHGRMSEKEARKK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  128 AFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTD--FAAFIKpvylpednPGEFLFYFDTSKRrtcYLAPERFNSK 205
Cdd:cd14071   105 FWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADfgFSNFFK--------PGELLKTWCGSPP---YAAPEVFEGK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  206 LYqDGksnngrltKEMDIFSLGCVIAEIFAEGRPiFNLSQLFKYKSNSydVNREFLMEEMNSTDLRNLVLDMIQLDPSKR 285
Cdd:cd14071   174 EY-EG--------PQLDIWSLGVVLYVLVCGALP-FDGSTLQTLRDRV--LSGRFRIPFFMSTDCEHLIRRMLVLDPSKR 241

                  ....*...
gi 342187153  286 LSCDELLN 293
Cdd:cd14071   242 LTIEQIKK 249
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
114-293 1.70e-12

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 69.10  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  114 SLRPYLQDIELKFIAFQLLNALKDI-------HNLNIVHGDIKTENILVTSwNWCI-LTDFaafikpvylpednpGEFLF 185
Cdd:cd13999    76 SLYDLLHKKKIPLSWSLRLKIALDIargmnylHSPPIIHRDLKSLNILLDE-NFTVkIADF--------------GLSRI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 YFDTSKRRT------CYLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNRE 259
Cdd:cd13999   141 KNSTTEKMTgvvgtpRWMAPEVLRGEPY----------TEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRP 210
                         170       180       190
                  ....*....|....*....|....*....|....
gi 342187153  260 FLMEEMnSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd13999   211 PIPPDC-PPELSKLIKRCWNEDPEKRPSFSEIVK 243
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
130-293 2.04e-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: 69.25  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSwNWCI-LTDF--AAFIKPVYLPEdNPGEFLFYFDTskrrTCYLAPERFNSkl 206
Cdd:cd06626   107 QLLEGLAYLHENGIVHRDIKPANIFLDS-NGLIkLGDFgsAVKLKNNTTTM-APGEVNSLVGT----PAYMAPEVITG-- 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  207 yqDGKSNNGRltkEMDIFSLGCVIAEIFAEGRPIFNLSQLFKyksnsydvnrefLM-------------EEMNSTDLRNL 273
Cdd:cd06626   179 --NKGEGHGR---AADIWSLGCVVLEMATGKRPWSELDNEWA------------IMyhvgmghkppipdSLQLSPEGKDF 241
                         170       180
                  ....*....|....*....|
gi 342187153  274 VLDMIQLDPSKRLSCDELLN 293
Cdd:cd06626   242 LSRCLESDPKKRPTASELLD 261
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
83-293 2.12e-12

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: 69.34  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWN-W 160
Cdd:cd14084    71 PCIIKIEDFFDAEDDYYIVLELMEGgELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeE 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  161 CIL--TDFaafikpvylpednpGEFLFYFDTSKRRT-C----YLAPERFNsklyqdgksNNGRL--TKEMDIFSLGCVIA 231
Cdd:cd14084   151 CLIkiTDF--------------GLSKILGETSLMKTlCgtptYLAPEVLR---------SFGTEgyTRAVDCWSLGVILF 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187153  232 EIFAeGRPIFNLSqlfkYKSNSYD---VNRE--FLMEEMNSTDLR--NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14084   208 ICLS-GYPPFSEE----YTQMSLKeqiLSGKytFIPKAWKNVSEEakDLVKKMLVVDPSRRPSIEEALE 271
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
54-293 3.69e-12

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: 68.05  E-value: 3.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   54 KVFIK--PKDQYSLRPFLQRI-RAQSF-KLGQLPHVLNYSKLIETNRAGYMIRQHL-KNNLYDRLSLRPYLQDIELKFIA 128
Cdd:cd14081    28 KVAIKivNKEKLSKESVLMKVeREIAImKLIEHPNVLKLYDVYENKKYLYLVLEYVsGGELFDYLVKKGRLTEKEARKFF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  129 FQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEdnpgeflfyfdTSkrrtC----YLAPERF 202
Cdd:cd14081   108 RQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFgmASLQPEGSLLE-----------TS----CgsphYACPEVI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  203 NSKLYQDGKSnngrltkemDIFSLGcVIAEIFAEGRPIF---NLSQLF-KYKsnsydvNREFLMEEMNSTDLRNLVLDMI 278
Cdd:cd14081   173 KGEKYDGRKA---------DIWSCG-VILYALLVGALPFdddNLRQLLeKVK------RGVFHIPHFISPDAQDLLRRML 236
                         250
                  ....*....|....*
gi 342187153  279 QLDPSKRLSCDELLN 293
Cdd:cd14081   237 EVNPEKRITIEEIKK 251
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
99-293 4.13e-12

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: 68.06  E-value: 4.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 YMIRQH-------LKNNLYD--RLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI--LTDFa 167
Cdd:cd14133    70 FYFKNHlcivfelLSQNLYEflKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQikIIDF- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  168 afikpvylpednpGEFLFyfdTSKRRTCYL------APERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPif 241
Cdd:cd14133   149 -------------GSSCF---LTQRLYSYIqsryyrAPEVILGLPY----------DEKIDMWSLGCILAELYT-GEP-- 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187153  242 nlsqLFKYKSNSYDVNR---------EFLMEEMNSTD--LRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14133   200 ----LFPGASEVDQLARiigtigippAHMLDQGKADDelFVDFLKKLLEIDPKERPTASQALS 258
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
125-286 6.20e-12

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


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 67.63  E-value: 6.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDNPGEFLFYFD---TSKRRTC----YL 197
Cdd:cd05579    96 RIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKLSIQKKSNGapeKEDRRIVgtpdYL 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  198 APERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEiFAEGRPIFNLS---QLFKyKSNSYDVNREflmEEMN-STDLRNL 273
Cdd:cd05579   176 APEILLGQGH----------GKTVDWWSLGVILYE-FLVGIPPFHAEtpeEIFQ-NILNGKIEWP---EDPEvSDEAKDL 240
                         170
                  ....*....|...
gi 342187153  274 VLDMIQLDPSKRL 286
Cdd:cd05579   241 ISKLLTPDPEKRL 253
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
42-293 7.04e-12

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 67.23  E-value: 7.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   42 CKALD-PNGEIV-IKVfIKPKDQYSLRPFLQRIRAqsFKLGQLPHVLNYSKLIETNRAGYMIRQHL-KNNLYDRLSLRPY 118
Cdd:cd05122    17 YKARHkKTGQIVaIKK-INLESKEKKESILNEIAI--LKKCKHPNIVKYYGSYLKKDELWIVMEFCsGGSLKDLLKNTNK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 -LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIkpvylpedNPGEFLFYFDTSKrrtC 195
Cdd:cd05122    94 tLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFglSAQL--------SDGKTRNTFVGTP---Y 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 YLAPERFNSKLYqDGKSnngrltkemDIFSLGCVIAEIfAEGR-PIFNL---SQLFKYKSNsydVNREFLMEEMNSTDLR 271
Cdd:cd05122   163 WMAPEVIQGKPY-GFKA---------DIWSLGITAIEM-AEGKpPYSELppmKALFLIATN---GPPGLRNPKKWSKEFK 228
                         250       260
                  ....*....|....*....|..
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd05122   229 DFLKKCLQKDPEKRPTAEQLLK 250
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
83-292 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: 66.97  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNwc 161
Cdd:cd14167    61 PNIVALDDIYESGGHLYLIMQLVSGgELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLD-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 ilTDFAAFIKPVYLPE-DNPGEFLfyfDTSKRRTCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIAEIFAEGRPI 240
Cdd:cd14167   139 --EDSKIMISDFGLSKiEGSGSVM---STACGTPGYVAPEVLAQKPY----------SKAVDCWSIG-VIAYILLCGYPP 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 342187153  241 F---NLSQLF-KYKSNSYDVNREFLMEEMNSTdlRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14167   203 FydeNDAKLFeQILKAEYEFDSPYWDDISDSA--KDFIQHLMEKDPEKRFTCEQAL 256
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
122-293 1.45e-11

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 66.53  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  122 IELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC-----ILTDFAAFIKpvylpednpgefLFYFDTSKRRTC- 195
Cdd:cd13982    99 LEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHgnvraMISDFGLCKK------------LDVGRSSFSRRSg 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 ------YLAPERFNSklyqdgkSNNGRLTKEMDIFSLGCVIAEIFAEGRPIF--NLSQLFKYKSNSYDVNREFLMEEmNS 267
Cdd:cd13982   167 vagtsgWIAPEMLSG-------STKRRQTRAVDIFSLGCVFYYVLSGGSHPFgdKLEREANILKGKYSLDKLLSLGE-HG 238
                         170       180
                  ....*....|....*....|....*.
gi 342187153  268 TDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd13982   239 PEAQDLIERMIDFDPEKRPSAEEVLN 264
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
127-295 2.71e-11

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: 65.78  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDF--AAFIKPVyLPEDNPGEFLFYFDTSKRRT-----CYLA 198
Cdd:cd13996   112 LFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVkIGDFglATSIGNQ-KRELNNLNNNNNGNTSNNSVgigtpLYAS 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFN----LSQLFKYKSNSYdvnrefLMEEMNstDLRNLV 274
Cdd:cd13996   191 PEQLDGENY----------NEKADIYSLGIILFEMLHPFKTAMErstiLTDLRNGILPES------FKAKHP--KEADLI 252
                         170       180
                  ....*....|....*....|.
gi 342187153  275 LDMIQLDPSKRLSCDELLNKY 295
Cdd:cd13996   253 QSLLSKNPEERPSAEQLLRSL 273
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
55-302 2.85e-11

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 66.19  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   55 VFI---KPKDQYSLR---PFLQRIRAQSFKLGQL--PHVLNYSKLIETNRAGYM-----IRQHLKNNLYDRLSLRPY--- 118
Cdd:cd14011    26 VFVfekKQLEEYSKRdreQILELLKRGVKQLTRLrhPRILTVQHPLEESRESLAfatepVFASLANVLGERDNMPSPppe 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 -----LQDIELKFIAFQLLNALKDIHN-LNIVHGDIKTENILVTS---WnwcILTDFAAFIKPvylpEDNPGEFLFY--F 187
Cdd:cd14011   106 lqdykLYDVEIKYGLLQISEALSFLHNdVKLVHGNICPESVVINSngeW---KLAGFDFCISS----EQATDQFPYFreY 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  188 DTSKRRTC-----YLAPERFNSKlyqdgksnngRLTKEMDIFSLGCVIAEIFAEGRPIFNL-SQLFKYKSNSYDVNR-EF 260
Cdd:cd14011   179 DPNLPPLAqpnlnYLAPEYILSK----------TCDPASDMFSLGVLIYAIYNKGKPLFDCvNNLLSYKKNSNQLRQlSL 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 342187153  261 LMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLnkyRGIFFPD 302
Cdd:cd14011   249 SLLEKVPEELRDHVKTLLNVTPEVRPDAEQLS---KIPFFDD 287
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
92-241 7.53e-11

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 65.40  E-value: 7.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   92 IETNRAGYMIRQHLKNNLYdRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwnWCILT--DFAaf 169
Cdd:cd07849    77 FESFKDVYIVQELMETDLY-KLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNT--NCDLKicDFG-- 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187153  170 IKPVYLPEDNPGEFLF-YFDTSkrrtCYLAPE-RFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF 241
Cdd:cd07849   152 LARIADPEHDHTGFLTeYVATR----WYRAPEiMLNSKGY----------TKAIDIWSVGCILAEMLS-NRPLF 210
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
54-293 7.90e-11

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 64.33  E-value: 7.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   54 KVFIKPKDQYSLRPFLQRIRAQSFKLGQL--PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQ 130
Cdd:cd14078    30 KVAIKIMDKKALGDDLPRVKTEIEALKNLshQHICRLYHVIETDNKIFMVLEYCPGgELFDYIVAKDRLSEDEARVFFRQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  131 LLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDNpgeflfyFDTSKRRTCYLAPERFNSKLYqdg 210
Cdd:cd14078   110 IVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDHH-------LETCCGSPAYAAPELIQGKPY--- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  211 ksnngrLTKEMDIFSLGCVIAEIFAEGRPiF---NLSQLF-KYKSNSYDVNrEFLmeemnSTDLRNLVLDMIQLDPSKRL 286
Cdd:cd14078   180 ------IGSEADVWSMGVLLYALLCGFLP-FdddNVMALYrKIQSGKYEEP-EWL-----SPSSKLLLDQMLQVDPKKRI 246

                  ....*..
gi 342187153  287 SCDELLN 293
Cdd:cd14078   247 TVKELLN 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
130-293 8.31e-11

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


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 64.35  E-value: 8.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEdnpgeflfyfdTSKRRTCYLAPERFNSKly 207
Cdd:cd06632   110 QILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFgmAKHVEAFSFAK-----------SFKGSPYWMAPEVIMQK-- 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  208 qdgksnNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQ---LFKYkSNSYDVNrefLMEEMNSTDLRNLVLDMIQLDPSK 284
Cdd:cd06632   177 ------NSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGvaaIFKI-GNSGELP---PIPDHLSPDAKDFIRLCLQRDPED 246

                  ....*....
gi 342187153  285 RLSCDELLN 293
Cdd:cd06632   247 RPTASQLLE 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
49-293 8.37e-11

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 63.97  E-value: 8.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   49 GEIV-IKVFIKPK-DQYSLRPFLQRIRAqsFKLGQLPHVLNYSKLIETNRAGYMIRQhLKN--NLYDRLSLRPYLQDIEL 124
Cdd:cd14074    28 GEKVaVKVIDKTKlDDVSKAHLFQEVRC--MKLVQHPNVVRLYEVIDTQTKLYLILE-LGDggDMYDYIMKHENGLNEDL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAF-QLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFAafikpvYLPEDNPGEFLfyfDTSKRRTCYLAPERF 202
Cdd:cd14074   105 ARKYFrQIVSAISYCHKLHVVHRDLKPENVVFFEKQGLVkLTDFG------FSNKFQPGEKL---ETSCGSLAYSAPEIL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  203 NSKLYqDGKSnngrltkeMDIFSLGcVIAEIFAEGRPIFNLSQLFKYKSNSYDVnrEFLMEEMNSTDLRNLVLDMIQLDP 282
Cdd:cd14074   176 LGDEY-DAPA--------VDIWSLG-VILYMLVCGQPPFQEANDSETLTMIMDC--KYTVPAHVSPECKDLIRRMLIRDP 243
                         250
                  ....*....|.
gi 342187153  283 SKRLSCDELLN 293
Cdd:cd14074   244 KKRASLEEIEN 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
83-293 8.93e-11

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: 64.13  E-value: 8.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC 161
Cdd:cd14080    62 PNIIQVYSIFERGSKVFIFMEYAEHgDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNV 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 ILTDFaAFIKpvYLPEDNPGEFlfyfdtSKrrT-C----YLAPERFNSKLYqDGKSNngrltkemDIFSLGCVIAeIFAE 236
Cdd:cd14080   142 KLSDF-GFAR--LCPDDDGDVL------SK--TfCgsaaYAAPEILQGIPY-DPKKY--------DIWSLGVILY-IMLC 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187153  237 GRPIF---NLSQLFKYKSN---SYDVNREFLmeemnSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14080   201 GSMPFddsNIKKMLKDQQNrkvRFPSSVKKL-----SPECKDLIDQLLEPDPTKRATIEEILN 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
119-292 1.46e-10

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 64.47  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwNwCILT--DF--AAFIkpvyLPEDNPGEFLFYFDTskrRT 194
Cdd:cd07834   100 LTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNS-N-CDLKicDFglARGV----DPDEDKGFLTEYVVT---RW 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 cYLAPE-RFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF----NLSQL--------------FKYKSNsyD 255
Cdd:cd07834   171 -YRAPElLLSSKKY----------TKAIDIWSVGCIFAELLT-RKPLFpgrdYIDQLnlivevlgtpseedLKFISS--E 236
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 342187153  256 VNREFL-------------MEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd07834   237 KARNYLkslpkkpkkplseVFPGASPEAIDLLEKMLVFNPKKRITADEAL 286
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
78-286 1.48e-10

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


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 63.96  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   78 KLGQLPHVLNYSKLIETNRAGYMIR--QHLKNNLYDRLSLrPYLQDIEL---------------KFIAFQLLNALKDIHN 140
Cdd:cd14209    41 KLKQVEHTLNEKRILQAINFPFLVKleYSFKDNSNLYMVM-EYVPGGEMfshlrrigrfsephaRFYAAQIVLAFEYLHS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  141 LNIVHGDIKTENILVTSWNWCILTDFaAFIKPVylpednpgeflfyfdtsKRRT---C----YLAPERFNSKLYqdgksn 213
Cdd:cd14209   120 LDLIYRDLKPENLLIDQQGYIKVTDF-GFAKRV-----------------KGRTwtlCgtpeYLAPEIILSKGY------ 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153  214 ngrlTKEMDIFSLGCVIAEiFAEGRPIFNLSQLFKYksnsYD--VNREFLMEEMNSTDLRNLVLDMIQLDPSKRL 286
Cdd:cd14209   176 ----NKAVDWWALGVLIYE-MAAGYPPFFADQPIQI----YEkiVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRF 241
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
118-294 1.72e-10

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 63.47  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  118 YLQDIELKFIAFQLLNALKDIHNLNIV---HGDIKTENILVTSWNWCILTDFAAfIKPVYLPEDNPGEFLFYFDTSKRRt 194
Cdd:cd13986   102 FFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGS-MNPARIEIEGRREALALQDWAAEH- 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 C---YLAPERFNSKLYQDgksnngrLTKEMDIFSLGCVI-AEIFAEG--RPIFN---------LSQLFKYKSNSYdvnre 259
Cdd:cd13986   180 CtmpYRAPELFDVKSHCT-------IDEKTDIWSLGCTLyALMYGESpfERIFQkgdslalavLSGNYSFPDNSR----- 247
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 342187153  260 flmeemNSTDLRNLVLDMIQLDPSKRLSCDELLNK 294
Cdd:cd13986   248 ------YSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
100-293 1.87e-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: 63.33  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  100 MIRQHLKNNLYdrlslrpylqdIELKFI---AFQLLNALKDIHNLN-----IVHGDIKTENILVTSWNWCILTDFAaFIK 171
Cdd:cd08217    91 LIKKCKKENQY-----------IPEEFIwkiFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFG-LAR 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  172 pvYLPEDnpgeflfyfdTSKRRTC-----YLAPERFNSKLYqDGKSnngrltkemDIFSLGCVIAEIFAeGRPIF---NL 243
Cdd:cd08217   159 --VLSHD----------SSFAKTYvgtpyYMSPELLNEQSY-DEKS---------DIWSLGCLIYELCA-LHPPFqaaNQ 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 342187153  244 SQLFKyKSNSYDVNReflMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd08217   216 LELAK-KIKEGKFPR---IPSRYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
124-292 1.93e-10

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 63.20  E-value: 1.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  124 LKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFAAFIKpvyLPEDNPgeflfYFDTSKRRTCYLAPERF 202
Cdd:cd06624   110 IGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVkISDFGTSKR---LAGINP-----CTETFTGTLQYMAPEVI 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  203 NSKLYQDGksnngrltKEMDIFSLGCVIAEIfAEGRPIF---NLSQLFKYKSNSYDVNREfLMEEMnSTDLRNLVLDMIQ 279
Cdd:cd06624   182 DKGQRGYG--------PPADIWSLGCTIIEM-ATGKPPFielGEPQAAMFKVGMFKIHPE-IPESL-SEEAKSFILRCFE 250
                         170
                  ....*....|...
gi 342187153  280 LDPSKRLSCDELL 292
Cdd:cd06624   251 PDPDKRATASDLL 263
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
106-292 2.01e-10

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 63.14  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvYLPEDNPGEFLf 185
Cdd:cd14093    93 KGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFG------FATRLDEGEKL- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 yfdtskRRTC----YLAPERFNSKLYQDGKSnngrLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKsNSYDVNREFL 261
Cdd:cd14093   166 ------RELCgtpgYLAPEVLKCSMYDNAPG----YGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLR-NIMEGKYEFG 234
                         170       180       190
                  ....*....|....*....|....*....|...
gi 342187153  262 MEEMN--STDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14093   235 SPEWDdiSDTAKDLISKLLVVDPKKRLTAEEAL 267
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
109-286 2.19e-10

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 63.78  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYLPEDNPGEFLFYFD 188
Cdd:cd05614    92 LFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFG--LSKEFLTEEKERTYSFCGT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  189 TSkrrtcYLAPERFNsklyqdGKSNNGrltKEMDIFSLGCVIAEIFAEGRPiFNLSqlfKYKSNSYDVNREFL-----ME 263
Cdd:cd05614   170 IE-----YMAPEIIR------GKSGHG---KAVDWWSLGILMFELLTGASP-FTLE---GEKNTQSEVSRRILkcdppFP 231
                         170       180
                  ....*....|....*....|...
gi 342187153  264 EMNSTDLRNLVLDMIQLDPSKRL 286
Cdd:cd05614   232 SFIGPVARDLLQKLLCKDPKKRL 254
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
119-292 2.85e-10

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 63.58  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVylPEDNPGEFLFYFDTSkrrtCY 196
Cdd:cd07857   102 LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFglARGFSEN--PGENAGFMTEYVATR----WY 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  197 LAPERFNSklyqdgksnNGRLTKEMDIFSLGCVIAEIFAeGRPIF-------NLSQLFKY-------------KSNSYDV 256
Cdd:cd07857   176 RAPEIMLS---------FQSYTKAIDVWSVGCILAELLG-RKPVFkgkdyvdQLNQILQVlgtpdeetlsrigSPKAQNY 245
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 342187153  257 NREF-LMEEMN--------STDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd07857   246 IRSLpNIPKKPfesifpnaNPLALDLLEKLLAFDPTKRISVEEAL 290
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
78-303 3.12e-10

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 62.63  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   78 KLGQLPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVT 156
Cdd:cd14182    65 KVSGHPNIIQLKDTYETNTFFFLVFDLMKKgELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  157 SWNWCILTDFAafikpvYLPEDNPGEFLfyfdtskRRTC----YLAPERFNSKLyqdgKSNNGRLTKEMDIFSLGCVIAE 232
Cdd:cd14182   145 DDMNIKLTDFG------FSCQLDPGEKL-------REVCgtpgYLAPEIIECSM----DDNHPGYGKEVDMWSTGVIMYT 207
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187153  233 IFAEGRPIFNLSQLFKYK---SNSYdvnrEFLMEEMN--STDLRNLVLDMIQLDPSKRLSCDELLNKyrgIFFPDY 303
Cdd:cd14182   208 LLAGSPPFWHRKQMLMLRmimSGNY----QFGSPEWDdrSDTVKDLISRFLVVQPQKRYTAEEALAH---PFFQQY 276
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
119-293 3.20e-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: 62.27  E-value: 3.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVylpednpgEFLFYFDTSKRRT-CYL 197
Cdd:cd14002    96 LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDF-GFARAM--------SCNTLVLTSIKGTpLYM 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  198 APERFNSKLYqDGKSnngrltkemDIFSLGCVIAEIFAeGRP------IFNLSQLFKYKSNSYDvnreflmEEMnSTDLR 271
Cdd:cd14002   167 APELVQEQPY-DHTA---------DLWSLGCILYELFV-GQPpfytnsIYQLVQMIVKDPVKWP-------SNM-SPEFK 227
                         170       180
                  ....*....|....*....|..
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14002   228 SFLQGLLNKDPSKRLSWPDLLE 249
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
49-293 4.19e-10

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 61.94  E-value: 4.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   49 GEiVIKVFIKPKDQ-YSLRPFLQRIRAQSFKLGQLPHVLNYSKL------IETNRAgYMIRQHL-------KNNLYDRLS 114
Cdd:cd14050    15 GE-VFKVRSREDGKlYAVKRSRSRFRGEKDRKRKLEEVERHEKLgehpncVRFIKA-WEEKGILyiqtelcDTSLQQYCE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  115 LRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvyLPEDNPGeflfyfDTSKRRT 194
Cdd:cd14050    93 ETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE---LDKEDIH------DAQEGDP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 CYLAPERFnsklyqdgksnNGRLTKEMDIFSLGCVIAEIFAegrpifNLsQLFKYKSNSYDVNREFLMEEMN---STDLR 271
Cdd:cd14050   164 RYMAPELL-----------QGSFTKAADIFSLGITILELAC------NL-ELPSGGDGWHQLRQGYLPEEFTaglSPELR 225
                         250       260
                  ....*....|....*....|..
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14050   226 SIIKLMMDPDPERRPTAEDLLA 247
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
66-288 5.16e-10

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 62.33  E-value: 5.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   66 RPFLQRIRAQSFKLgqlphVLNYSklIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIV 144
Cdd:cd05613    55 RQVLEHIRQSPFLV-----TLHYA--FQTDTKLHLILDYINGgELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGII 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  145 HGDIKTENILVTSWNWCILTDFAafIKPVYLPEDNPGEFLFyfdtskrrtC----YLAPErfnskLYQDGKSNNgrlTKE 220
Cdd:cd05613   128 YRDIKLENILLDSSGHVVLTDFG--LSKEFLLDENERAYSF---------CgtieYMAPE-----IVRGGDSGH---DKA 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187153  221 MDIFSLGCVIAEIFAEGRPiFNLSqlfKYKSNSYDVNREFLMEEMN-STDLRNLVLDMIQL----DPSKRLSC 288
Cdd:cd05613   189 VDWWSLGVLMYELLTGASP-FTVD---GEKNSQAEISRRILKSEPPyPQEMSALAKDIIQRllmkDPKKRLGC 257
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
106-292 6.46e-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: 61.91  E-value: 6.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvYLPEDNPGEFLf 185
Cdd:cd14181   100 RGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFG------FSCHLEPGEKL- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 yfdtskRRTC----YLAPERFNSKLyqdGKSNNGrLTKEMDIFSLGCVIAEIFAEGRPIFNLSQL----------FKYKS 251
Cdd:cd14181   173 ------RELCgtpgYLAPEILKCSM---DETHPG-YGKEVDLWACGVILFTLLAGSPPFWHRRQMlmlrmimegrYQFSS 242
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 342187153  252 NSYDvNReflmeemnSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14181   243 PEWD-DR--------SSTVKDLISRLLVVDPEIRLTAEQAL 274
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
50-293 6.78e-10

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 61.38  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   50 EIVIKVFIKPK-DQYSLRPFLQRIRAqsFKLGQLPHVLNYSKLIETNRAGYMIRQHLK-NNLYDRLSLRPYLQDIELKFI 127
Cdd:cd14072    27 EVAIKIIDKTQlNPSSLQKLFREVRI--MKILNHPNIVKLFEVIETEKTLYLVMEYASgGEVFDYLVAHGRMKEKEARAK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  128 AFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvYLPEDNPGEFLfyfDTSKRRTCYLAPERFNSKLY 207
Cdd:cd14072   105 FRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFG------FSNEFTPGNKL---DTFCGSPPYAAPELFQGKKY 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  208 qDGksnngrltKEMDIFSLGcVIAEIFAEGRPIF---NLSQLF------KYKSnsydvnrEFLMeemnSTDLRNLVLDMI 278
Cdd:cd14072   176 -DG--------PEVDVWSLG-VILYTLVSGSLPFdgqNLKELRervlrgKYRI-------PFYM----STDCENLLKKFL 234
                         250
                  ....*....|....*
gi 342187153  279 QLDPSKRLSCDELLN 293
Cdd:cd14072   235 VLNPSKRGTLEQIMK 249
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
106-293 8.94e-10

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 61.20  E-value: 8.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRP--YLQDIELKFIAFQLLNALKDIHNLN--IVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLPEDn 179
Cdd:cd13985    85 PGSLVDILEKSPpsPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFgsATTEHYPLERAE- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  180 pgEFLFYFDTSKRRTC--YLAPERFNskLYQDgksnnGRLTKEMDIFSLGCVIAEI------FAEGRPIFNLSQLFKYKS 251
Cdd:cd13985   164 --EVNIIEEEIQKNTTpmYRAPEMID--LYSK-----KPIGEKADIWALGCLLYKLcffklpFDESSKLAIVAGKYSIPE 234
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 342187153  252 NSYdvnreflmeemNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd13985   235 QPR-----------YSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
125-293 9.39e-10

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


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 61.12  E-value: 9.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVYLpednpgeflfyfDTSKRRT-CYLAPER 201
Cdd:cd05578   103 KFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFniATKLTDGTL------------ATSTSGTkPYMAPEV 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  202 FNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLS--------QLFKYKSNSYDVNreflmeemNSTDLRNL 273
Cdd:cd05578   171 FMRAGY----------SFAVDWWSLGVTAYEMLRGKRPYEIHSrtsieeirAKFETASVLYPAG--------WSEEAIDL 232
                         170       180
                  ....*....|....*....|.
gi 342187153  274 VLDMIQLDPSKRLSC-DELLN 293
Cdd:cd05578   233 INKLLERDPQKRLGDlSDLKN 253
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
75-292 1.10e-09

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 60.95  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   75 QSFKLGQLPHVLNY--SKLIETNRagYMIRQHlknnlYDRLSLRPYL--QDIELKFIAF---QLLNALKDIHNLNIVHGD 147
Cdd:cd06917    54 SQLKLGQPKNIIKYygSYLKGPSL--WIIMDY-----CEGGSIRTLMraGPIAERYIAVimrEVLVALKFIHKDGIIHRD 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  148 IKTENILVTSWNWCILTDF--AAfikpvylpednpgefLFYFDTSKRRTC-----YLAPErfnskLYQDGKSNNGRltke 220
Cdd:cd06917   127 IKAANILVTNTGNVKLCDFgvAA---------------SLNQNSSKRSTFvgtpyWMAPE-----VITEGKYYDTK---- 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187153  221 MDIFSLGCVIAEIfAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06917   183 ADIWSLGITTYEM-ATGNPPYSDVDALRAVMLIPKSKPPRLEGNGYSPLLKEFVAACLDEEPKDRLSADELL 253
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
130-292 1.18e-09

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: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYlpEDNPGEFLFyfdtsKRRTC----YLAPERFNSK 205
Cdd:cd14165   110 QLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDF-GFSKRCL--RDENGRIVL-----SKTFCgsaaYAAPEVLQGI 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  206 LYQdgksnngrlTKEMDIFSLGcVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKR 285
Cdd:cd14165   182 PYD---------PRIYDIWSLG-VILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSECKDLIYRLLQPDVSQR 251

                  ....*..
gi 342187153  286 LSCDELL 292
Cdd:cd14165   252 LCIDEVL 258
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1080-1312 1.18e-09

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: 61.20  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1080 PNSITSSAVSPgETPYLITGSDQGVIKIWNLKeiivGEVYSSSLTyDCSSTVTQITMIPNFDAFAVSSKDGQIIVLKVNh 1159
Cdd:cd00200     9 TGGVTCVAFSP-DGKLLATGSGDGTIKVWDLE----TGELLRTLK-GHTGPVRDVAASADGTYLASGSSDKTIRLWDLE- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1160 yqqesevkflNCECIRKinLKNFGKNEYAVrmrAFVNeEKSLLVALTNLSRVIIFDIRTLERLQIIENsprH-GAVSSIC 1238
Cdd:cd00200    82 ----------TGECVRT--LTGHTSYVSSV---AFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRG---HtDWVNSVA 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153 1239 IDEECCVLILGTTRGIIDIWDIRFNVLIRswSFGDH-APITHVevcQFYGKNSVIVVGGSSKTfLTIWNFVKGHC 1312
Cdd:cd00200   143 FSPDGTFVASSSQDGTIKLWDLRTGKCVA--TLTGHtGEVNSV---AFSPDGEKLLSSSSDGT-IKLWDLSTGKC 211
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
125-286 1.86e-09

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 60.19  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAfQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNPGeflfYFDTSKrrtcYLAPERFNs 204
Cdd:cd05611   101 QYIA-EVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDF-GLSRNGLEKRHNKK----FVGTPD----YLAPETIL- 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 klyqdGKSNNgrltKEMDIFSLGCVIAEiFAEGRPIFNLS---QLFKyKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLD 281
Cdd:cd05611   170 -----GVGDD----KMSDWWSLGCVIFE-FLFGYPPFHAEtpdAVFD-NILSRRINWPEEVKEFCSPEAVDLINRLLCMD 238

                  ....*
gi 342187153  282 PSKRL 286
Cdd:cd05611   239 PAKRL 243
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
108-241 1.96e-09

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 60.64  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  108 NLYDRLSLRPY--LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNW-CI-LTDF--AAFIkpvylpednpG 181
Cdd:cd14210   100 NLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKsSIkVIDFgsSCFE----------G 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  182 EFLFYFDTSKrrtCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF 241
Cdd:cd14210   170 EKVYTYIQSR---FYRAPEVILGLPY----------DTAIDMWSLGCILAELYT-GYPLF 215
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
42-292 2.08e-09

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: 60.13  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   42 CKALDPNGEIVIKVFikPKDQYSLRpflQRIRAQS----FKLGQLPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLR 116
Cdd:cd08220    19 CRRKDDNKLVIIKQI--PVEQMTKE---ERQAALNevkvLSMLHHPNIIEYYESFLEDKALMIVMEYAPGgTLFEYIQQR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  117 --PYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFaafikpvylpednpGEFLFYFDTSKRR 193
Cdd:cd08220    94 kgSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVkIGDF--------------GISKILSSKSKAY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  194 T-----CYLAPERFNSKLYQDgKSnngrltkemDIFSLGCVIAEIFAEGRPI--FNLSQL-FKYKSNSYDVnreflMEEM 265
Cdd:cd08220   160 TvvgtpCYISPELCEGKPYNQ-KS---------DIWALGCVLYELASLKRAFeaANLPALvLKIMRGTFAP-----ISDR 224
                         250       260
                  ....*....|....*....|....*..
gi 342187153  266 NSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd08220   225 YSEELRHLILSMLHLDPNKRPTLSEIM 251
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
127-293 2.81e-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: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCIL--TDF--AAFIkpvylpedNPGEFLFYFdtskrrtC----YLA 198
Cdd:cd14098   106 LTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVkiSDFglAKVI--------HTGTFLVTF-------CgtmaYLA 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSKlyqdGKSNNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMN-STDLRNLVLDM 277
Cdd:cd14098   171 PEILMSK----EQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVDFNiSEEAIDFILRL 246
                         170
                  ....*....|....*.
gi 342187153  278 IQLDPSKRLSCDELLN 293
Cdd:cd14098   247 LDVDPEKRMTAAQALD 262
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
131-293 2.90e-09

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 59.61  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  131 LLNALKDIHNLNIVHGDIKTENILVTSwNWCI-LTDF----------AAFIKPVYLPEDNPGEflfYFDTSKRRT-CYLA 198
Cdd:cd14010   103 LVRGLHYIHSKGIIYCDLKPSNILLDG-NGTLkLSDFglarregeilKELFGQFSDEGNVNKV---SKKQAKRGTpYYMA 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF---NLSQLFKyKSNSYDVNREFLMEEMN-STDLRNLV 274
Cdd:cd14010   179 PELFQGGVH----------SFASDLWALGCVLYEMFT-GKPPFvaeSFTELVE-KILNEDPPPPPPKVSSKpSPDFKSLL 246
                         170
                  ....*....|....*....
gi 342187153  275 LDMIQLDPSKRLSCDELLN 293
Cdd:cd14010   247 KGLLEKDPAKRLSWDELVK 265
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
17-292 3.40e-09

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 59.62  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   17 IFSYIDVL-----EEVHYVSQLNSSRF--LKTCKAL----DPNGEIVIKVfikpkdqyslrpfLQRIRAQSfklgqlphV 85
Cdd:cd14166     4 TFIFMEVLgsgafSEVYLVKQRSTGKLyaLKCIKKSplsrDSSLENEIAV-------------LKRIKHEN--------I 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   86 LNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILvtswnwcilt 164
Cdd:cd14166    63 VTLEDIYESTTHYYLVMQLVSGgELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLL---------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  165 dfaafikpVYLPEDNPGEFLFYFDTSKRR-------TC----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIAEI 233
Cdd:cd14166   133 --------YLTPDENSKIMITDFGLSKMEqngimstACgtpgYVAPEVLAQKPY----------SKAVDCWSIG-VITYI 193
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187153  234 FAEGRPIF---NLSQLF-KYKSNSYDVNREFLMEEMNSTdlRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14166   194 LLCGYPPFyeeTESRLFeKIKEGYYEFESPFWDDISESA--KDFIRHLLEKNPSKRYTCEKAL 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
83-293 4.50e-09

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 58.82  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNN-LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC 161
Cdd:cd14079    62 PHIIRLYEVIETPTDIFMVMEYVSGGeLFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNV 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 ILTDF--AAFIKpvylpednPGEFLfyfdtskRRTC----YLAPERFNSKLYqdgksnngrLTKEMDIFSLGcVIAEIFA 235
Cdd:cd14079   142 KIADFglSNIMR--------DGEFL-------KTSCgspnYAAPEVISGKLY---------AGPEVDVWSCG-VILYALL 196
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187153  236 EGRPIF---NLSQLF-KYKSNSYDVNrEFLmeemnSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14079   197 CGSLPFddeHIPNLFkKIKSGIYTIP-SHL-----SPGARDLIKRMLVVDPLKRITIPEIRQ 252
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
49-309 4.90e-09

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: 58.79  E-value: 4.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   49 GEIVIK-VFIKP--KDQYSLRPFLQRIRAQsfklgqlPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIEL 124
Cdd:cd14187    37 GKIVPKsLLLKPhqKEKMSMEIAIHRSLAH-------QHVVGFHGFFEDNDFVYVVLELCRRrSLLELHKRRKALTEPEA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYlpednPGEflfyfdtSKRRTC----YLAPE 200
Cdd:cd14187   110 RYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEY-----DGE-------RKKTLCgtpnYIAPE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  201 RFNSKlyqdGKSNngrltkEMDIFSLGCVIAEIFAeGRPIFNLSQL----FKYKSNSYDVNREflmeeMNSTdLRNLVLD 276
Cdd:cd14187   178 VLSKK----GHSF------EVDIWSIGCIMYTLLV-GKPPFETSCLketyLRIKKNEYSIPKH-----INPV-AASLIQK 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 342187153  277 MIQLDPSKRLSCDELLNkyrgiffpDYFYTFIY 309
Cdd:cd14187   241 MLQTDPTARPTINELLN--------DEFFTSGY 265
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
84-292 4.94e-09

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 58.79  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   84 HVLNYSKLIETNRAGYMIRQHL-KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI 162
Cdd:cd14189    62 HVVKFSHHFEDAENIYIFLELCsRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  163 LTDF--AAFIKPVylpednpgeflfyfDTSKRRTC----YLAPErfnsKLYQDGKSnngrltKEMDIFSLGCVIAEIFAe 236
Cdd:cd14189   142 VGDFglAARLEPP--------------EQRKKTICgtpnYLAPE----VLLRQGHG------PESDVWSLGCVMYTLLC- 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153  237 GRPIFNLSQLfkykSNSYDVNRE--FLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14189   197 GNPPFETLDL----KETYRCIKQvkYTLPASLSLPARHLLAGILKRNPGDRLTLDQIL 250
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
68-241 5.05e-09

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: 59.26  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   68 FLQRIRAQsfklgqlPHVLnysKLIETNRAG---YMIRQHLKNNLYDRL--SLRPyLQDIELKFIAFQLLNALKDIHNLN 142
Cdd:cd07832    52 ALQACQGH-------PYVV---KLRDVFPHGtgfVLVFEYMLSSLSEVLrdEERP-LTEAQVKRYMRMLLKGVAYMHANR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  143 IVHGDIKTENILVTSWNWCILTDFAafIKPVYlpeDNPGEFLFYFDTSKRRtcYLAPE-RFNSKLYQDGksnngrltkeM 221
Cdd:cd07832   121 IMHRDLKPANLLISSTGVLKIADFG--LARLF---SEEDPRLYSHQVATRW--YRAPElLYGSRKYDEG----------V 183
                         170       180
                  ....*....|....*....|
gi 342187153  222 DIFSLGCVIAEIFAeGRPIF 241
Cdd:cd07832   184 DLWAVGCIFAELLN-GSPLF 202
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
109-292 7.00e-09

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 58.75  E-value: 7.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwnwcILTDFAAFIKPVYLPEDNPGEFLfyfD 188
Cdd:cd14169    88 LFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAT----PFEDSKIMISDFGLSKIEAQGML---S 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  189 TSKRRTCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIAEIFAEGRPIF---NLSQLFK-YKSNSYDVNREFLMEE 264
Cdd:cd14169   161 TACGTPGYVAPELLEQKPY----------GKAVDVWAIG-VISYILLCGYPPFydeNDSELFNqILKAEYEFDSPYWDDI 229
                         170       180
                  ....*....|....*....|....*...
gi 342187153  265 MNSTdlRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14169   230 SESA--KDFIRHLLERDPEKRFTCEQAL 255
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
43-293 8.16e-09

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


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 58.01  E-value: 8.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   43 KALDPN-GEIV----IKVFIKPKDqyslrpFLQRIRAQSFKLGQL--PHVLNYSKLIETNRAGYMIRQHLKNNlydrlsl 115
Cdd:cd06627    18 KGLNLNtGEFVaikqISLEKIPKS------DLKSVMGEIDLLKKLnhPNIVKYIGSVKTKDSLYIILEYVENG------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  116 rpYLQDIELKF-------IA---FQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvyLPEDNPGEFlf 185
Cdd:cd06627    85 --SLASIIKKFgkfpeslVAvyiYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATK---LNEVEKDEN-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 yfdtSKRRTCY-LAPERFNSKlyqdgksnngRLTKEMDIFSLGCVIAEIFAEGRPIFNL---SQLFKYKSnsydvNREFL 261
Cdd:cd06627   158 ----SVVGTPYwMAPEVIEMS----------GVTTASDIWSVGCTVIELLTGNPPYYDLqpmAALFRIVQ-----DDHPP 218
                         250       260       270
                  ....*....|....*....|....*....|..
gi 342187153  262 MEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd06627   219 LPENISPELRDFLLQCFQKDPTLRPSAKELLK 250
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
109-288 1.00e-08

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 58.17  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYLPEDNPGEFLFyfd 188
Cdd:cd05583    86 LFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFG--LSKEFLPGENDRAYSF--- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  189 tskrrtC----YLAPERFNSKlyQDGKSnngrltKEMDIFSLGCVIAEIFAEGRPiFNLSqlfKYKSNSYDVNREFL--- 261
Cdd:cd05583   161 ------CgtieYMAPEVVRGG--SDGHD------KAVDWWSLGVLTYELLTGASP-FTVD---GERNSQSEISKRILksh 222
                         170       180
                  ....*....|....*....|....*....
gi 342187153  262 --MEEMNSTDLRNLVLDMIQLDPSKRLSC 288
Cdd:cd05583   223 ppIPKTFSAEAKDFILKLLEKDPKKRLGA 251
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
125-293 1.12e-08

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


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 57.78  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKP--VYlpeDNPGeflfyfDTSKRRTCY-LAPER 201
Cdd:cd06629   111 RFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSddIY---GNNG------ATSMQGSVFwMAPEV 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  202 FNSklyqDGKSNNGRLtkemDIFSLGCVIAEIFAEGRPIFNLSQ---LFKYKSNSydvNREFLMEEMN-STDLRNLVLDM 277
Cdd:cd06629   182 IHS----QGQGYSAKV----DIWSLGCVVLEMLAGRRPWSDDEAiaaMFKLGNKR---SAPPVPEDVNlSPEALDFLNAC 250
                         170
                  ....*....|....*.
gi 342187153  278 IQLDPSKRLSCDELLN 293
Cdd:cd06629   251 FAIDPRDRPTAAELLS 266
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
126-293 1.45e-08

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 57.22  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  126 FIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPvylpednpgeflfyfDTSKRRTC-----YLA 198
Cdd:cd06614   101 YVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFgfAAQLTK---------------EKSKRNSVvgtpyWMA 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSKLYQDgksnngrltkEMDIFSLGCVIAEIfAEGR-PIFN---LSQLFKYKSNSYDVNREflmEEMNSTDLRNLV 274
Cdd:cd06614   166 PEVIKRKDYGP----------KVDIWSLGIMCIEM-AEGEpPYLEeppLRALFLITTKGIPPLKN---PEKWSPEFKDFL 231
                         170
                  ....*....|....*....
gi 342187153  275 LDMIQLDPSKRLSCDELLN 293
Cdd:cd06614   232 NKCLVKDPEKRPSAEELLQ 250
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
79-292 1.99e-08

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 57.41  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   79 LGQLPHVLNY-SKLIEtnrAGYMIRQHLKNN---LYDRLS----LRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKT 150
Cdd:cd14051    56 LGKHPHVVRYySAWAE---DDHMIIQNEYCNggsLADAISenekAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKP 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  151 ENILVTSWNwciltdfaafiKPVYLPEDNPGEFLFYFDTSKRR-----------TCYLAPE------RFNSK-LYQDGKS 212
Cdd:cd14051   133 GNIFISRTP-----------NPVSSEEEEEDFEGEEDNPESNEvtykigdlghvTSISNPQveegdcRFLANeILQENYS 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  213 NngrLTKEmDIFSLGCVIAEIfAEGRPifnlsqLFKYKSNSYDVNREFLMEEMN-STDLRNLVLDMIQLDPSKRLSCDEL 291
Cdd:cd14051   202 H---LPKA-DIFALALTVYEA-AGGGP------LPKNGDEWHEIRQGNLPPLPQcSPEFNELLRSMIHPDPEKRPSAAAL 270

                  .
gi 342187153  292 L 292
Cdd:cd14051   271 L 271
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
84-292 2.58e-08

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 56.56  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   84 HVLNYSKLIETNRAGYMIRQHL-KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI 162
Cdd:cd14188    62 HVVQFYHYFEDKENIYILLEYCsRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELK 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  163 LTDF--AAFIKPVylpednpgeflfyfdTSKRRT-C----YLAPERFNsklyqdgKSNNGrltKEMDIFSLGCVIAEIFA 235
Cdd:cd14188   142 VGDFglAARLEPL---------------EHRRRTiCgtpnYLSPEVLN-------KQGHG---CESDIWALGCVMYTMLL 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 342187153  236 eGRPIFNLSQLfkykSNSYDVNRE--FLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14188   197 -GRPPFETTNL----KETYRCIREarYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEII 250
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
119-292 2.60e-08

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 57.69  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwnWC---ILtDFAafikpvyLPEDNPGEFLFYFDTSkrrtC 195
Cdd:cd07851   115 LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNE--DCelkIL-DFG-------LARHTDDEMTGYVATR----W 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 YLAPE-RFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF----NLSQLFKYKSNSYDVNREFlMEEMNSTDL 270
Cdd:cd07851   181 YRAPEiMLNWMHY----------NQTVDIWSVGCIMAELLT-GKTLFpgsdHIDQLKRIMNLVGTPDEEL-LKKISSESA 248
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 342187153  271 RNLV----------------------LD----MIQLDPSKRLSCDELL 292
Cdd:cd07851   249 RNYIqslpqmpkkdfkevfsganplaIDllekMLVLDPDKRITAAEAL 296
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
50-166 3.20e-08

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 56.56  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   50 EIVIKVFikPKDQYSLRPFLQRIRAqSFKLGQLPHVLN-YSKLIETNRAgYMIRQHL--KNNLYDRLSLRPYLQDIELKF 126
Cdd:cd13987    20 KMALKFV--PKPSTKLKDFLREYNI-SLELSVHPHIIKtYDVAFETEDY-YVFAQEYapYGDLFSIIPPQVGLPEERVKR 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILV--TSWNWCILTDF 166
Cdd:cd13987    96 CAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDF 137
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
52-298 3.74e-08

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 56.08  E-value: 3.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   52 VIKVFIKPKDQ-YSLRPFlqrIRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQH----------------LKNNLYDRLS 114
Cdd:cd05572     9 VELVQLKSKGRtFALKCV---KKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYrtfkdkkylymlmeycLGGELWTILR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  115 LRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYlpednpgeflfyfdtSKRRT 194
Cdd:cd05572    86 DRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDF-GFAKKLG---------------SGRKT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 ---C----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEiFAEGRPIFNLSQLFKYKsnsydVNREFLMEEMN- 266
Cdd:cd05572   150 wtfCgtpeYVAPEIILNKGY----------DFSVDYWSLGILLYE-LLTGRPPFGGDDEDPMK-----IYNIILKGIDKi 213
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 342187153  267 ------STDLRNLVLDMIQLDPSKRLSCdeLLNKYRGI 298
Cdd:cd05572   214 efpkyiDKNAKNLIKQLLRRNPEERLGY--LKGGIRDI 249
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
83-292 3.97e-08

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 56.26  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC 161
Cdd:cd14663    60 PNIVELHEVMATKTKIFFVMELVTGgELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 ILTDFAAFIkpvyLPEDNPGEFLFYfdtskrRTC----YLAPERFNSKLYQDGKSnngrltkemDIFSLGCVIAEIFAEG 237
Cdd:cd14663   140 KISDFGLSA----LSEQFRQDGLLH------TTCgtpnYVAPEVLARRGYDGAKA---------DIWSCGVILFVLLAGY 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153  238 RPiF---NLSQLFKYKSNSydvnrEFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14663   201 LP-FddeNLMALYRKIMKG-----EFEYPRWFSPGAKSLIKRILDPNPSTRITVEQIM 252
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
117-288 4.79e-08

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 56.00  E-value: 4.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  117 PYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikPVYLPEDNPgeflfyFDTSKRRTCY 196
Cdd:cd05577    90 RGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGL---AVEFKGGKK------IKGRVGTHGY 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  197 LAPErfnskLYQDGKSnngrLTKEMDIFSLGCVIAEIFAeGRPIFnlsQLFKYKSNSYDVNREFLMEEM-----NSTDLR 271
Cdd:cd05577   161 MAPE-----VLQKEVA----YDFSVDWFALGCMLYEMIA-GRSPF---RQRKEKVDKEELKRRTLEMAVeypdsFSPEAR 227
                         170
                  ....*....|....*..
gi 342187153  272 NLVLDMIQLDPSKRLSC 288
Cdd:cd05577   228 SLCEGLLQKDPERRLGC 244
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
83-294 4.83e-08

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 55.97  E-value: 4.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLR---PYLQDIELKFIAfQLLNALKDIHNLNIVHGDIKTENILVTSW 158
Cdd:cd08218    59 PNIVQYQESFEENGNLYIVMDYCDGgDLYKRINAQrgvLFPEDQILDWFV-QLCLALKHVHDRKILHRDIKSQNIFLTKD 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  159 NWCILTDFAafIKPVYlpeDNPGEFlfyfdtskRRTC-----YLAPERFNSKLYqdgksNNgrltkEMDIFSLGCVIAEI 233
Cdd:cd08218   138 GIIKLGDFG--IARVL---NSTVEL--------ARTCigtpyYLSPEICENKPY-----NN-----KSDIWALGCVLYEM 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153  234 ------FAEGrpifNLSQL-FKYKSNSYDVnreflMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLNK 294
Cdd:cd08218   195 ctlkhaFEAG----NMKNLvLKIIRGSYPP-----VPSRYSYDLRSLVSQLFKRNPRDRPSINSILEK 253
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
125-241 5.10e-08

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 56.71  E-value: 5.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF----AAFikpvylpEDNPGEfLFYFDTSKRRtCYLAPE 200
Cdd:cd07859   106 QFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFglarVAF-------NDTPTA-IFWTDYVATR-WYRAPE 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 342187153  201 RFNSKLyqdgksnnGRLTKEMDIFSLGCVIAEIFAeGRPIF 241
Cdd:cd07859   177 LCGSFF--------SKYTPAIDIWSIGCIFAEVLT-GKPLF 208
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
130-294 5.18e-08

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 55.74  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikpvylpednpGEFlFYFDT----SKRRT-CYLAPERFNS 204
Cdd:cd08224   112 QLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL------------GRF-FSSKTtaahSLVGTpYYMSPERIRE 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 KLYqDGKSnngrltkemDIFSLGCVIAEIFAEGRPIF----NLSQLFKYKSNSydvnrEF--LMEEMNSTDLRNLVLDMI 278
Cdd:cd08224   179 QGY-DFKS---------DIWSLGCLLYEMAALQSPFYgekmNLYSLCKKIEKC-----EYppLPADLYSQELRDLVAACI 243
                         170
                  ....*....|....*.
gi 342187153  279 QLDPSKRLSCDELLNK 294
Cdd:cd08224   244 QPDPEKRPDISYVLDV 259
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
99-285 5.32e-08

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 56.14  E-value: 5.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 YMIRQHLKNNLYDRLSLRpyLQDIELKFIAFQLLNALKDIHNLN--IVHGDIKTENILVTSWNWCILTDFAAfIKPVYLP 176
Cdd:cd14037    87 YCKGGGVIDLMNQRLQTG--LTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGS-ATTKILP 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  177 EDNPGEFLFYFDTSKRRT--CYLAPERFNskLYQdGKSnngrLTKEMDIFSLGCVIAEI------FAEGRPIFNLSQLFK 248
Cdd:cd14037   164 PQTKQGVTYVEEDIKKYTtlQYRAPEMID--LYR-GKP----ITEKSDIWALGCLLYKLcfyttpFEESGQLAILNGNFT 236
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 342187153  249 YKSNSydvnreflmeeMNSTDLRNLVLDMIQLDPSKR 285
Cdd:cd14037   237 FPDNS-----------RYSKRLHKLIRYMLEEDPEKR 262
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
130-293 5.34e-08

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 56.40  E-value: 5.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDNpgeflfyFDTSKRRTC--YLAPERFNSKLY 207
Cdd:cd14094   117 QILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESG-------LVAGGRVGTphFMAPEVVKREPY 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  208 qdgksnngrlTKEMDIFSLGcVIAEIFAEGRPIFNLSQLFKYKS---NSYDVNREflMEEMNSTDLRNLVLDMIQLDPSK 284
Cdd:cd14094   190 ----------GKPVDVWGCG-VILFILLSGCLPFYGTKERLFEGiikGKYKMNPR--QWSHISESAKDLVRRMLMLDPAE 256

                  ....*....
gi 342187153  285 RLSCDELLN 293
Cdd:cd14094   257 RITVYEALN 265
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
126-290 5.48e-08

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 56.21  E-value: 5.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  126 FIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikPVYLPEDnpgeflfyfDTSKRRT---CYLAPERF 202
Cdd:cd05605   106 FYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGL---AVEIPEG---------ETIRGRVgtvGYMAPEVV 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  203 NSKLYqdgksnngrlTKEMDIFSLGCVIAEIFaEGRPIFnlsQLFKYKSNSYDVNREFLMEEMN-----STDLRNLVLDM 277
Cdd:cd05605   174 KNERY----------TFSPDWWGLGCLIYEMI-EGQAPF---RARKEKVKREEVDRRVKEDQEEysekfSEEAKSICSQL 239
                         170
                  ....*....|...
gi 342187153  278 IQLDPSKRLSCDE 290
Cdd:cd05605   240 LQKDPKTRLGCRG 252
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
99-293 5.98e-08

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 56.15  E-value: 5.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 YMIRQHLK-NNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwnwcilTDFAAFIKPV---- 173
Cdd:cd14092    75 YLVMELLRgGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTD------EDDDAEIKIVdfgf 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  174 --YLPEDNPgeflfyfdtsKRRTC----YLAPERFNSKLYQDGKSNNgrltkeMDIFSLGcVIAEIFAEGRPIFnlsqlf 247
Cdd:cd14092   149 arLKPENQP----------LKTPCftlpYAAPEVLKQALSTQGYDES------CDLWSLG-VILYTMLSGQVPF------ 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  248 kyKSNSYDVNREFLMEEMN--------------STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14092   206 --QSPSRNESAAEIMKRIKsgdfsfdgeewknvSSEAKSLIQGLLTVDPSKRLTMSELRN 263
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
129-292 8.18e-08

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 55.52  E-value: 8.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  129 FQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFA---AFIKPVYLpednpgeflfyFDTSKRRTCYLAPE-RFNS 204
Cdd:cd07839   106 FQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGlarAFGIPVRC-----------YSAEVVTLWYRPPDvLFGA 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 KLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIF-------------------------NLSQLFKYKS-NSYDVNR 258
Cdd:cd07839   175 KLY----------STSIDMWSAGCIFAELANAGRPLFpgndvddqlkrifrllgtpteeswpGVSKLPDYKPyPMYPATT 244
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 342187153  259 EFLME--EMNSTDlRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd07839   245 SLVNVvpKLNSTG-RDLLQNLLVCNPVQRISAEEAL 279
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
108-292 8.34e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 55.13  E-value: 8.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  108 NLYDRLSL--RPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYLPEDNPGEflf 185
Cdd:cd08221    85 NLHDKIAQqkNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFG--ISKVLDSESSMAE--- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 yfdtskrrTC-----YLAPERFNSKLYqDGKSnngrltkemDIFSLGCVIAEIFAEGRpIFNLSQLFKYKSNSYDVNREF 260
Cdd:cd08221   160 --------SIvgtpyYMSPELVQGVKY-NFKS---------DIWAVGCVLYELLTLKR-TFDATNPLRLAVKIVQGEYED 220
                         170       180       190
                  ....*....|....*....|....*....|..
gi 342187153  261 LMEEMnSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd08221   221 IDEQY-SEEIIQLVHDCLHQDPEDRPTAEELL 251
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
53-293 8.79e-08

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


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 55.04  E-value: 8.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   53 IKVFIKPK-DQYSLRPFLQRIRAQSfKLGQlPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQ 130
Cdd:cd14075    32 IKILDKTKlDQKTQRLLSREISSME-KLHH-PNIIRLYEVVETLSKLHLVMEYASGgELYTKISTEGKLSESEAKPLFAQ 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  131 LLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvYLPEDNPGEFLFYFDTSKRrtcYLAPERFNSKLYQdg 210
Cdd:cd14075   110 IVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFG------FSTHAKRGETLNTFCGSPP---YAAPELFKDEHYI-- 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  211 ksnnGRLtkeMDIFSLGcVIAEIFAEGRPIFNLSQLFKYKSNSYDvnREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDE 290
Cdd:cd14075   179 ----GIY---VDIWALG-VLLYFMVTGVMPFRAETVAKLKKCILE--GTYTIPSYVSEPCQELIRGILQPVPSDRYSIDE 248

                  ...
gi 342187153  291 LLN 293
Cdd:cd14075   249 IKN 251
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
68-292 9.35e-08

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 55.83  E-value: 9.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   68 FLQRIraqsfklgQLPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSL-RPYLQDIELKFIAFQLLNALKDIHNLNIVHG 146
Cdd:cd06635    78 FLQRI--------KHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVhKKPLQEIEIAAITHGALQGLAYLHSHNMIHR 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  147 DIKTENILVTSWNWCILTDF--AAFIKPVYLPEDNPgeflfyfdtskrrtCYLAPERFnskLYQDgksnNGRLTKEMDIF 224
Cdd:cd06635   150 DIKAGNILLTEPGQVKLADFgsASIASPANSFVGTP--------------YWMAPEVI---LAMD----EGQYDGKVDVW 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342187153  225 SLGCVIAEIFAEGRPIFNLSQLfkykSNSYDV--NREFLMEEMNSTD-LRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06635   209 SLGITCIELAERKPPLFNMNAM----SALYHIaqNESPTLQSNEWSDyFRNFVDSCLQKIPQDRPTSEELL 275
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
83-293 9.49e-08

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 55.18  E-value: 9.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNR-AGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC 161
Cdd:cd14076    66 PNIVRLLDVLKTKKyIGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 ILTDFaAFIKPVYLpedNPGEFlfyFDTSKRRTCYLAPERFNSKLYQDGksnngrltKEMDIFSLGCVIAEIFAEGRPI- 240
Cdd:cd14076   146 VITDF-GFANTFDH---FNGDL---MSTSCGSPCYAAPELVVSDSMYAG--------RKADIWSCGVILYAMLAGYLPFd 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342187153  241 --------FNLSQLFKYKsnsydVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14076   211 ddphnpngDNVPRLYRYI-----CNTPLIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMR 266
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
112-289 9.56e-08

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 55.58  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  112 RLSLRPYLQDIELKF-----IAFQLLNALKDIHNLNIVHGDIKTENILV----TSWNWCILTDFAAfikpvYLPEDNPGE 182
Cdd:cd14018   123 PCTLRQYLWVNTPSYrlarvMILQLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGC-----CLADDSIGL 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  183 FLFYFDTSKRR---TCYLAPERFNSKLYQDGKSNNGRltkeMDIFSLGCVIAEIFAEGRPIFNLSQLfKYKSNSYDVNRE 259
Cdd:cd14018   198 QLPFSSWYVDRggnACLMAPEVSTAVPGPGVVINYSK----ADAWAVGAIAYEIFGLSNPFYGLGDT-MLESRSYQESQL 272
                         170       180       190
                  ....*....|....*....|....*....|
gi 342187153  260 FLMEEMNSTDLRNLVLDMIQLDPSKRLSCD 289
Cdd:cd14018   273 PALPSAVPPDVRQVVKDLLQRDPNKRVSAR 302
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
53-293 1.19e-07

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: 54.61  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   53 IKVFIKPK--DQYsLRPFLQRiRAQSFKLGQLPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAF 129
Cdd:cd14162    30 IKIVSKKKapEDY-LQKFLPR-EIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENgDLLDYIRKNGALPEPQARRWFR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNPGEFLFYFDTSkrrTCYLAPERFNSKLYQD 209
Cdd:cd14162   108 QLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDF-GFARGVMKTKDGKPKLSETYCGS---YAYASPEILRGIPYDP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  210 GKSnngrltkemDIFSLGcVIAEIFAEGRPIF---NLSQLFKyksnsyDVNRE--FLMEEMNSTDLRNLVLDMIQLDPsK 284
Cdd:cd14162   184 FLS---------DIWSMG-VVLYTMVYGRLPFddsNLKVLLK------QVQRRvvFPKNPTVSEECKDLILRMLSPVK-K 246

                  ....*....
gi 342187153  285 RLSCDELLN 293
Cdd:cd14162   247 RITIEEIKR 255
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
42-294 1.26e-07

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 54.46  E-value: 1.26e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153     42 CKALDPNGEIVIKVFIK----PKDQYSLRPFLQRIRAqsfkLGQL--PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRL- 113
Cdd:smart00219   18 GKLKGKGGKKKVEVAVKtlkeDASEQQIEEFLREARI----MRKLdhPNVVKLLGVCTEEEPLYIVMEYMEGgDLLSYLr 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    114 SLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvyLPEDNPGEFLFYFDTSKRR 193
Cdd:smart00219   94 KNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG-------LSRDLYDDDYYRKRGGKLP 166
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    194 TCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGR---PIFNLSQLFKYKSNSYdvnREFLMEEMnSTDL 270
Cdd:smart00219  167 IRWMAPESLKEGKF----------TSKSDVWSFGVLLWEIFTLGEqpyPGMSNEEVLEYLKNGY---RLPQPPNC-PPEL 232
                           250       260
                    ....*....|....*....|....
gi 342187153    271 RNLVLDMIQLDPSKRLSCDELLNK 294
Cdd:smart00219  233 YDLMLQCWAEDPEDRPTFSELVEI 256
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
119-293 1.26e-07

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 54.63  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNwCILTDFAAFIK---PVYLPEDNPGEFLfyfdtskrrtc 195
Cdd:cd13995    93 MREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTK-AVLVDFGLSVQmteDVYVPKDLRGTEI----------- 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 YLAPERFNSKlyqdgksnnGRLTKeMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFL----MEEMNSTDLR 271
Cdd:cd13995   161 YMSPEVILCR---------GHNTK-ADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPpledIAQDCSPAMR 230
                         170       180
                  ....*....|....*....|..
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd13995   231 ELLEAALERNPNHRSSAAELLK 252
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
130-292 1.78e-07

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 53.90  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCI---LTDFAAfikpVYLPED-NPGEFLFYFdtskRRTCYLAPErfnsk 205
Cdd:cd14012   112 QLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGivkLTDYSL----GKTLLDmCSRGSLDEF----KQTYWLPPE----- 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  206 lyqDGKSNNgRLTKEMDIFSLG-CVIAEIFaeGRPIFnlsqlfkyksNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSK 284
Cdd:cd14012   179 ---LAQGSK-SPTRKTDVWDLGlLFLQMLF--GLDVL----------EKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKK 242

                  ....*...
gi 342187153  285 RLSCDELL 292
Cdd:cd14012   243 RPTALELL 250
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
42-294 1.87e-07

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 54.09  E-value: 1.87e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153     42 CKALDPNGEIVIKVFIK----PKDQYSLRPFLQRIRAqsfkLGQL--PHVLNYSKLIETNRAGYMI---------RQHLK 106
Cdd:smart00221   18 GTLKGKGDGKEVEVAVKtlkeDASEQQIEEFLREARI----MRKLdhPNIVKLLGVCTEEEPLMIVmeympggdlLDYLR 93
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    107 NNLYDRLSLRpylqdiELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvyLPEDNPGEFLFY 186
Cdd:smart00221   94 KNRPKELSLS------DLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFG-------LSRDLYDDDYYK 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    187 FDTSKRRTCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGR---PIFNLSQLFKYKSNSYdvnREFLME 263
Cdd:smart00221  161 VKGGKLPIRWMAPESLKEGKF----------TSKSDVWSFGVLLWEIFTLGEepyPGMSNAEVLEYLKKGY---RLPKPP 227
                           250       260       270
                    ....*....|....*....|....*....|.
gi 342187153    264 EMnSTDLRNLVLDMIQLDPSKRLSCDELLNK 294
Cdd:smart00221  228 NC-PPELYKLMLQCWAEDPEDRPTFSELVEI 257
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
108-293 2.07e-07

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 53.78  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  108 NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDF--AAFIKpvylpednpgefl 184
Cdd:cd14005    93 DLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTGEVkLIDFgcGALLK------------- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  185 fyfDTSKRRTC----YLAPERFNSKLYqdgksnngrLTKEMDIFSLGCVIAEIfaegrpifnLSQLFKYKSNSYDVNREF 260
Cdd:cd14005   160 ---DSVYTDFDgtrvYSPPEWIRHGRY---------HGRPATVWSLGILLYDM---------LCGDIPFENDEQILRGNV 218
                         170       180       190
                  ....*....|....*....|....*....|...
gi 342187153  261 LMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14005   219 LFRPRLSKECCDLISRCLQFDPSKRPSLEQILS 251
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
125-300 2.22e-07

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 54.64  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNPGEFLfyfDTSKrrtcYLAPERFNS 204
Cdd:cd05602   111 RFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDF-GLCKENIEPNGTTSTFC---GTPE----YLAPEVLHK 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 KLYQdgksnngrltKEMDIFSLGCVIAEIFAeGRPIFnlsqlfkYKSNS---YD--VNREFLMEEMNSTDLRNLVLDMIQ 279
Cdd:cd05602   183 QPYD----------RTVDWWCLGAVLYEMLY-GLPPF-------YSRNTaemYDniLNKPLQLKPNITNSARHLLEGLLQ 244
                         170       180
                  ....*....|....*....|..
gi 342187153  280 LDPSKRLSC-DELLNKYRGIFF 300
Cdd:cd05602   245 KDRTKRLGAkDDFTEIKNHIFF 266
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
131-293 2.35e-07

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 53.87  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  131 LLNALKDIHNLNIVHGDIKTENILV---TSWNWCI-LTDF--AAFIK-PVYLPEDNPgeflfyfdtskrrtCYLAPERFN 203
Cdd:cd14095   107 LAQALKYLHSLSIVHRDIKPENLLVvehEDGSKSLkLADFglATEVKePLFTVCGTP--------------TYVAPEILA 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  204 SKLYqdgksnngrlTKEMDIFSLGcVIAEIFAEGRPIF-----NLSQLF-KYKSNSYdvnrEFLMEEMN--STDLRNLVL 275
Cdd:cd14095   173 ETGY----------GLKVDIWAAG-VITYILLCGFPPFrspdrDQEELFdLILAGEF----EFLSPYWDniSDSAKDLIS 237
                         170
                  ....*....|....*...
gi 342187153  276 DMIQLDPSKRLSCDELLN 293
Cdd:cd14095   238 RMLVVDPEKRYSAGQVLD 255
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
109-154 2.45e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 53.71  E-value: 2.45e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENIL 154
Cdd:PHA03390   96 LFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVL 141
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
68-293 2.56e-07

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 54.26  E-value: 2.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   68 FLQRIRAqsfklgqlPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSL-RPYLQDIELKFIAFQLLNALKDIHNLNIVHG 146
Cdd:cd06634    68 FLQKLRH--------PNTIEYRGCYLREHTAWLVMEYCLGSASDLLEVhKKPLQEVEIAAITHGALQGLAYLHSHNMIHR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  147 DIKTENILVTSWNWCILTDF--AAFIKPVYLPEDNPgeflfyfdtskrrtCYLAPERFnskLYQDgksnNGRLTKEMDIF 224
Cdd:cd06634   140 DVKAGNILLTEPGLVKLGDFgsASIMAPANSFVGTP--------------YWMAPEVI---LAMD----EGQYDGKVDVW 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187153  225 SLGCVIAEIFAEGRPIFN---LSQLFKYKSNSYDVnrefLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd06634   199 SLGITCIELAERKPPLFNmnaMSALYHIAQNESPA----LQSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLK 266
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
109-293 2.97e-07

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: 53.97  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDNPGEFLFYFD 188
Cdd:cd14086    87 LFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGT 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  189 TSkrrtcYLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIAEIFAEGRPIF---NLSQLF-KYKSNSYDvnreFLMEE 264
Cdd:cd14086   167 PG-----YLSPEVLRKDPY----------GKPVDIWACG-VILYILLVGYPPFwdeDQHRLYaQIKAGAYD----YPSPE 226
                         170       180       190
                  ....*....|....*....|....*....|.
gi 342187153  265 MNS--TDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14086   227 WDTvtPEAKDLINQMLTVNPAKRITAAEALK 257
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
79-293 3.14e-07

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 53.61  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   79 LGQL---PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENIL 154
Cdd:cd14077    66 LSSLlnhPHICRLRDFLRTPNHYYMLFEYVDGgQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENIL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  155 VTSWNWCILTDFAafIKPVYLPEDNPGEFL--FYFdtskrrtcyLAPERFNSKLYqdgksnngrLTKEMDIFSLGCVIAE 232
Cdd:cd14077   146 ISKSGNIKIIDFG--LSNLYDPRRLLRTFCgsLYF---------AAPELLQAQPY---------TGPEVDVWSFGVVLYV 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153  233 IFAeGRPIF---NLSQLF-KYKSNSYDVNREFlmeemnSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14077   206 LVC-GKVPFddeNMPALHaKIKKGKVEYPSYL------SSECKSLISRMLVVDPKKRATLEQVLN 263
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
124-295 3.22e-07

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: 53.82  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  124 LKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaafikpvylpednpGEFLFYFDTSKRRTC-----YLA 198
Cdd:cd07838   109 IKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADF--------------GLARIYSFEMALTSVvvtlwYRA 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PErfnsKLYQDGKSNngrltkEMDIFSLGCVIAEIFAEgRPIF-------NLSQLFK---------------YKSNSYDV 256
Cdd:cd07838   175 PE----VLLQSSYAT------PVDMWSVGCIFAELFNR-RPLFrgsseadQLGKIFDviglpseeewprnsaLPRSSFPS 243
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 342187153  257 NREFLMEEM---NSTDLRNLVLDMIQLDPSKRLS-CDELLNKY 295
Cdd:cd07838   244 YTPRPFKSFvpeIDEEGLDLLKKMLTFNPHKRISaFEALQHPY 286
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
99-292 3.96e-07

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 53.98  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 YMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwNwCILT--DFAAFIKpvylp 176
Cdd:cd07853    80 YVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNS-N-CVLKicDFGLARV----- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  177 EDnpgeflfyFDTSKRRTC------YLAPERF-NSKLYqdgksnngrlTKEMDIFSLGCVIAE------IFAEGRPIFNL 243
Cdd:cd07853   153 EE--------PDESKHMTQevvtqyYRAPEILmGSRHY----------TSAVDIWSVGCIFAEllgrriLFQAQSPIQQL 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187153  244 -----------------------SQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd07853   215 dlitdllgtpsleamrsacegarAHILRGPHKPPSLPVLYTLSSQATHEAVHLLCRMLVFDPDKRISAADAL 286
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
125-286 4.95e-07

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 52.97  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKpvYLPEdnpgeflfyfdtskrRTC-------YL 197
Cdd:cd05580   104 KFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDF-GFAK--RVKD---------------RTYtlcgtpeYL 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  198 APERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYK---SNSYDVNREFlmeemnSTDLRNLV 274
Cdd:cd05580   166 APEIILSKGH----------GKAVDWWALGILIYEMLAGYPPFFDENPMKIYEkilEGKIRFPSFF------DPDAKDLI 229
                         170
                  ....*....|..
gi 342187153  275 LDMIQLDPSKRL 286
Cdd:cd05580   230 KRLLVVDLTKRL 241
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
102-294 5.06e-07

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 52.93  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  102 RQHLKNN-LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvyLPEDNP 180
Cdd:cd00192    84 LDFLRKSrPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFG-------LSRDIY 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  181 GEFLFYFDTSKR---RtcYLAPERFNSKLYqDGKSnngrltkemDIFSLGCVIAEIFAEGR-PIFNLS--QLFKYksnsy 254
Cdd:cd00192   157 DDDYYRKKTGGKlpiR--WMAPESLKDGIF-TSKS---------DVWSFGVLLWEIFTLGAtPYPGLSneEVLEY----- 219
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 342187153  255 dVNREFLME--EMNSTDLRNLVLDMIQLDPSKRLSCDELLNK 294
Cdd:cd00192   220 -LRKGYRLPkpENCPDELYELMLSCWQLDPEDRPTFSELVER 260
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
127-268 5.21e-07

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 53.17  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHN-LNIVHGDIKTENILVTS-WNWCILTDFAafikpVYLPEDNPGEFLfyfdtSKRRTCYLAPERFNS 204
Cdd:cd14001   115 VALSIARALEYLHNeKKILHGDIKSGNVLIKGdFESVKLCDFG-----VSLPLTENLEVD-----SDPKAQYVGTEPWKA 184
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187153  205 KlyqDGKSNNGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQlfkykSNSYDVNREFLMEEMNST 268
Cdd:cd14001   185 K---EALEEGGVITDKADIFAYGLVLWEMMTLSVPHLNLLD-----IEDDDEDESFDEDEEDEE 240
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
84-293 6.23e-07

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 52.55  E-value: 6.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   84 HVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRP-YLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSW---- 158
Cdd:cd14097    61 HIIHLEEVFETPKRMYLVMELCEDGELKELLLRKgFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidn 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  159 --NWCI-LTDFAAFIKPVYLPEDnpgeflfYFDTSKRRTCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIAEIFA 235
Cdd:cd14097   141 ndKLNIkVTDFGLSVQKYGLGED-------MLQETCGTPIYMAPEVISAHGY----------SQQCDIWSIG-VIMYMLL 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187153  236 EGRPIFnlsqLFKYKSNSYDVNREFLMEEMN------STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14097   203 CGEPPF----VAKSEEKLFEEIRKGDLTFTQsvwqsvSDAAKNVLQQLLKVDPAHRMTASELLD 262
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
127-293 6.34e-07

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 52.68  E-value: 6.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNW-CI--LTDFaAFIK----------PVYLPednpgeflfYfdtskrr 193
Cdd:cd14089   105 IMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnAIlkLTDF-GFAKetttkkslqtPCYTP---------Y------- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  194 tcYLAPERFNSKLYQdgksnngrltKEMDIFSLGcVIAEIFAEGRPIF------NLSQLFKYK--SNSYdvnrEFLMEEM 265
Cdd:cd14089   168 --YVAPEVLGPEKYD----------KSCDMWSLG-VIMYILLCGYPPFysnhglAISPGMKKRirNGQY----EFPNPEW 230
                         170       180       190
                  ....*....|....*....|....*....|
gi 342187153  266 N--STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14089   231 SnvSEEAKDLIRGLLKTDPSERLTIEEVMN 260
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
127-293 7.42e-07

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 52.44  E-value: 7.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVylPEDNPgeflfyfdtsKRR----TCY-LAPER 201
Cdd:cd06648   108 VCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDF-GFCAQV--SKEVP----------RRKslvgTPYwMAPEV 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  202 FNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLD 281
Cdd:cd06648   175 ISRLPY----------GTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFLDRMLVRD 244
                         170
                  ....*....|..
gi 342187153  282 PSKRLSCDELLN 293
Cdd:cd06648   245 PAQRATAAELLN 256
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
79-244 7.53e-07

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 52.28  E-value: 7.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   79 LGQLPH--VLNYSKLIETNRAGYMIRQHLKNNLYDRlslrpYLQDIELKFIAFQLLNALKDI-------HNLNIVHGDIK 149
Cdd:cd05063    60 MGQFSHhnIIRLEGVVTKFKPAMIITEYMENGALDK-----YLRDHDGEFSSYQLVGMLRGIaagmkylSDMNYVHRDLA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  150 TENILVTSWNWCILTDFAAfikpVYLPEDNPgEFLFYFDTSKRRTCYLAPERFNSKlyqdgksnngRLTKEMDIFSLGCV 229
Cdd:cd05063   135 ARNILVNSNLECKVSDFGL----SRVLEDDP-EGTYTTSGGKIPIRWTAPEAIAYR----------KFTSASDVWSFGIV 199
                         170
                  ....*....|....*.
gi 342187153  230 IAEIFAEG-RPIFNLS 244
Cdd:cd05063   200 MWEVMSFGeRPYWDMS 215
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
126-288 9.02e-07

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 52.33  E-value: 9.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  126 FIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikPVYLPEDNpgeflfyfdTSKRR---TCYLAPERF 202
Cdd:cd05630   106 FYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGL---AVHVPEGQ---------TIKGRvgtVGYMAPEVV 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  203 nsklyqdgksNNGRLTKEMDIFSLGCVIAEIFAEGRPIfnlsQLFKYKSNSYDVNRefLMEEMN-------STDLRNLVL 275
Cdd:cd05630   174 ----------KNERYTFSPDWWALGCLLYEMIAGQSPF----QQRKKKIKREEVER--LVKEVPeeysekfSPQARSLCS 237
                         170
                  ....*....|...
gi 342187153  276 DMIQLDPSKRLSC 288
Cdd:cd05630   238 MLLCKDPAERLGC 250
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
99-247 9.16e-07

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: 52.31  E-value: 9.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 YMIRQHLKNNLYDRLSLRP--YLQDiELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPvyLP 176
Cdd:cd07848    76 YLVFEYVEKNMLELLEEMPngVPPE-KVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDF-GFARN--LS 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153  177 EDNPGEFLFYFDTSkrrtCYLAPERFNSKLYqdGKSnngrltkeMDIFSLGCVIAEIfAEGRPIF----NLSQLF 247
Cdd:cd07848   152 EGSNANYTEYVATR----WYRSPELLLGAPY--GKA--------VDMWSVGCILGEL-SDGQPLFpgesEIDQLF 211
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
128-292 1.02e-06

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 52.24  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  128 AFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFAAFIKpvylpEDNpgEFLFYFDTSKrrtcYLAPE-RFNSK 205
Cdd:cd14020   116 ARDVLEALAFLHHEGYVHADLKPRNILWSAEDECFkLIDFGLSFK-----EGN--QDVKYIQTDG----YRAPEaELQNC 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  206 LYQDGKSNNGRLTKEMDIFSLGCVIAEIFAeGRPIFNLSQLFKYKSNSYDVNREFLMEEM--NST----DLRNLVLDMIQ 279
Cdd:cd14020   185 LAQAGLQSETECTSAVDLWSLGIVLLEMFS-GMKLKHTVRSQEWKDNSSAIIDHIFASNAvvNPAipayHLRDLIKSMLH 263
                         170
                  ....*....|...
gi 342187153  280 LDPSKRLSCDELL 292
Cdd:cd14020   264 NDPGKRATAEAAL 276
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
117-290 1.22e-06

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 52.28  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  117 PYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvyLPEDnpgeflfyfDTSKRR--- 193
Cdd:cd05632    99 PGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK---IPEG---------ESIRGRvgt 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  194 TCYLAPERFnsklyqdgksNNGRLTKEMDIFSLGCVIAEIFaEGRPIFNLSqlfKYKSNSYDVNREFLMEEMN-----ST 268
Cdd:cd05632   167 VGYMAPEVL----------NNQRYTLSPDYWGLGCLIYEMI-EGQSPFRGR---KEKVKREEVDRRVLETEEVysakfSE 232
                         170       180
                  ....*....|....*....|..
gi 342187153  269 DLRNLVLDMIQLDPSKRLSCDE 290
Cdd:cd05632   233 EAKSICKMLLTKDPKQRLGCQE 254
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
31-285 1.63e-06

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 51.36  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   31 SQLNSSRFLKTCKALD-PNGEIV-IKVFIK---PKDQYSLRPFLQRIRAQsfKLGQLPHVLNYSKLIETNRAGYMIRQH- 104
Cdd:cd14070     8 RKLGEGSFAKVREGLHaVTGEKVaIKVIDKkkaKKDSYVTKNLRREGRIQ--QMIRHPNITQLLDILETENSYYLVMELc 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  105 LKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikpvylpeDNPGEFL 184
Cdd:cd14070    86 PGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGL---------SNCAGIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  185 FY---FDTSKRRTCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPI----FNLSQLFkyksnsydvn 257
Cdd:cd14070   157 GYsdpFSTQCGSPAYAAPELLARKKY----------GPKVDVWSIGVNMYAMLTGTLPFtvepFSLRALH---------- 216
                         250       260       270
                  ....*....|....*....|....*....|....
gi 342187153  258 REFLMEEMN------STDLRNLVLDMIQLDPSKR 285
Cdd:cd14070   217 QKMVDKEMNplptdlSPGAISFLRSLLEPDPLKR 250
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
50-292 2.49e-06

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


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 50.49  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   50 EIVIKVFIK---PKDQYSlrpflqRIRAQSFKLGQLPH--VLNYSKLIETNRAGYMIRQHLKNNLYDRL--SLRPYLQDI 122
Cdd:cd14082    30 DVAIKVIDKlrfPTKQES------QLRNEVAILQQLSHpgVVNLECMFETPERVFVVMEKLHGDMLEMIlsSEKGRLPER 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  123 ELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWN---WCILTDF--AAFIkpvylpednpGEFLFyfdtskRRT--- 194
Cdd:cd14082   104 ITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFgfARII----------GEKSF------RRSvvg 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 --CYLAPERFNSKLYQdgksnngrltKEMDIFSLGcVIAEIFAEGRPIFN---------LSQLFKYKSNSYdvnreflmE 263
Cdd:cd14082   168 tpAYLAPEVLRNKGYN----------RSLDMWSVG-VIIYVSLSGTFPFNededindqiQNAAFMYPPNPW--------K 228
                         250       260
                  ....*....|....*....|....*....
gi 342187153  264 EMnSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14082   229 EI-SPDAIDLINNLLQVKMRKRYSVDKSL 256
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
100-241 3.37e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 51.03  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  100 MIRQHLKNNLYDRLSLRPYLQDIELKF-IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLP-- 176
Cdd:PHA03209  134 MVLPHYSSDLYTYLTKRSRPLPIDQALiIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPaf 213
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187153  177 -------EDNPGEFlfyfdtskrrtcyLAPERFNSKlyqdgksnngrltkeMDIFSLGCVIAEIFAEGRPIF 241
Cdd:PHA03209  214 lglagtvETNAPEV-------------LARDKYNSK---------------ADIWSAGIVLFEMLAYPSTIF 257
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
130-294 3.64e-06

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 50.34  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSwNWCI--LTDFAafikpVYLPEDNPGEFlfyfdtskRRTC-----YLAPERF 202
Cdd:cd08225   109 QISLGLKHIHDRKILHRDIKSQNIFLSK-NGMVakLGDFG-----IARQLNDSMEL--------AYTCvgtpyYLSPEIC 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  203 NSKLYqdgksNNgrltkEMDIFSLGCVIAEIFAEGRPI--FNLSQLFKYKSNSY--DVNREFlmeemnSTDLRNLVLDMI 278
Cdd:cd08225   175 QNRPY-----NN-----KTDIWSLGCVLYELCTLKHPFegNNLHQLVLKICQGYfaPISPNF------SRDLRSLISQLF 238
                         170
                  ....*....|....*.
gi 342187153  279 QLDPSKRLSCDELLNK 294
Cdd:cd08225   239 KVSPRDRPSITSILKR 254
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
83-233 3.70e-06

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 50.50  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNNLYDR----LSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSW 158
Cdd:cd14052    63 DNIVQLIDSWEYHGHLYIQTELCENGSLDVflseLGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFE 142
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187153  159 NWCILTDFA-AFIKPVYLPEDNPGEflfyfdtskrRTcYLAPERFNSKLYQdgksnngrltKEMDIFSLGCVIAEI 233
Cdd:cd14052   143 GTLKIGDFGmATVWPLIRGIEREGD----------RE-YIAPEILSEHMYD----------KPADIFSLGLILLEA 197
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
68-292 3.70e-06

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 50.81  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   68 FLQRIRAqsfklgqlPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSL--RPyLQDIELKFIAFQLLNALKDIHNLNIVH 145
Cdd:cd06633    74 FLQQLKH--------PNTIEYKGCYLKDHTAWLVMEYCLGSASDLLEVhkKP-LQEVEIAAITHGALQGLAYLHSHNMIH 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  146 GDIKTENILVTSWNWCILTDF--AAFIKPVYLPEDNPgeflfyfdtskrrtCYLAPERFnskLYQDgksnNGRLTKEMDI 223
Cdd:cd06633   145 RDIKAGNILLTEPGQVKLADFgsASIASPANSFVGTP--------------YWMAPEVI---LAMD----EGQYDGKVDI 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187153  224 FSLGCVIAEIFAEGRPIFN---LSQLFKYKSNsydvNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06633   204 WSLGITCIELAERKPPLFNmnaMSALYHIAQN----DSPTLQSNEWTDSFRGFVDYCLQKIPQERPSSAELL 271
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
49-233 4.14e-06

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 49.95  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   49 GEI-VIKVFIKpKDQYSLRPFLQRIRAqsFKLGQLPHVLNYSKLIETNRAGYMIRQHLKNNlydrlSLRPYLQDIELKFI 127
Cdd:cd14221    18 GEVmVMKELIR-FDEETQRTFLKEVKV--MRCLEHPNVLKFIGVLYKDKRLNFITEYIKGG-----TLRGIIKSMDSHYP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  128 AFQLLNALKDI-------HNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYLPEDNPGEFLFYFDTSKRRTCY---- 196
Cdd:cd14221    90 WSQRVSFAKDIasgmaylHSMNIIHRDLNSHNCLVRENKSVVVADFG--LARLMVDEKTQPEGLRSLKKPDRKKRYtvvg 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 342187153  197 ----LAPERFNSKLYQDgksnngrltkEMDIFSLGCVIAEI 233
Cdd:cd14221   168 npywMAPEMINGRSYDE----------KVDVFSFGIVLCEI 198
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
49-233 4.53e-06

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 50.20  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   49 GEI-VIKVFIKpKDQYSLRPFLQRIRAqsFKLGQLPHVLNYSKLIETNRAGYMIRQH-----LKNNLYDRLSLRPYLQDI 122
Cdd:cd14154    18 GEVmVMKELIR-FDEEAQRNFLKEVKV--MRSLDHPNVLKFIGVLYKDKKLNLITEYipggtLKDVLKDMARPLPWAQRV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  123 EL-KFIAfqllNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFI--KPVYLPEDNPGEFLFYFDTSKRRTCY- 196
Cdd:cd14154    95 RFaKDIA----SGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFglARLIveERLPSGNMSPSETLRHLKSPDRKKRYt 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 342187153  197 -------LAPERFNSKLYQDgksnngrltkEMDIFSLGCVIAEI 233
Cdd:cd14154   171 vvgnpywMAPEMLNGRSYDE----------KVDIFSFGIVLCEI 204
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
127-238 5.06e-06

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 50.11  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikpvylpednPGEFLFYFDTSKRRTC-YLAPERFNSK 205
Cdd:cd06621   110 IAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGV-----------SGELVNSLAGTFTGTSyYMAPERIQGG 178
                          90       100       110
                  ....*....|....*....|....*....|...
gi 342187153  206 LYqdgksnngrlTKEMDIFSLGCVIAEIfAEGR 238
Cdd:cd06621   179 PY----------SITSDVWSLGLTLLEV-AQNR 200
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
58-286 5.10e-06

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 50.04  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   58 KPKDQYSLRPFLQRIRAQS------FKLGQ-LPHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAF 129
Cdd:cd14179    30 KTNQEYAVKIVSKRMEANTqreiaaLKLCEgHPNIVKLHEVYHDQLHTFLVMELLKGgELLERIKKKQHFSETEASHIMR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVT--SWNWCI-LTDFA-AFIKPvylPEDNPgeflfyFDTSKRRTCYLAPERFNSK 205
Cdd:cd14179   110 KLVSAVSHMHDVGVVHRDLKPENLLFTdeSDNSEIkIIDFGfARLKP---PDNQP------LKTPCFTLHYAAPELLNYN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  206 LYQDgksnngrltkEMDIFSLGcVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMN---------STDLRNLVLD 276
Cdd:cd14179   181 GYDE----------SCDLWSLG-VILYTMLSGQVPFQCHDKSLTCTSAEEIMKKIKQGDFSfegeawknvSQEAKDLIQG 249
                         250
                  ....*....|
gi 342187153  277 MIQLDPSKRL 286
Cdd:cd14179   250 LLTVDPNKRI 259
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
119-293 5.87e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 50.14  E-value: 5.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDNPGEFLFYFD-----TSKRR 193
Cdd:PTZ00024  116 LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGYPPYSDTLSKDETMQrreemTSKVV 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  194 TC-YLAPE-RFNSKLYQDGksnngrltkeMDIFSLGCVIAEIFAeGRPIF-------NLSQLFKYKSNSYDVN------- 257
Cdd:PTZ00024  196 TLwYRAPElLMGAEKYHFA----------VDMWSVGCIFAELLT-GKPLFpgeneidQLGRIFELLGTPNEDNwpqakkl 264
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 342187153  258 ---REFlmEEMNSTDLRN-----------LVLDMIQLDPSKRLSCDELLN 293
Cdd:PTZ00024  265 plyTEF--TPRKPKDLKTifpnasddaidLLQSLLKLNPLERISAKEALK 312
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
108-241 6.44e-06

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: 49.58  E-value: 6.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  108 NLYDRLSLRP-YLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwNWCILTDFAAfIKPVY--LPednpgeFL 184
Cdd:cd07831    85 NLYELIKGRKrPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGS-CRGIYskPP------YT 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187153  185 FYFDTSkrrtCYLAPERFNSklyqdgksnNGRLTKEMDIFSLGCVIAEIFAEgRPIF 241
Cdd:cd07831   157 EYISTR----WYRAPECLLT---------DGYYGPKMDIWAVGCVFFEILSL-FPLF 199
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
39-292 7.24e-06

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 49.18  E-value: 7.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   39 LKTCKALDPNGEIVIKVFIKPKdqysLRPFLQRIRAQSFKLGQLPHVlNYSKLI---ETNRAGYMIRQHLKN-NLYDRLS 114
Cdd:cd14185    16 VKECRHWNENQEYAMKIIDKSK----LKGKEDMIESEILIIKSLSHP-NIVKLFevyETEKEIYLILEYVRGgDLFDAII 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  115 LRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILV-------TSWNwciLTDFAAFI---KPVYLPEDNPgefl 184
Cdd:cd14185    91 ESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpdksTTLK---LADFGLAKyvtGPIFTVCGTP---- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  185 fyfdtskrrtCYLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIAEIFAEGRPIF-----NLSQLFK-YKSNSYdvnr 258
Cdd:cd14185   164 ----------TYVAPEILSEKGY----------GLEVDMWAAG-VILYILLCGFPPFrsperDQEELFQiIQLGHY---- 218
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 342187153  259 EFLMEEMN--STDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14185   219 EFLPPYWDniSEAAKDLISRLLVVDPEKRYTAKQVL 254
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
109-292 8.08e-06

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 49.38  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILV--TSWNWCI-LTDFaAFIKpvylpEDNpGEFLf 185
Cdd:cd14171    96 LFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdNSEDAPIkLCDF-GFAK-----VDQ-GDLM- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 yfdTSKRRTCYLAPERFNSKLYQDgKSNNGRLT--------KEMDIFSLGcVIAEIFAEGRPIF-------NLSQLFKYK 250
Cdd:cd14171   168 ---TPQFTPYYVAPQVLEAQRRHR-KERSGIPTsptpytydKSCDMWSLG-VIIYIMLCGYPPFysehpsrTITKDMKRK 242
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 342187153  251 --SNSYdvnrEFLMEEMN--STDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14171   243 imTGSY----EFPEEEWSqiSEMAKDIVRKLLCVDPEERMTIEEVL 284
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
119-292 9.38e-06

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 48.97  E-value: 9.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVylpednpgeflfyfDTSKRRTCY-- 196
Cdd:cd06611   100 LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNK--------------STLQKRDTFig 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  197 ----LAPERFNSKLYQDGKSNNgrltkEMDIFSLGCVIAEIfAEGRPIFN-------LSQLFKYKSNSYDVNREFlmeem 265
Cdd:cd06611   166 tpywMAPEVVACETFKDNPYDY-----KADIWSLGITLIEL-AQMEPPHHelnpmrvLLKILKSEPPTLDQPSKW----- 234
                         170       180
                  ....*....|....*....|....*..
gi 342187153  266 nSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06611   235 -SSSFNDFLKSCLVKDPDDRPTAAELL 260
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
29-291 9.65e-06

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 48.80  E-value: 9.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   29 YVSQLNSSRFLKTCKALDPNGEIVIKVFIKpKDQYSLRPFLQRIRAQSFKLGQL--PHVLNYSKLIETNRAGYMIRQHL- 105
Cdd:cd14161     7 FLETLGKGTYGRVKKARDSSGRLVAIKSIR-KDRIKDEQDLLHIRREIEIMSSLnhPHIISVYEVFENSSKIVIVMEYAs 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYlpedNPGEFLF 185
Cdd:cd14161    86 RGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFG--LSNLY----NQDKFLQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  186 YFDTSKrrtCYLAPERFNSKLYQDgksnngrltKEMDIFSLGcVIAEIFAEGRPIFNLSQlfkYKSNSYDVNREFLMEEM 265
Cdd:cd14161   160 TYCGSP---LYASPEIVNGRPYIG---------PEVDSWSLG-VLLYILVHGTMPFDGHD---YKILVKQISSGAYREPT 223
                         250       260
                  ....*....|....*....|....*.
gi 342187153  266 NSTDLRNLVLDMIQLDPSKRLSCDEL 291
Cdd:cd14161   224 KPSDACGLIRWLLMVNPERRATLEDV 249
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
130-292 9.69e-06

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 48.80  E-value: 9.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikPVYLPednpgeflfyfdtSKRRT--C----YLAPERFN 203
Cdd:cd14116   113 ELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGW---SVHAP-------------SSRRTtlCgtldYLPPEMIE 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  204 SKLYQDgksnngrltkEMDIFSLGCVIAEiFAEGRPIFNLSQlfkYKSNSYDVNR-EFLMEEMNSTDLRNLVLDMIQLDP 282
Cdd:cd14116   177 GRMHDE----------KVDLWSLGVLCYE-FLVGKPPFEANT---YQETYKRISRvEFTFPDFVTEGARDLISRLLKHNP 242
                         170
                  ....*....|
gi 342187153  283 SKRLSCDELL 292
Cdd:cd14116   243 SQRPMLREVL 252
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
119-292 1.09e-05

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 48.60  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKPVylpednpgeflfyfdTSKRRTCY 196
Cdd:cd06607    98 LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFgsASLVCPA---------------NSFVGTPY 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  197 -LAPERFnskLYQDgksnNGRLTKEMDIFSLGCVIAEIFAEGRPIFN---LSQLFKYKSNsydvNREFLMEEMNSTDLRN 272
Cdd:cd06607   163 wMAPEVI---LAMD----EGQYDGKVDVWSLGITCIELAERKPPLFNmnaMSALYHIAQN----DSPTLSSGEWSDDFRN 231
                         170       180
                  ....*....|....*....|
gi 342187153  273 LVLDMIQLDPSKRLSCDELL 292
Cdd:cd06607   232 FVDSCLQKIPQDRPSAEDLL 251
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
119-292 1.21e-05

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 49.27  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvyLPEDNPGEFLFYFDTSkrrtCYLA 198
Cdd:cd07877   117 LTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFG-------LARHTDDEMTGYVATR----WYRA 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSKLYQDgksnngrltKEMDIFSLGCVIAEIFAeGRPIF-------NLSQLFKY---------KSNSYDVNREFL- 261
Cdd:cd07877   186 PEIMLNWMHYN---------QTVDIWSVGCIMAELLT-GRTLFpgtdhidQLKLILRLvgtpgaellKKISSESARNYIq 255
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 342187153  262 ----MEEMNSTDL--------RNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd07877   256 sltqMPKMNFANVfiganplaVDLLEKMLVLDSDKRITAAQAL 298
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
54-247 1.44e-05

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 48.81  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   54 KVFIKPKDQYSL---RPFLQRIRAQSFKLGqlphvLNYSklIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAF 129
Cdd:cd05603    31 KTILKKKEQNHImaeRNVLLKNLKHPFLVG-----LHYS--FQTSEKLYFVLDYVNGgELFFHLQRERCFLEPRARFYAA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNPGEFlfyfdtskrrtC----YLAPERFNSK 205
Cdd:cd05603   104 EVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDF-GLCKEGMEPEETTSTF-----------CgtpeYLAPEVLRKE 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 342187153  206 LYQdgksnngrltKEMDIFSLGCVIAEIFaEGRPIF---NLSQLF 247
Cdd:cd05603   172 PYD----------RTVDWWCLGAVLYEML-YGLPPFysrDVSQMY 205
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
106-245 1.48e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 49.12  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLYDRLSLRPY-LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAA--FIKPVYlpeDNPge 182
Cdd:PHA03211  243 RSDLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAacFARGSW---STP-- 317
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187153  183 flFYF------DTSkrrtcylAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQ 245
Cdd:PHA03211  318 --FHYgiagtvDTN-------APEVLAGDPY----------TPSVDIWSAGLVIFEAAVHTASLFSASR 367
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
119-292 1.77e-05

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 48.51  E-value: 1.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvyLPEDNPGEFLFYFDTSkrrtCYLA 198
Cdd:cd07878   115 LSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFG-------LARQADDEMTGYVATR----WYRA 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERFNSKLYQDgksnngrltKEMDIFSLGCVIAEIFaEGRPIFN----LSQLFKYKSNSYDVNREFLME----------- 263
Cdd:cd07878   184 PEIMLNWMHYN---------QTVDIWSVGCIMAELL-KGKALFPgndyIDQLKRIMEVVGTPSPEVLKKisseharkyiq 253
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 342187153  264 ---EMNSTDLR-----------NLVLDMIQLDPSKRLSCDELL 292
Cdd:cd07878   254 slpHMPQQDLKkifrganplaiDLLEKMLVLDSDKRISASEAL 296
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
134-293 1.79e-05

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 48.06  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  134 ALKDIHNLNIVHGDIKTENILVTSWN---WCILTDFA---------AFIKPVYLPEdnpgeflfyfdtskrrtcYLAPER 201
Cdd:cd14172   115 AIQYLHSMNIAHRDVKPENLLYTSKEkdaVLKLTDFGfakettvqnALQTPCYTPY------------------YVAPEV 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  202 FNSKLYQdgksnngrltKEMDIFSLGcVIAEIFAEGRPIF--NLSQLF------KYKSNSYdvnrEFLMEEMN--STDLR 271
Cdd:cd14172   177 LGPEKYD----------KSCDMWSLG-VIMYILLCGFPPFysNTGQAIspgmkrRIRMGQY----GFPNPEWAevSEEAK 241
                         170       180
                  ....*....|....*....|..
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14172   242 QLIRHLLKTDPTERMTITQFMN 263
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
114-288 1.95e-05

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 48.15  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  114 SLRPYLQDIE--------LKFiAFQLLNALKDIHNLNIVHGDIKTENILVTSwNWCI-LTDF--AAFIkpvylPED---- 178
Cdd:cd05038    94 SLRDYLQRHRdqidlkrlLLF-ASQICKGMEYLGSQRYIHRDLAARNILVES-EDLVkISDFglAKVL-----PEDkeyy 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  179 ---NPGEF-LFYFdtskrrtcylAPERFNSKlyqdgksnngRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFkyksnsy 254
Cdd:cd05038   167 yvkEPGESpIFWY----------APECLRES----------RFSSASDVWSFGVTLYELFTYGDPSQSPPALF------- 219
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 342187153  255 dvnreflMEEMNSTDLRNLVLDMIQ-LDPSKRLSC 288
Cdd:cd05038   220 -------LRMIGIAQGQMIVTRLLElLKSGERLPR 247
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
47-292 2.43e-05

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 47.74  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   47 PNGEIV-IKVFIKPKDQYSLRPFLQRIRAQSfkLGQLPHVLNYSKLIETNRAGYMIRQHLK-NNLYDRLSLRPYLQDIEL 124
Cdd:cd06610    24 PKKEKVaIKRIDLEKCQTSMDELRKEIQAMS--QCNHPNVVSYYTSFVVGDELWLVMPLLSgGSLLDIMKSSYPRGGLDE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQL---LNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIkpvYLPEDNpgeflfyfdTSKRRT----- 194
Cdd:cd06610   102 AIIATVLkevLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFgvSASL---ATGGDR---------TRKVRKtfvgt 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  195 -CYLAPERFNSKLYQDGKSnngrltkemDIFSLGCVIAEIfAEGRPIFnlSQLFKYK---------SNSYDVNREFlmeE 264
Cdd:cd06610   170 pCWMAPEVMEQVRGYDFKA---------DIWSFGITAIEL-ATGAAPY--SKYPPMKvlmltlqndPPSLETGADY---K 234
                         250       260
                  ....*....|....*....|....*...
gi 342187153  265 MNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06610   235 KYSKSFRKMISLCLQKDPSKRPTAEELL 262
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
124-241 2.60e-05

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


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 47.72  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  124 LKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYlpednpgEFLFYFDTSKRRTCYLAPERFN 203
Cdd:cd07862   112 IKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFG--LARIY-------SFQMALTSVVVTLWYRAPEVLL 182
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 342187153  204 SKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEgRPIF 241
Cdd:cd07862   183 QSSY----------ATPVDLWSVGCIFAEMFRR-KPLF 209
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
105-241 2.76e-05

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: 48.02  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  105 LKNNLYDRLSLRPY----LQDIelKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWN--WCILTDF--AAFikpvylp 176
Cdd:cd14212    84 LGVNLYELLKQNQFrglsLQLI--RKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDspEIKLIDFgsACF------- 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 342187153  177 ednpgeflfyfdtsKRRTCYL--------APERFNSKLYQDGksnngrltkeMDIFSLGCVIAEIFAeGRPIF 241
Cdd:cd14212   155 --------------ENYTLYTyiqsrfyrSPEVLLGLPYSTA----------IDMWSLGCIAAELFL-GLPLF 202
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
70-352 3.04e-05

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 47.74  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   70 QRIRAQSFKLGQLPHVLNYSKLIET-NRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDI 148
Cdd:cd14223    50 ERIMLSLVSTGDCPFIVCMSYAFHTpDKLSFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  149 KTENILVTSWNWCILTDFAafikpvylpednpgeflFYFDTSKRRT-------CYLAPERFNSKLYQDGKSnngrltkem 221
Cdd:cd14223   130 KPANILLDEFGHVRISDLG-----------------LACDFSKKKPhasvgthGYMAPEVLQKGVAYDSSA--------- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  222 DIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSC-----DELLNK-- 294
Cdd:cd14223   184 DWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCmgrgaQEVKEEpf 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 342187153  295 YRGIffpDYFYTFIYDYFRNLVTMTTSTPISDNTCTNSTLEDN---VKLLDETTEkIYRDF 352
Cdd:cd14223   264 FRGL---DWQMVFLQKYPPPLIPPRGEVNAADAFDIGSFDEEDtkgIKLLESDQE-LYRNF 320
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
123-241 3.08e-05

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: 47.75  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  123 ELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYLPEDNPGeflfyfdTSKRRTC-YLAPE- 200
Cdd:cd07845   109 QVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFG--LARTYGLPAKPM-------TPKVVTLwYRAPEl 179
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 342187153  201 RFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF 241
Cdd:cd07845   180 LLGCTTY----------TTAIDMWAVGCILAELLA-HKPLL 209
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
32-295 3.25e-05

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 47.32  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   32 QLNSSRF--LKTCKALDPNGEIVIKvFIKPKDQYSLRPFLQRIRAQS----FKLGQLPHVLNYSKLIETNRAGYMIRQHL 105
Cdd:cd14194    12 ELGSGQFavVKKCREKSTGLQYAAK-FIKKRRTKSSRRGVSREDIERevsiLKEIQHPNVITLHEVYENKTDVILILELV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWN----WCILTDFAAFIKPvylpeDNP 180
Cdd:cd14194    91 AGgELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHKI-----DFG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  181 GEFLFYFDTSKrrtcYLAPERFNsklYQDgksnngrLTKEMDIFSLGcVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREF 260
Cdd:cd14194   166 NEFKNIFGTPE----FVAPEIVN---YEP-------LGLEADMWSIG-VITYILLSGASPFLGDTKQETLANVSAVNYEF 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 342187153  261 LMEEMNSTD--LRNLVLDMIQLDPSKRLSC-DELLNKY 295
Cdd:cd14194   231 EDEYFSNTSalAKDFIRRLLVKDPKKRMTIqDSLQHPW 268
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
117-292 3.46e-05

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 47.42  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  117 PYLQDIELKFIaFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFAAFIKpvyLPEDNPGEFLF---YFDTskr 192
Cdd:cd06630    99 AFSENVIINYT-LQILRGLAYLHDNQIIHRDLKGANLLVDSTGQRLrIADFGAAAR---LASKGTGAGEFqgqLLGT--- 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  193 rTCYLAPERFNSKLYqdGKSnngrltkeMDIFSLGCVIAEIfAEGRPIFN-------LSQLFKYKSnsydVNREFLMEEM 265
Cdd:cd06630   172 -IAFMAPEVLRGEQY--GRS--------CDVWSVGCVIIEM-ATAKPPWNaekisnhLALIFKIAS----ATTPPPIPEH 235
                         170       180
                  ....*....|....*....|....*..
gi 342187153  266 NSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06630   236 LSPGLRDVTLRCLELQPEDRPPARELL 262
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
119-292 3.75e-05

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 47.23  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFA--AFIKPvylpednpgeflfyfDTSKRRTC- 195
Cdd:cd06647   100 MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGfcAQITP---------------EQSKRSTMv 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 ----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIfAEGRPIF----NLSQLFKYKSNSydvNREFLMEEMNS 267
Cdd:cd06647   165 gtpyWMAPEVVTRKAY----------GPKVDIWSLGIMAIEM-VEGEPPYlnenPLRALYLIATNG---TPELQNPEKLS 230
                         170       180
                  ....*....|....*....|....*
gi 342187153  268 TDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06647   231 AIFRDFLNRCLEMDVEKRGSAKELL 255
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
26-156 3.88e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 47.32  E-value: 3.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   26 EVHYVSQLNSSRF---LKTCKALDpnGEI-VIKVFIKP-----KDQYSLRpflqRIRAQSFkLGQLPHVLNY-SKLIETN 95
Cdd:cd14138     6 EFHELEKIGSGEFgsvFKCVKRLD--GCIyAIKRSKKPlagsvDEQNALR----EVYAHAV-LGQHSHVVRYySAWAEDD 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153   96 ragYMIRQHLKNN---LYDRLS----LRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVT 156
Cdd:cd14138    79 ---HMLIQNEYCNggsLADAISenyrIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIS 143
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
115-293 4.02e-05

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 47.24  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  115 LRPY-LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKpvylpednpgeflfyFDTSK 191
Cdd:cd06609    90 LKPGpLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFgvSGQLT---------------STMSK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  192 RRTC-----YLAPERFNSKLYqDGKSnngrltkemDIFSLGCVIAEIfAEGRP----IFNLSQLFKYKSNSYDVnrefLM 262
Cdd:cd06609   155 RNTFvgtpfWMAPEVIKQSGY-DEKA---------DIWSLGITAIEL-AKGEPplsdLHPMRVLFLIPKNNPPS----LE 219
                         170       180       190
                  ....*....|....*....|....*....|.
gi 342187153  263 EEMNSTDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd06609   220 GNKFSKPFKDFVELCLNKDPKERPSAKELLK 250
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
125-286 4.59e-05

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 47.12  E-value: 4.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVylPEdnpgeflfyfdtskrRT---C----YL 197
Cdd:PTZ00263  121 KFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDF-GFAKKV--PD---------------RTftlCgtpeYL 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  198 APERFNSKLYQdgksnngrltKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSnsyDVNREFLMEEMNSTDLRNLVLDM 277
Cdd:PTZ00263  183 APEVIQSKGHG----------KAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEK---ILAGRLKFPNWFDGRARDLVKGL 249

                  ....*....
gi 342187153  278 IQLDPSKRL 286
Cdd:PTZ00263  250 LQTDHTKRL 258
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
125-286 6.50e-05

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 46.93  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNPGEFlfyfdtskrrtC----YLAPE 200
Cdd:cd05575    99 RFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDF-GLCKEGIEPSDTTSTF-----------CgtpeYLAPE 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  201 RFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIFnlsqlfkYKSNS---YD--VNREFLMEEMNSTDLRNLVL 275
Cdd:cd05575   167 VLRKQPY----------DRTVDWWCLGAVLYEMLY-GLPPF-------YSRDTaemYDniLHKPLRLRTNVSPSARDLLE 228
                         170
                  ....*....|.
gi 342187153  276 DMIQLDPSKRL 286
Cdd:cd05575   229 GLLQKDRTKRL 239
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
108-288 8.21e-05

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 46.59  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  108 NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpvylpednpgeflFYF 187
Cdd:cd05633    94 DLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLG-----------------LAC 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  188 DTSKRRT-------CYLAPERFNSKLYQDGKSnngrltkemDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREF 260
Cdd:cd05633   157 DFSKKKPhasvgthGYMAPEVLQKGTAYDSSA---------DWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNV 227
                         170       180
                  ....*....|....*....|....*...
gi 342187153  261 LMEEMNSTDLRNLVLDMIQLDPSKRLSC 288
Cdd:cd05633   228 ELPDSFSPELKSLLEGLLQRDVSKRLGC 255
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
98-166 8.65e-05

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 44.56  E-value: 8.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   98 GYMIRQHLKN-NLYDRLSLRPYLQDIelkfiAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILtDF 166
Cdd:COG3642    31 ADLVMEYIEGeTLADLLEEGELPPEL-----LRELGRLLARLHRAGIVHGDLTTSNILVDDGGVYLI-DF 94
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
126-290 9.30e-05

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 46.14  E-value: 9.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  126 FIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikPVYLPEdnpGEflfyfdTSKRR---TCYLAPERF 202
Cdd:cd05631   106 FYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGL---AVQIPE---GE------TVRGRvgtVGYMAPEVI 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  203 NSKLYqdgksnngrlTKEMDIFSLGCVIAEIFaEGRPIFnlsQLFKYKSNSYDVNREFLMEEMN-----STDLRNLVLDM 277
Cdd:cd05631   174 NNEKY----------TFSPDWWGLGCLIYEMI-QGQSPF---RKRKERVKREEVDRRVKEDQEEysekfSEDAKSICRML 239
                         170
                  ....*....|...
gi 342187153  278 IQLDPSKRLSCDE 290
Cdd:cd05631   240 LTKNPKERLGCRG 252
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
83-292 9.31e-05

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 46.26  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI 162
Cdd:cd06654    77 PNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVK 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  163 LTDFA--AFIKPvylpednpgeflfyfDTSKRRTC-----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFA 235
Cdd:cd06654   157 LTDFGfcAQITP---------------EQSKRSTMvgtpyWMAPEVVTRKAY----------GPKVDIWSLGIMAIEMIE 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187153  236 EGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06654   212 GEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELL 268
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
81-334 9.45e-05

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 46.23  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   81 QLPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLS-LRPYLQDIEL---------------KFIAFQLLNALKDIHNLNIV 144
Cdd:cd05593    58 EVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCfVMEYVNGGELffhlsrervfsedrtRFYGAEIVSALDYLHSGKIV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  145 HGDIKTENILVTSWNWCILTDFAAFIKPVYlpednpgeflfyfDTSKRRTCYLAPERFNSKLYQDgkSNNGRltkEMDIF 224
Cdd:cd05593   138 YRDLKLENLMLDKDGHIKITDFGLCKEGIT-------------DAATMKTFCGTPEYLAPEVLED--NDYGR---AVDWW 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  225 SLGCVIAEIFAEGRPIFNL--SQLFKYksnsydvnreFLMEEMN-----STDLRNLVLDMIQLDPSKRLSC--DELLNKY 295
Cdd:cd05593   200 GLGVVMYEMMCGRLPFYNQdhEKLFEL----------ILMEDIKfprtlSADAKSLLSGLLIKDPNKRLGGgpDDAKEIM 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 342187153  296 RGIFFPDYFYTFIYDY-----FRNLVTMTTSTPISDNTCTNSTL 334
Cdd:cd05593   270 RHSFFTGVNWQDVYDKklvppFKPQVTSETDTRYFDEEFTAQTI 313
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
115-291 9.88e-05

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 45.88  E-value: 9.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  115 LRPYLQD-------IELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSwNWCI-LTDFAAfikPVYLPEDNpgeflfY 186
Cdd:cd05056    93 LRSYLQVnkysldlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS-PDCVkLGDFGL---SRYMEDES------Y 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  187 FDTSKRR--TCYLAPERFNSKlyqdgksnngRLTKEMDIFSLGCVIAEIFAEGRpifnlsQLFKYKSNSyDV-----NRE 259
Cdd:cd05056   163 YKASKGKlpIKWMAPESINFR----------RFTSASDVWMFGVCMWEILMLGV------KPFQGVKNN-DVigrieNGE 225
                         170       180       190
                  ....*....|....*....|....*....|...
gi 342187153  260 FL-MEEMNSTDLRNLVLDMIQLDPSKRLSCDEL 291
Cdd:cd05056   226 RLpMPPNCPPTLYSLMTKCWAYDPSKRPRFTEL 258
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
109-157 1.04e-04

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 46.02  E-value: 1.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 342187153  109 LYDRL---SLRPY-LQDIelKFIAFQLLNALKDIHNLNIVHGDIKTENILVTS 157
Cdd:cd14134   100 LYDFLkknNYGPFpLEHV--QHIAKQLLEAVAFLHDLKLTHTDLKPENILLVD 150
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
130-293 1.07e-04

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 45.74  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCIL--TDF--AAFIKpvylpednPGEFLFYFDTSKrrtCYLAPERFNSK 205
Cdd:cd14121   103 QLASALQFLREHNISHMDLKPQNLLLSSRYNPVLklADFgfAQHLK--------PNDEAHSLRGSP---LYMAPEMILKK 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  206 LYqDGKsnngrltkeMDIFSLGCVIAEI-FaeGRPifnlsqlfKYKSNSYdvnrEFLMEEMN-------------STDLR 271
Cdd:cd14121   172 KY-DAR---------VDLWSVGVILYEClF--GRA--------PFASRSF----EELEEKIRsskpieiptrpelSADCR 227
                         170       180
                  ....*....|....*....|..
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14121   228 DLLLRLLQRDPDRRISFEEFFA 249
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
113-184 1.11e-04

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 45.68  E-value: 1.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153  113 LSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIKP-VYLPEDNPGEFL 184
Cdd:cd14110    90 LAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLgnAQPFNQgKVLMTDKKGDYV 164
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
81-353 1.16e-04

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 46.15  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   81 QLPHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSL-----------------RPYLQDiELKFIAFQLLNALKDIHNLNI 143
Cdd:cd05595    38 EVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFvmeyanggelffhlsreRVFTED-RARFYGAEIVSALEYLHSRDV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  144 VHGDIKTENILVTSWNWCILTDFAAFIKPVYlpednpgeflfyfDTSKRRT-C----YLAPERFNSKLYqdgksnnGRlt 218
Cdd:cd05595   117 VYRDIKLENLMLDKDGHIKITDFGLCKEGIT-------------DGATMKTfCgtpeYLAPEVLEDNDY-------GR-- 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  219 kEMDIFSLGCVIAEIFAEGRPIFNL--SQLFKyksnsydvnrEFLMEEMN-----STDLRNLVLDMIQLDPSKRL----- 286
Cdd:cd05595   175 -AVDWWGLGVVMYEMMCGRLPFYNQdhERLFE----------LILMEEIRfprtlSPEAKSLLAGLLKKDPKQRLgggps 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187153  287 -SCDELLNK-YRGIFFPDYFYTFIYDYFRNLVTMTTSTPISDNTCTNSTLE-------DNVKLLDETTEKIYRDFS 353
Cdd:cd05595   244 dAKEVMEHRfFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITitppdryDSLDLLESDQRTHFPQFS 319
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
109-290 1.17e-04

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 46.11  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVylpeDNPGEFLFYFD 188
Cdd:cd05604    84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGI----SNSDTTTTFCG 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  189 TSKrrtcYLAPERFNSKLYQdgksnngrltKEMDIFSLGCVIAEIFAEGRPIFNlsqlfKYKSNSYD--VNREFLMEEMN 266
Cdd:cd05604   160 TPE----YLAPEVIRKQPYD----------NTVDWWCLGSVLYEMLYGLPPFYC-----RDTAEMYEniLHKPLVLRPGI 220
                         170       180
                  ....*....|....*....|....
gi 342187153  267 STDLRNLVLDMIQLDPSKRLSCDE 290
Cdd:cd05604   221 SLTAWSILEELLEKDRQLRLGAKE 244
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
127-239 1.33e-04

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 45.42  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSwNWCILTDFAAFIKPVYLpedNPGEFLFYFDTSKRRTCYLAPERFnsKL 206
Cdd:cd14063   102 IAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSLSGLL---QPGRREDTLVIPNGWLCYLAPEII--RA 175
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 342187153  207 YQDGKSNNGRL--TKEMDIFSLGCVIAEIFAEGRP 239
Cdd:cd14063   176 LSPDLDFEESLpfTKASDVYAFGTVWYELLAGRWP 210
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
108-288 1.36e-04

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 45.69  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  108 NLYDRLSLRP--YLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--------------AAFIK 171
Cdd:cd05574    87 ELFRLLQKQPgkRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppvrKSLRK 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  172 PVYLPEDNPGEFLFYFDTSKRRTC-------YLAPERFNSklyqDGKSNNgrltkeMDIFSLGCVIAEiFAEGRPIF--- 241
Cdd:cd05574   167 GSRRSSVKSIEKETFVAEPSARSNsfvgteeYIAPEVIKG----DGHGSA------VDWWTLGILLYE-MLYGTTPFkgs 235
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 342187153  242 NLSQLFkykSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSC 288
Cdd:cd05574   236 NRDETF---SNILKKELTFPESPPVSSEAKDLIRKLLVKDPSKRLGS 279
WD40 COG2319
WD40 repeat [General function prediction only];
1069-1261 1.40e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.06  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1069 GKLIATLmENEPNSITSSAVSP-GETpyLITGSDQGVIKIWNLKEiivGEVySSSLTYDcSSTVTQITMIPNFDAFAVSS 1147
Cdd:COG2319   236 GKLLRTL-TGHSGSVRSVAFSPdGRL--LASGSADGTVRLWDLAT---GEL-LRTLTGH-SGGVNSVAFSPDGKLLASGS 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1148 KDGQIIVLKVNHYQQesevkflncecirkinLKNFGKNEYAVRMRAFVNEEKSLLVALTNlSRVIIFDIRTLERLQIIEN 1227
Cdd:COG2319   308 DDGTVRLWDLATGKL----------------LRTLTGHTGAVRSVAFSPDGKTLASGSDD-GTVRLWDLATGELLRTLTG 370
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 342187153 1228 sprH-GAVSSICIDEECCVLILGTTRGIIDIWDIR 1261
Cdd:COG2319   371 ---HtGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
109-157 1.54e-04

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: 44.95  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTS 157
Cdd:cd14006    76 LLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLAD 124
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
32-293 1.98e-04

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 44.95  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   32 QLNSSRF--LKTCKALDPNGEIVIKVFIKPKDQYSLRPFL-QRIRAQSFKLGQLPHVlNYSKL--IETNRAGYMIRQHLK 106
Cdd:cd14196    12 ELGSGQFaiVKKCREKSTGLEYAAKFIKKRQSRASRRGVSrEEIEREVSILRQVLHP-NIITLhdVYENRTDVVLILELV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  107 N--NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI----LTDFAAfikpVYLPEDNP 180
Cdd:cd14196    91 SggELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIphikLIDFGL----AHEIEDGV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  181 gEFLFYFDTSKrrtcYLAPERFNsklYQDgksnngrLTKEMDIFSLGcVIAEIFAEGRPIF----NLSQLFKYKSNSYDV 256
Cdd:cd14196   167 -EFKNIFGTPE----FVAPEIVN---YEP-------LGLEADMWSIG-VITYILLSGASPFlgdtKQETLANITAVSYDF 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 342187153  257 NREFLmeeMNSTDL-RNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14196   231 DEEFF---SHTSELaKDFIRKLLVKETRKRLTIQEALR 265
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
83-292 1.99e-04

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 45.10  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI 162
Cdd:cd06655    76 PNIVNFLDSFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVK 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  163 LTDFA--AFIKPvylpednpgeflfyfDTSKRRTC-----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFA 235
Cdd:cd06655   156 LTDFGfcAQITP---------------EQSKRSTMvgtpyWMAPEVVTRKAY----------GPKVDIWSLGIMAIEMVE 210
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187153  236 EGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06655   211 GEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELL 267
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
130-291 2.38e-04

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 44.56  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikpvylpednpGEFLFYFD------TSKRRTCYLAPERFN 203
Cdd:cd14119   105 QLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGV------------AEALDLFAeddtctTSQGSPAFQPPEIAN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  204 SKLYQDGksnngrltKEMDIFSLG-----CVIAEIFAEGRPIFNLsqlfkYKSNSydvNREFLMEEMNSTDLRNLVLDMI 278
Cdd:cd14119   173 GQDSFSG--------FKVDIWSAGvtlynMTTGKYPFEGDNIYKL-----FENIG---KGEYTIPDDVDPDLQDLLRGML 236
                         170
                  ....*....|...
gi 342187153  279 QLDPSKRLSCDEL 291
Cdd:cd14119   237 EKDPEKRFTIEQI 249
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
83-292 2.44e-04

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 44.71  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI 162
Cdd:cd06656    76 PNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVK 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  163 LTDFA--AFIKPvylpednpgeflfyfDTSKRRTC-----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFA 235
Cdd:cd06656   156 LTDFGfcAQITP---------------EQSKRSTMvgtpyWMAPEVVTRKAY----------GPKVDIWSLGIMAIEMVE 210
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 342187153  236 EGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd06656   211 GEPPYLNENPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELL 267
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1081-1259 2.44e-04

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: 44.63  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1081 NSITSSAVSPGETpYLITGSDQGVIKIWNLKEIIVGEVYSSSltydcSSTVTQITMIPNFDAFAVSSKDGQIIVlkvnhy 1160
Cdd:cd00200   136 DWVNSVAFSPDGT-FVASSSQDGTIKLWDLRTGKCVATLTGH-----TGEVNSVAFSPDGEKLLSSSSDGTIKL------ 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1161 qqeSEVKFLNCecirkinLKNFGKNEYAVRMRAFvNEEKSLLVALTNLSRVIIFDIRTLERLQIIENSPrhGAVSSICID 1240
Cdd:cd00200   204 ---WDLSTGKC-------LGTLRGHENGVNSVAF-SPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHT--NSVTSLAWS 270
                         170
                  ....*....|....*....
gi 342187153 1241 EECCVLILGTTRGIIDIWD 1259
Cdd:cd00200   271 PDGKRLASGSADGTIRIWD 289
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
83-158 2.58e-04

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 44.64  E-value: 2.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSW 158
Cdd:cd14184    59 PNIIMLIEEMDTPAELYLVMELVKGgDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEY 135
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
130-285 2.59e-04

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 44.63  E-value: 2.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikpvylpednpGEFlFYFDTSKRRTC-----YLAPERFNS 204
Cdd:cd08228   114 QLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL------------GRF-FSSKTTAAHSLvgtpyYMSPERIHE 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 KLYqDGKSnngrltkemDIFSLGCVIAEIFAEGRPIF-NLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPS 283
Cdd:cd08228   181 NGY-NFKS---------DIWSLGCLLYEMAALQSPFYgDKMNLFSLCQKIEQCDYPPLPTEHYSEKLRELVSMCIYPDPD 250

                  ..
gi 342187153  284 KR 285
Cdd:cd08228   251 QR 252
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
130-293 2.87e-04

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 44.35  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVY-LPEDNPGEFLfyfdTSKRRTCY-LAPERFNskly 207
Cdd:cd06631   111 QILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCInLSSGSQSQLL----KSMRGTPYwMAPEVIN---- 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  208 qdgKSNNGRltkEMDIFSLGCVIAEIfAEGRP----IFNLSQLFKYKSNSYDVNReflMEEMNSTDLRNLVLDMIQLDPS 283
Cdd:cd06631   183 ---ETGHGR---KSDIWSIGCTVFEM-ATGKPpwadMNPMAAIFAIGSGRKPVPR---LPDKFSPEARDFVHACLTRDQD 252
                         170
                  ....*....|
gi 342187153  284 KRLSCDELLN 293
Cdd:cd06631   253 ERPSAEQLLK 262
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1069-1154 2.94e-04

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: 44.63  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153 1069 GKLIATLMENEpNSITSSAVSPGETPYLITGSDqGVIKIWNLKEIIVGEVYSSsltydCSSTVTQITMIPNFDAFAVSSK 1148
Cdd:cd00200   167 GKCVATLTGHT-GEVNSVAFSPDGEKLLSSSSD-GTIKLWDLSTGKCLGTLRG-----HENGVNSVAFSPDGYLLASGSE 239

                  ....*.
gi 342187153 1149 DGQIIV 1154
Cdd:cd00200   240 DGTIRV 245
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
123-239 2.98e-04

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 44.18  E-value: 2.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  123 ELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYlpednpgeflfyfDTSKRRT-----CYL 197
Cdd:cd06612   100 EIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTD-------------TMAKRNTvigtpFWM 166
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 342187153  198 APE-----RFNSKlyqdgksnngrltkeMDIFSLGCVIAEIfAEGRP 239
Cdd:cd06612   167 APEviqeiGYNNK---------------ADIWSLGITAIEM-AEGKP 197
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
100-155 3.14e-04

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 44.45  E-value: 3.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 342187153  100 MIRQHLKNnlYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILV 155
Cdd:cd14132    92 LIFEYVNN--TDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI 145
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
125-249 3.35e-04

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 44.61  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvylpEDNPGefLFYFDTSKRRTCYLAPERFNS 204
Cdd:cd05621   154 KFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMK-----MDETG--MVHCDTAVGTPDYISPEVLKS 226
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 342187153  205 klyQDGKSNNGRltkEMDIFSLGCVIAEIFAEGRPIFNLSQLFKY 249
Cdd:cd05621   227 ---QGGDGYYGR---ECDWWSVGVFLFEMLVGDTPFYADSLVGTY 265
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
119-292 3.69e-04

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


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 44.26  E-value: 3.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  119 LQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAaFIKPVYLpednpgeflfyfDTSKRRTC--- 195
Cdd:cd06658   115 MNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFG-FCAQVSK------------EVPKRKSLvgt 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  196 --YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNL 273
Cdd:cd06658   182 pyWMAPEVISRLPY----------GTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLRGF 251
                         170
                  ....*....|....*....
gi 342187153  274 VLDMIQLDPSKRLSCDELL 292
Cdd:cd06658   252 LDLMLVREPSQRATAQELL 270
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
103-292 3.77e-04

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 43.91  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  103 QHLKNNLYDRLSLRPYLQdielkfIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvyLPEDNP-G 181
Cdd:cd13979    90 QQLIYEGSEPLPLAHRIL------ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVK---LGEGNEvG 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  182 EFLFYFdtskRRTC-YLAPERFNSKlyqdgksnngRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVnREF 260
Cdd:cd13979   161 TPRSHI----GGTYtYRAPELLKGE----------RVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDL-RPD 225
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 342187153  261 LMEEMNSTD---LRNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd13979   226 LSGLEDSEFgqrLRSLISRCWSAQPAERPNADESL 260
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
67-157 3.91e-04

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 43.73  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   67 PFLQRIRAQSFK----LGQLPHVLNYSKL--IETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIH 139
Cdd:cd14107    36 PLRSSTRARAFQerdiLARLSHRRLTCLLdqFETRKTLILILELCSSeELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLH 115
                          90
                  ....*....|....*...
gi 342187153  140 NLNIVHGDIKTENILVTS 157
Cdd:cd14107   116 GMNILHLDIKPDNILMVS 133
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
42-294 4.28e-04

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 43.64  E-value: 4.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153    42 CKALDPNGEIVIKVFIKpkdqySLRPFLQRIRAQSFK-----LGQL--PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRL 113
Cdd:pfam07714   18 GTLKGEGENTKIKVAVK-----TLKEGADEEEREDFLeeasiMKKLdhPNIVKLLGVCTQGEPLYIVTEYMPGgDLLDFL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   114 -SLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF----AAFIKPVYLPEDNpgeflfyfd 188
Cdd:pfam07714   93 rKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFglsrDIYDDDYYRKRGG--------- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   189 tSKRRTCYLAPERFnsklyqdgksNNGRLTKEMDIFSLGCVIAEIFAEGR-PIFNLS--QLFKYksnsydVNREFLME-- 263
Cdd:pfam07714  164 -GKLPIKWMAPESL----------KDGKFTSKSDVWSFGVLLWEIFTLGEqPYPGMSneEVLEF------LEDGYRLPqp 226
                          250       260       270
                   ....*....|....*....|....*....|.
gi 342187153   264 EMNSTDLRNLVLDMIQLDPSKRLSCDELLNK 294
Cdd:pfam07714  227 ENCPDELYDLMKQCWAYDPEDRPTFSELVED 257
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
100-243 4.39e-04

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 43.67  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  100 MIRQHLKN-NLYDRLSLRPYLQDIELKF-IAFQLLNALKDIHNLN--IVHGDIKTENILVTSWNWCILTDF--AAFIKPv 173
Cdd:cd14064    69 IVTQYVSGgSLFSLLHEQKRVIDLQSKLiIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFgeSRFLQS- 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187153  174 yLPEDN----PGEFLfyfdtskrrtcYLAPERFnsklyqdgkSNNGRLTKEMDIFSLGCVIAEIFAEGRPIFNL 243
Cdd:cd14064   148 -LDEDNmtkqPGNLR-----------WMAPEVF---------TQCTRYSIKADVFSYALCLWELLTGEIPFAHL 200
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
78-288 4.41e-04

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


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 43.96  E-value: 4.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   78 KLGQLPHVLNYSKLIETNRAGYMIR----QHLKNNLYdrlSLRPYLQDIEL---------------KFIAFQLLNALKDI 138
Cdd:cd05612    41 RLKQEQHVHNEKRVLKEVSHPFIIRlfwtEHDQRFLY---MLMEYVPGGELfsylrnsgrfsnstgLFYASEIVCALEYL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  139 HNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVylpednpgeflfyfdtsKRRT---C----YLAPERFNSKLYQdgk 211
Cdd:cd05612   118 HSKEIVYRDLKPENILLDKEGHIKLTDF-GFAKKL-----------------RDRTwtlCgtpeYLAPEVIQSKGHN--- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  212 snngrltKEMDIFSLGCVIAEIFAeGRPIFNLSQLF----KYKSNSYDVNREFlmeemnSTDLRNLVLDMIQLDPSKRLS 287
Cdd:cd05612   177 -------KAVDWWALGILIYEMLV-GYPPFFDDNPFgiyeKILAGKLEFPRHL------DLYAKDLIKKLLVVDRTRRLG 242

                  .
gi 342187153  288 C 288
Cdd:cd05612   243 N 243
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
109-293 4.72e-04

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 43.53  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  109 LYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafIKPVYlpedNPGEFLFYFD 188
Cdd:cd14073    88 LYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFG--LSNLY----SKDKLLQTFC 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  189 TSKrrtCYLAPERFNSKLYQDgksnngrltKEMDIFSLGcVIAEIFAEGRPIFNLSQlfkYKSNSYDVNREFLMEEMNST 268
Cdd:cd14073   162 GSP---LYASPEIVNGTPYQG---------PEVDCWSLG-VLLYTLVYGTMPFDGSD---FKRLVKQISSGDYREPTQPS 225
                         170       180
                  ....*....|....*....|....*
gi 342187153  269 DLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14073   226 DASGLIRWMLTVNPKRRATIEDIAN 250
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
127-297 4.82e-04

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 43.80  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVtswnWCI---------LTDFA----AFIKPVYLPEDNPGeflfyfdtskrr 193
Cdd:cd14067   119 IAYQIAAGLAYLHKKNIIFCDLKSDNILV----WSLdvqehinikLSDYGisrqSFHEGALGVEGTPG------------ 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  194 tcYLAPERFNSKLYQDgksnngrltkEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVnREFL--MEEMNSTDLR 271
Cdd:cd14067   183 --YQAPEIRPRIVYDE----------KVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKGI-RPVLgqPEEVQFFRLQ 249
                         170       180
                  ....*....|....*....|....*.
gi 342187153  272 NLVLDMIQLDPSKRLSCDELLNKYRG 297
Cdd:cd14067   250 ALMMECWDTKPEKRPLACSVVEQMKD 275
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
106-293 5.71e-04

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 43.84  E-value: 5.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLY---------DRLSLRPYLQDI----ELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIK- 171
Cdd:cd05601    73 SENLYlvmeyhpggDLLSLLSRYDDIfeesMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKl 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  172 ----------PVYLPEdnpgeflfyfdtskrrtcYLAPERFNSkLYQDGKSNNGrltKEMDIFSLGCVIAEI------FA 235
Cdd:cd05601   153 ssdktvtskmPVGTPD------------------YIAPEVLTS-MNGGSKGTYG---VECDWWSLGIVAYEMlygktpFT 210
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153  236 EGRPIFNLSQLFKYKSNSydvnrEFLMEEMNSTDLRNLVLDMIQlDPSKRLSCDELLN 293
Cdd:cd05601   211 EDTVIKTYSNIMNFKKFL-----KFPEDPKVSESAVDLIKGLLT-DAKERLGYEGLCC 262
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
124-258 7.26e-04

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 43.91  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  124 LKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFI--------KPVY---LPEDNPGEFLFYfdtskR 192
Cdd:PLN03224  311 IKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGAAVdmctginfNPLYgmlDPRYSPPEELVM-----P 385
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187153  193 RTCYLAPERFNSKLYQDGKSNNGRlTKEMDIFSLGCVIAEI-FAEGRPIFNLsQLFKYKSNSY--DVNR 258
Cdd:PLN03224  386 QSCPRAPAPAMAALLSPFAWLYGR-PDLFDSYTAGVLLMQMcVPELRPVANI-RLFNTELRQYdnDLNR 452
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
124-287 8.48e-04

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


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 43.20  E-value: 8.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  124 LKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDFAAF----IKPVYLPEDnpgeflFYFDTSkrrtcYLA 198
Cdd:cd14013   122 IKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGQFkIIDLGAAadlrIGINYIPKE------FLLDPR-----YAP 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  199 PERF------------------NSKLYQDGKSNngrltkEMDIFSLGCVIAEI-FAEGRPIFNLSQL-FKYKSNSYDVNR 258
Cdd:cd14013   191 PEQYimstqtpsappapvaaalSPVLWQMNLPD------RFDMYSAGVILLQMaFPNLRSDSNLIAFnRQLKQCDYDLNA 264
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 342187153  259 -EFLMEEMNSTDLR--------------NLVLDMIQLDPSKRLS 287
Cdd:cd14013   265 wRMLVEPRASADLRegfeildlddgagwDLVTKLIRYKPRGRLS 308
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
83-294 9.17e-04

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 42.65  E-value: 9.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSL---RPYLQDIELKFIAfQLLNALKDIHNLNIVHGDIKTENILVTSW 158
Cdd:cd08219    58 PNIVAFKESFEADGHLYIVMEYCDGgDLMQKIKLqrgKLFPEDTILQWFV-QMCLGVQHIHEKRVLHRDIKSKNIFLTQN 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  159 NWCILTDF--AAFIKpvylpedNPGEF-LFYFDTSKrrtcYLAPErfnskLYQDGKSNNgrltkEMDIFSLGCVIAEIFA 235
Cdd:cd08219   137 GKVKLGDFgsARLLT-------SPGAYaCTYVGTPY----YVPPE-----IWENMPYNN-----KSDIWSLGCILYELCT 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 342187153  236 EGRPIFNLSQ---LFKYKSNSYDVnreflMEEMNSTDLRNLVLDMIQLDPSKRLSCDELLNK 294
Cdd:cd08219   196 LKHPFQANSWknlILKVCQGSYKP-----LPSHYSYELRSLIKQMFKRNPRSRPSATTILSR 252
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
127-155 9.70e-04

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 42.83  E-value: 9.70e-04
                          10        20
                  ....*....|....*....|....*....
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILV 155
Cdd:cd14016   101 LADQMISRLEYLHSKGYIHRDIKPENFLM 129
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
79-155 1.09e-03

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1b subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 42.61  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   79 LGQLPHVLNY-SKLIETNragYMIRQH-------LKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKT 150
Cdd:cd14139    56 LGHHPHVVRYySAWAEDD---HMIIQNeycnggsLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKP 132

                  ....*
gi 342187153  151 ENILV 155
Cdd:cd14139   133 SNIFI 137
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
99-166 1.09e-03

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 42.77  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187153   99 YMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF 166
Cdd:cd05582    73 YLILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDF 141
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
51-237 1.11e-03

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 42.42  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   51 IVIKVfIKPKDQYSLRPFLQRIraQSFKLGQLPHVLNYSKLIETNRAGYMIRQhlknnLYDRLSLRPYLQDIE------- 123
Cdd:cd05148    33 VAIKI-LKSDDLLKQQDFQKEV--QALKRLRHKHLISLFAVCSVGEPVYIITE-----LMEKGSLLAFLRSPEgqvlpva 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  124 -LKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIK-PVYLPEDnpgeflfyfdtSKRRTCYLAP 199
Cdd:cd05148   105 sLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFglARLIKeDVYLSSD-----------KKIPYKWTAP 173
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 342187153  200 ErfnsklyqdgKSNNGRLTKEMDIFSLGCVIAEIFAEG 237
Cdd:cd05148   174 E----------AASHGTFSTKSDVWSFGILLYEMFTYG 201
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
138-233 1.24e-03

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 42.75  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  138 IHNLNIVHGDIKTENILVTSWNWCILTDFAAFIK--PVYLPED--NPGEflfyFDTSKrrtcYLAPERFNSKL-YQDGKS 212
Cdd:cd14055   123 RPKIPIAHRDLKSSNILVKNDGTCVLADFGLALRldPSLSVDElaNSGQ----VGTAR----YMAPEALESRVnLEDLES 194
                          90       100
                  ....*....|....*....|.
gi 342187153  213 nngrlTKEMDIFSLGCVIAEI 233
Cdd:cd14055   195 -----FKQIDVYSMALVLWEM 210
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
100-171 1.48e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 42.91  E-value: 1.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342187153  100 MIRQHLKNNLY---DRLSLRPYLQDIelkFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIK 171
Cdd:PHA03207  163 MVMPKYKCDLFtyvDRSGPLPLEQAI---TIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACK 234
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
127-294 1.54e-03

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 42.11  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIH--NLNIVHGDIKTENILVTSWNWCILTDFAAFIKPVYLPEDN--PGEFLFYFDTSKRRTC--YLAPE 200
Cdd:cd14036   113 IFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDYSwsAQKRSLVEDEITRNTTpmYRTPE 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  201 RFNskLYqdgkSNNgRLTKEMDIFSLGCVIAEIFAEGRPifnlsqlFKYKSNSYDVNREFLMEEMNS--TDLRNLVLDMI 278
Cdd:cd14036   193 MID--LY----SNY-PIGEKQDIWALGCILYLLCFRKHP-------FEDGAKLRIINAKYTIPPNDTqyTVFHDLIRSTL 258
                         170
                  ....*....|....*.
gi 342187153  279 QLDPSKRLSCDELLNK 294
Cdd:cd14036   259 KVNPEERLSITEIVEQ 274
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
125-249 1.62e-03

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 42.69  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvyLPEDNPGEFLFYFDTSKrrtcYLAPERFNS 204
Cdd:cd05623   176 RFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLK---LMEDGTVQSSVAVGTPD----YISPEILQA 248
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 342187153  205 klYQDGKsnnGRLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKY 249
Cdd:cd05623   249 --MEDGK---GKYGPECDWWSLGVCMYEMLYGETPFYAESLVETY 288
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
132-293 1.68e-03

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 42.28  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  132 LNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKpvyLPEDNPgeflfyfdtsKRRTC-----YLAPERFNSKL 206
Cdd:cd06659   127 LQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQ---ISKDVP----------KRKSLvgtpyWMAPEVISRCP 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  207 YqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSKRL 286
Cdd:cd06659   194 Y----------GTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKASPVLRDFLERMLVRDPQERA 263

                  ....*..
gi 342187153  287 SCDELLN 293
Cdd:cd06659   264 TAQELLD 270
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
80-304 1.70e-03

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 41.98  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   80 GQLPHVLNYSKLIE-----TNRAGYMIRQHLKNNlydrlSLRPYLQDIE---LKF-----IAFQLLNALKDIHNLNIVHG 146
Cdd:cd05070    55 AQIMKKLKHDKLVQlyavvSEEPIYIVTEYMSKG-----SLLDFLKDGEgraLKLpnlvdMAAQVAAGMAYIERMNYIHR 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  147 DIKTENILVTSWNWCILTDFAAfikpVYLPEDNPGEFLfyfDTSKRRTCYLAPErfnSKLYqdgksnnGRLTKEMDIFSL 226
Cdd:cd05070   130 DLRSANILVGNGLICKIADFGL----ARLIEDNEYTAR---QGAKFPIKWTAPE---AALY-------GRFTIKSDVWSF 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  227 GCVIAEIFAEGR---PIFNLSQLFKyksnsyDVNREFLM--EEMNSTDLRNLVLDMIQLDPSKRLSCDELLNkyrgiFFP 301
Cdd:cd05070   193 GILLTELVTKGRvpyPGMNNREVLE------QVERGYRMpcPQDCPISLHELMIHCWKKDPEERPTFEYLQG-----FLE 261

                  ...
gi 342187153  302 DYF 304
Cdd:cd05070   262 DYF 264
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
20-293 1.75e-03

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 42.09  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   20 YIDVLEEvhyvsqLNSSRF--LKTCKALDPNGEIVIKvFIKPKDQYSLRPFLQR--IRAQSFKLGQL--PHVLNYSKLIE 93
Cdd:cd14105     6 FYDIGEE------LGSGQFavVKKCREKSTGLEYAAK-FIKKRRSKASRRGVSRedIEREVSILRQVlhPNIITLHDVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   94 TNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI----LTDF-- 166
Cdd:cd14105    79 NKTDVVLILELVAGgELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIprikLIDFgl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  167 AAFIKPvylpednPGEFLFYFDTSKrrtcYLAPERFNsklYQDgksnngrLTKEMDIFSLGcVIAEIFAEGRPIFNLSQL 246
Cdd:cd14105   159 AHKIED-------GNEFKNIFGTPE----FVAPEIVN---YEP-------LGLEADMWSIG-VITYILLSGASPFLGDTK 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 342187153  247 FKYKSNSYDVNREFLMEEMNSTDlrNLVLDMIQL----DPSKRLSCDELLN 293
Cdd:cd14105   217 QETLANITAVNYDFDDEYFSNTS--ELAKDFIRQllvkDPRKRMTIQESLR 265
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
130-285 1.77e-03

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 41.94  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikpvylpednpGEFLFYFDTSKRRTC----YLAPERFNSK 205
Cdd:cd08229   136 QLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL------------GRFFSSKTTAAHSLVgtpyYMSPERIHEN 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  206 LYqDGKSnngrltkemDIFSLGCVIAEIFAEGRPIF-NLSQLFKYKSNSYDVNREFLMEEMNSTDLRNLVLDMIQLDPSK 284
Cdd:cd08229   204 GY-NFKS---------DIWSLGCLLYEMAALQSPFYgDKMNLYSLCKKIEQCDYPPLPSDHYSEELRQLVNMCINPDPEK 273

                  .
gi 342187153  285 R 285
Cdd:cd08229   274 R 274
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
83-291 1.83e-03

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 42.17  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWN-- 159
Cdd:cd14180    61 PNIVALHEVLHDQYHTYLVMELLRGgELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdg 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  160 ---WCILTDFAAFIKPVYLPEDNPGEFLFyfdtskrrtcYLAPERFNSKLYQDGksnngrltkeMDIFSLGcVIAEIFAE 236
Cdd:cd14180   141 avlKVIDFGFARLRPQGSRPLQTPCFTLQ----------YAAPELFSNQGYDES----------CDLWSLG-VILYTMLS 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187153  237 GRPIFNLSQLFKYKSNSYDV-----NREFLME----EMNSTDLRNLVLDMIQLDPSKRLSCDEL 291
Cdd:cd14180   200 GQVPFQSKRGKMFHNHAADImhkikEGDFSLEgeawKGVSEEAKDLVRGLLTVDPAKRLKLSEL 263
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
83-230 1.94e-03

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: 41.77  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIE-TNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWC 161
Cdd:cd14164    60 PNIVQMFECIEvANGRLYIVMEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDRK 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  162 I-LTDFaAFIKPVylpeDNPGEFLFYFDTSKrrtCYLAPERFNSKLYQdgksnngrlTKEMDIFSLGCVI 230
Cdd:cd14164   140 IkIADF-GFARFV----EDYPELSTTFCGSR---AYTPPEVILGTPYD---------PKKYDVWSLGVVL 192
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
127-234 1.96e-03

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 41.71  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAafikpVYLPEDNPGEflfyfdTSKRR--TCYLAPERFNS 204
Cdd:cd14047   122 IFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFG-----LVTSLKNDGK------RTKSKgtLSYMSPEQISS 190
                          90       100       110
                  ....*....|....*....|....*....|
gi 342187153  205 KLYQdgksnngrltKEMDIFSLGCVIAEIF 234
Cdd:cd14047   191 QDYG----------KEVDIYALGLILFELL 210
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
130-266 2.01e-03

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 41.83  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  130 QLLNALKDI-------HNLNIVHGDIKTENILVTSWNWCILtdfAAFIKPVYLPEDNPGEFLFYFDTSKRrtcYLAPERF 202
Cdd:cd14039   100 QVLSLLSDIgsgiqylHENKIIHRDLKPENIVLQEINGKIV---HKIIDLGYAKDLDQGSLCTSFVGTLQ---YLAPELF 173
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 342187153  203 NSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKY--KSNSYDVNREFLMEEMN 266
Cdd:cd14039   174 ENKSY----------TVTVDYWSFGTMVFECIAGFRPFLHNLQPFTWheKIKKKDPKHIFAVEEMN 229
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
83-173 2.21e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 42.29  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI 162
Cdd:PHA03212  143 PSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVC 222
                          90
                  ....*....|.
gi 342187153  163 LTDFAAFIKPV 173
Cdd:PHA03212  223 LGDFGAACFPV 233
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
83-248 2.43e-03

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 41.36  E-value: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVT---SW 158
Cdd:cd14087    57 TNIIQLIEVFETKERVYMVMELATGgELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYhpgPD 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  159 NWCILTDFAAfikpVYLPEDNPGEFLfyfdtskRRTC----YLAPERFNSKLYqdgksnngrlTKEMDIFSLGcVIAEIF 234
Cdd:cd14087   137 SKIMITDFGL----ASTRKKGPNCLM-------KTTCgtpeYIAPEILLRKPY----------TQSVDMWAVG-VIAYIL 194
                         170
                  ....*....|....*..
gi 342187153  235 AEGRPIF---NLSQLFK 248
Cdd:cd14087   195 LSGTMPFdddNRTRLYR 211
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
83-236 2.81e-03

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 41.47  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   83 PHVLNYSKLIETNRAGYMIRQHLKNNlydrlSLRPYLQDIElKFIAFQLLNALKDI-------HNLNIVHGDIKTENILV 155
Cdd:cd14222    50 PNVLKFIGVLYKDKRLNLLTEFIEGG-----TLKDFLRADD-PFPWQQKVSFAKGIasgmaylHSMSIIHRDLNSHNCLI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  156 TSWNWCILTDF--AAFI---KPVYLPEDNPGE--FLFYFDTSKRRTC-----YLAPERFNSKLYQDgksnngrltkEMDI 223
Cdd:cd14222   124 KLDKTVVVADFglSRLIveeKKKPPPDKPTTKkrTLRKNDRKKRYTVvgnpyWMAPEMLNGKSYDE----------KVDI 193
                         170
                  ....*....|...
gi 342187153  224 FSLGCVIAEIFAE 236
Cdd:cd14222   194 FSFGIVLCEIIGQ 206
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
115-293 2.84e-03

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 41.14  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  115 LRPyLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF--AAFIkpvylpednpgeflfyFDTSKR 192
Cdd:cd06613    91 TGP-LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFgvSAQL----------------TATIAK 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  193 R-----TCY-LAPE--RFNSKLYQDGKSnngrltkemDIFSLGCVIAEIfAEGR-PIFNL---SQLFKYKSNSYDVNRef 260
Cdd:cd06613   154 RksfigTPYwMAPEvaAVERKGGYDGKC---------DIWALGITAIEL-AELQpPMFDLhpmRALFLIPKSNFDPPK-- 221
                         170       180       190
                  ....*....|....*....|....*....|....
gi 342187153  261 LMEEMN-STDLRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd06613   222 LKDKEKwSPDFHDFIKKCLTKNPKKRPTATKLLQ 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
79-155 3.46e-03

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 41.04  E-value: 3.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 342187153   79 LGQLPH--VLNYSKLIETNRAGYMIRQHLKNNLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILV 155
Cdd:cd14108    52 LAELDHksIVRFHDAFEKRRVVIIVTELCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLM 130
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
125-336 3.73e-03

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 41.40  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFaAFIKPVYLPEDNPGEFLfyfdtskRRTCYLAPErfns 204
Cdd:cd05586    99 KFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDF-GLSKADLTDNKTTNTFC-------GTTEYLAPE---- 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  205 kLYQDGKSnngrLTKEMDIFSLGCVIAEIFAEGRPIFNLSQLFKYKSNSYDVNRefLMEEMNSTDLRNLVLDMIQLDPSK 284
Cdd:cd05586   167 -VLLDEKG----YTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVR--FPKDVLSDEGRSFVKGLLNRNPKH 239
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153  285 RL-SCDELLNKYRGIFFPDYFYTFIYDY-----FRNLVTMTTSTPISDNTCTNSTLED 336
Cdd:cd05586   240 RLgAHDDAVELKEHPFFADIDWDLLSKKkitppFKPIVDSDTDVSNFDPEFTNASLLN 297
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
118-238 4.43e-03

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 40.83  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  118 YLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAfikpVYLPEDNpgEFLFYfDTSKRRTCYL 197
Cdd:cd05069   104 YLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGL----ARLIEDN--EYTAR-QGAKFPIKWT 176
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 342187153  198 APErfnSKLYqdgksnnGRLTKEMDIFSLGCVIAEIFAEGR 238
Cdd:cd05069   177 APE---AALY-------GRFTIKSDVWSFGILLTELVTKGR 207
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
106-234 4.94e-03

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 40.79  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KNNLY---------DRLSLRPYLQDI----ELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKp 172
Cdd:cd05597    73 ENYLYlvmdyycggDLLTLLSKFEDRlpeeMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLK- 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 342187153  173 vyLPEDNpgeflfyfdTSKRRTC-----YLAPERFnsKLYQDGKsnnGRLTKEMDIFSLGCVIAEIF 234
Cdd:cd05597   152 --LREDG---------TVQSSVAvgtpdYISPEIL--QAMEDGK---GRYGPECDWWSLGVCMYEML 202
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
125-241 5.08e-03

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 40.73  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  125 KFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCILTDF---AAFIK----PVYLPEDNPGEF----LFYFDTSKRR 193
Cdd:cd05573   104 RFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFglcTKMNKsgdrESYLNDSVNTLFqdnvLARRRPHKQR 183
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 342187153  194 TC----------YLAPERFNSKLYqdgksnngrlTKEMDIFSLGCVIAEIFAeGRPIF 241
Cdd:cd05573   184 RVraysavgtpdYIAPEVLRGTGY----------GPECDWWSLGVILYEMLY-GFPPF 230
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
99-233 5.58e-03

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 40.54  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   99 YMIRQ-HLKNNLYDRLSLRPYLQDIELKfIAFQLLNALKDIHNL--------NIVHGDIKTENILVTSWNWCILTDFAAF 169
Cdd:cd14144    69 YLITDyHENGSLYDFLRGNTLDTQSMLK-LAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILVKKNGTCCIADLGLA 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 342187153  170 IKpvYLPEDNpgEFLFYFDTSKRRTCYLAPERFNSKLyqdgKSNNGRLTKEMDIFSLGCVIAEI 233
Cdd:cd14144   148 VK--FISETN--EVDLPPNTRVGTKRYMAPEVLDESL----NRNHFDAYKMADMYSFGLVLWEI 203
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
134-166 6.74e-03

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 40.08  E-value: 6.74e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 342187153  134 ALKDIHNLNIVHGDIKTENILVTSWNWCILTDF 166
Cdd:cd05609   112 ALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDF 144
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
32-292 6.74e-03

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


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 39.99  E-value: 6.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153   32 QLNSSRF--LKTCKALDPNGEIVIKvFIKPKDQYSLRPFLQRIRAQS----FKLGQLPHVLNYSKLIETNRAGYMIRQHL 105
Cdd:cd14195    12 ELGSGQFaiVRKCREKGTGKEYAAK-FIKKRRLSSSRRGVSREEIERevniLREIQHPNIITLHDIFENKTDVVLILELV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  106 KN-NLYDRLSLRPYLQDIELKFIAFQLLNALKDIHNLNIVHGDIKTENILVTSWN----WCILTDFAAFIKPvylpeDNP 180
Cdd:cd14195    91 SGgELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHKI-----EAG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  181 GEFLFYFDTSKrrtcYLAPERFNsklYQDgksnngrLTKEMDIFSLGCVIAEIFAEGRPIFNLSQ---LFKYKSNSYDVN 257
Cdd:cd14195   166 NEFKNIFGTPE----FVAPEIVN---YEP-------LGLEADMWSIGVITYILLSGASPFLGETKqetLTNISAVNYDFD 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 342187153  258 REFLmeeMNSTDL-RNLVLDMIQLDPSKRLSCDELL 292
Cdd:cd14195   232 EEYF---SNTSELaKDFIRRLLVKDPKKRMTIAQSL 264
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
128-293 7.11e-03

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 40.28  E-value: 7.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  128 AFQLLNALKDIHNLNIVHGDIKTENILVTSWNWCI-LTDF--AAFIKpvylpEDNPGEFL---FYfdtskRrtcylAPER 201
Cdd:cd14135   111 AQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLkLCDFgsASDIG-----ENEITPYLvsrFY-----R-----APEI 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  202 FNSKLYQDGksnngrltkeMDIFSLGCVIAEIFAeGRPIF------NLSQLF---------------KYKSNSYDVN--- 257
Cdd:cd14135   176 ILGLPYDYP----------IDMWSVGCTLYELYT-GKILFpgktnnHMLKLMmdlkgkfpkkmlrkgQFKDQHFDENlnf 244
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  258 --------------------------REFLMEEMNSTD--------LRNLVLDMIQLDPSKRLSCDELLN 293
Cdd:cd14135   245 iyrevdkvtkkevrrvmsdikptkdlKTLLIGKQRLPDedrkkllqLKDLLDKCLMLDPEKRITPNEALQ 314
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
127-155 7.50e-03

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


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 40.34  E-value: 7.50e-03
                          10        20
                  ....*....|....*....|....*....
gi 342187153  127 IAFQLLNALKDIHNLNIVHGDIKTENILV 155
Cdd:cd14015   132 LALRILDVLEYIHENGYVHADIKASNLLL 160
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
137-234 8.45e-03

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 40.04  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342187153  137 DIHNLNIVHGDIKTENILVTSWNWCILTDFAAFIKP----VYLPEDNPGEFLFYFDTSKRRtcYLAPERFnsklyqDGKS 212
Cdd:cd14054   117 DQYKPAIAHRDLNSRNVLVKADGSCVICDFGLAMVLrgssLVRGRPGAAENASISEVGTLR--YMAPEVL------EGAV 188
                          90       100
                  ....*....|....*....|....*
gi 342187153  213 N---NGRLTKEMDIFSLGCVIAEIF 234
Cdd:cd14054   189 NlrdCESALKQVDVYALGLVLWEIA 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH