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Conserved domains on  [gi|1113820495|ref|NP_001334650|]
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dual specificity tyrosine-phosphorylation-regulated kinase 1A isoform 2 [Homo sapiens]

Protein Classification

DYRK family dual specificity protein kinase( domain architecture ID 10197785)

DYRK family dual specificity protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates; similar to dual specificity tyrosine-phosphorylation-regulated kinases

CATH:  1.10.510.10
EC:  2.7.12.1
Gene Ontology:  GO:0004712|GO:0006468|GO:0005524
PubMed:  21048044|19614568
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
139-475 0e+00

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


:

Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 768.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRH 218
Cdd:cd14226     4 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYYIVRLKRH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVD 298
Cdd:cd14226    84 FMFRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPELSIIHCDLKPENILLCNPKRSAIKIID 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ 378
Cdd:cd14226   164 FGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPPVHMLDQ 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 379 APKARKFFEKLPDGTWNLKKTKDGKrEYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTR 458
Cdd:cd14226   244 APKARKFFEKLPDGTYYLKKTKDGK-KYKPPGSRKLHEILGVETGGPGGRRAGEPGHTVEDYLKFKDLILRMLDYDPKTR 322
                         330
                  ....*....|....*..
gi 1113820495 459 IQPYYALQHSFFKKTAD 475
Cdd:cd14226   323 ITPAEALQHSFFKRTAD 339
 
Name Accession Description Interval E-value
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
139-475 0e+00

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 768.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRH 218
Cdd:cd14226     4 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYYIVRLKRH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVD 298
Cdd:cd14226    84 FMFRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPELSIIHCDLKPENILLCNPKRSAIKIID 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ 378
Cdd:cd14226   164 FGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPPVHMLDQ 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 379 APKARKFFEKLPDGTWNLKKTKDGKrEYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTR 458
Cdd:cd14226   244 APKARKFFEKLPDGTYYLKKTKDGK-KYKPPGSRKLHEILGVETGGPGGRRAGEPGHTVEDYLKFKDLILRMLDYDPKTR 322
                         330
                  ....*....|....*..
gi 1113820495 459 IQPYYALQHSFFKKTAD 475
Cdd:cd14226   323 ITPAEALQHSFFKRTAD 339
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
150-470 6.56e-74

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 240.12  E-value: 6.56e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA--FLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLCL 227
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkkDRERILREIKILKKLK-HP-----NIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  228 VFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQL- 305
Cdd:smart00220  75 VMEYCEGgDLFDLLKKR--GRLSEDEARFYLRQILSALEYLH--SKGIVHRDLKPENILLDEDGH--VKLADFGLARQLd 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  306 -GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVevlgippahildqapkaRK 384
Cdd:smart00220 149 pGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI-----------------GK 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  385 FFEKLPDGTWNLKKTkdgkreykppgtrklhnilgvetggpggrragesghtvadylkFKDLILRMLDYDPKTRIQPYYA 464
Cdd:smart00220 212 PKPPFPPPEWDISPE-------------------------------------------AKDLIRKLLVKDPEKRLTAEEA 248

                   ....*.
gi 1113820495  465 LQHSFF 470
Cdd:smart00220 249 LQHPFF 254
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
150-475 7.44e-40

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 152.88  E-value: 7.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNkhdtemkyyIVHLKRHFM---FRNH-- 224
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHIN---------IIFLKDYYYtecFKKNek 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 ---LCLVFEMLSYNLYDLLR--NTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENiLLCNPKRSAIKIVDF 299
Cdd:PTZ00036  139 nifLNVVMEFIPQTVHKYMKhyARNNHALPLFLVKLYSYQLCRALAYIHSK--FICHRDLKPQN-LLIDPNTHTLKLCDF 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 GSSCQL--GQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAhil 376
Cdd:PTZ00036  216 GSAKNLlaGQRSVSYICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTPTE--- 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 DQAPKARKFFE--KLPDgtwnlKKTKDGKREYkPPGTRKlhnilgvetggpggrragesghtvaDYLKFkdlILRMLDYD 454
Cdd:PTZ00036  293 DQLKEMNPNYAdiKFPD-----VKPKDLKKVF-PKGTPD-------------------------DAINF---ISQFLKYE 338
                         330       340
                  ....*....|....*....|.
gi 1113820495 455 PKTRIQPYYALQHSFFKKTAD 475
Cdd:PTZ00036  339 PLKRLNPIEALADPFFDDLRD 359
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
148-382 7.73e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 138.99  E-value: 7.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK----NKKAFLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRN 223
Cdd:COG0515     7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARERFRREARALARLN-HP-----NIVRVYDVGEEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLS-YNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGSS 302
Cdd:COG0515    81 RPYLVMEYVEgESLADLLRRR--GPLPPAEALRILAQLAEALAAAH--AAGIVHRDIKPANILLTPDGR--VKLIDFGIA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQLGQ----RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ 378
Cdd:COG0515   155 RALGGatltQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPD 234

                  ....
gi 1113820495 379 APKA 382
Cdd:COG0515   235 LPPA 238
Pkinase pfam00069
Protein kinase domain;
150-470 7.04e-32

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 123.51  E-value: 7.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA---FLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLC 226
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLN-HP-----NIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALlflatpelsiihcdlkpENillcnpkrsaikivdfgsscql 305
Cdd:pfam00069  75 LVLEYVEGgSLFDLLSEK--GAFSEREAKFIMKQILEGL-----------------ES---------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNkivevlgippaHILDQAPKARKF 385
Cdd:pfam00069 114 GSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYE-----------LIIDQPYAFPEL 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 386 FEKLPDgtwnlkktkdgkreykppgtrklhnilgvetggpggrragesghtvadylKFKDLILRMLDYDPKTRIQPYYAL 465
Cdd:pfam00069 183 PSNLSE--------------------------------------------------EAKDLLKKLLKKDPSKRLTATQAL 212

                  ....*
gi 1113820495 466 QHSFF 470
Cdd:pfam00069 213 QHPWF 217
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
148-354 1.65e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.43  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK----NKKAFL----NQAQIEVRLlelmnKH-------DT---EMK 209
Cdd:NF033483    7 GRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRpdlaRDPEFVarfrREAQSAASL-----SHpnivsvyDVgedGGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 210 YYIVhlkrhfMfrnhlclvfEmlsY----NLYDLLRNtnfRGVsLNLTR--KFAQQMCTALlflatpELS----IIHCDL 279
Cdd:NF033483   82 PYIV------M---------E---YvdgrTLKDYIRE---HGP-LSPEEavEIMIQILSAL------EHAhrngIVHRDI 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 280 KPENILLcnPKRSAIKIVDFG--------SSCQ----LGqriyqyiqSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:NF033483  134 KPQNILI--TKDGRVKVTDFGiaralsstTMTQtnsvLG--------TVHYLSPEQARGGTVDARSDIYSLGIVLYEMLT 203

                  ....*..
gi 1113820495 348 GEPLFSG 354
Cdd:NF033483  204 GRPPFDG 210
 
Name Accession Description Interval E-value
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
139-475 0e+00

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 768.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRH 218
Cdd:cd14226     4 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTENKYYIVRLKRH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVD 298
Cdd:cd14226    84 FMFRNHLCLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTPELSIIHCDLKPENILLCNPKRSAIKIID 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ 378
Cdd:cd14226   164 FGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGMPPVHMLDQ 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 379 APKARKFFEKLPDGTWNLKKTKDGKrEYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTR 458
Cdd:cd14226   244 APKARKFFEKLPDGTYYLKKTKDGK-KYKPPGSRKLHEILGVETGGPGGRRAGEPGHTVEDYLKFKDLILRMLDYDPKTR 322
                         330
                  ....*....|....*..
gi 1113820495 459 IQPYYALQHSFFKKTAD 475
Cdd:cd14226   323 ITPAEALQHSFFKRTAD 339
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
139-470 9.34e-178

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: 510.55  E-value: 9.34e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRH 218
Cdd:cd14210     4 KVVLGDHIAYRYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQALVEVKILKHLNDNDPDDKHNIVRYKDS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVD 298
Cdd:cd14210    84 FIFRGHLCIVFELLSINLYELLKSNNFQGLSLSLIRKFAKQILQALQFLH--KLNIIHCDLKPENILLKQPSKSSIKVID 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ 378
Cdd:cd14210   162 FGSSCFEGEKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGVPPKSLIDK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 379 APKARKFFeklpDGTWNLKKTKDGKREYKPPGTRKLHNILGVetggpggrragesghtvaDYLKFKDLILRMLDYDPKTR 458
Cdd:cd14210   242 ASRRKKFF----DSNGKPRPTTNSKGKKRRPGSKSLAQVLKC------------------DDPSFLDFLKKCLRWDPSER 299
                         330
                  ....*....|..
gi 1113820495 459 IQPYYALQHSFF 470
Cdd:cd14210   300 MTPEEALQHPWI 311
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
150-470 8.55e-150

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: 437.47  E-value: 8.55e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVF 229
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEIRLLELLNKKDKADKYHIVRLKDVFYFKNHLCIVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRI 309
Cdd:cd14133    81 ELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLH--SLGLIHCDLKPENILLASYSRCQIKIIDFGSSCFLTQRL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 310 YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPkarkffekl 389
Cdd:cd14133   159 YSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGK--------- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 390 pdgtwnlkktkdgkreykppgtrklhnilgvetggpggrragesghtvADYLKFKDLILRMLDYDPKTRIQPYYALQHSF 469
Cdd:cd14133   230 ------------------------------------------------ADDELFVDFLKKLLEIDPKERPTASQALSHPW 261

                  .
gi 1113820495 470 F 470
Cdd:cd14133   262 L 262
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
150-470 5.55e-123

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: 371.20  E-value: 5.55e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMN-KHDTEMKYYIVHLKRHFMFRNHLCLV 228
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAYFRQAMLEIAILTLLNtKYDPEDKHHIVRLLDHFMHHGHLCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQR 308
Cdd:cd14212    81 FELLGVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVLK--DARIIHCDLKPENILLVNLDSPEIKLIDFGSACFENYT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 309 IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEK 388
Cdd:cd14212   159 LYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPPDWMLEKGKNTNKFFKK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 389 LPDG----TWNLKKTKDGKREYK---PPGTR-----KLHNIlgVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPK 456
Cdd:cd14212   239 VAKSggrsTYRLKTPEEFEAENNcklEPGKRyfkykTLEDI--IMNYPMKKSKKEQIDKEMETRLAFIDFLKGLLEYDPK 316
                         330
                  ....*....|....
gi 1113820495 457 TRIQPYYALQHSFF 470
Cdd:cd14212   317 KRWTPDQALNHPFI 330
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
149-470 8.43e-121

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 365.95  E-value: 8.43e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLV 228
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKILDALRRKDRDNSHNVIHMKEYFYFRNHLCIT 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQM--CTALLFLAtpelSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLG 306
Cdd:cd14225   124 FELLGMNLYELIKKNNFQGFSLSLIRRFAISLlqCLRLLYRE----RIIHCDLKPENILLRQRGQSSIKVIDFGSSCYEH 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 307 QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFF 386
Cdd:cd14225   200 QRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLPPPELIENAQRRRLFF 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 387 EKlPDGTWNLKKTKDGKREykpPGTRKLHNILGVEtggpggrragesghtvaDYLkFKDLILRMLDYDPKTRIQPYYALQ 466
Cdd:cd14225   280 DS-KGNPRCITNSKGKKRR---PNSKDLASALKTS-----------------DPL-FLDFIRRCLEWDPSKRMTPDEALQ 337

                  ....
gi 1113820495 467 HSFF 470
Cdd:cd14225   338 HEWI 341
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
149-467 4.03e-103

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 321.70  E-value: 4.03e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLV 228
Cdd:cd14224    66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEEIRILEHLKKQDKDNTMNVIHMLESFTFRNHICMT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQR 308
Cdd:cd14224   146 FELLSMNLYELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNK--IIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQR 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 309 IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEK 388
Cdd:cd14224   224 IYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQKLLETSKRAKNFISS 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 389 -----------LPDGTWNLK--KTKDGKREyKPPGTRKLHNIL-GVEtggpggrragesghtvaDYLkFKDLILRMLDYD 454
Cdd:cd14224   304 kgypryctvttLPDGSVVLNggRSRRGKMR-GPPGSKDWVTALkGCD-----------------DPL-FLDFLKRCLEWD 364
                         330
                  ....*....|...
gi 1113820495 455 PKTRIQPYYALQH 467
Cdd:cd14224   365 PAARMTPSQALRH 377
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
150-470 6.20e-102

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: 313.40  E-value: 6.20e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHdtEMKYYIVHLKRHFMFR--NHLCL 227
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKHLNDV--EGHPNIVKLLDVFEHRggNHLCL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRnTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcNPKRSAIKIVDFGSSCQLGQ 307
Cdd:cd05118    79 VFELMGMNLYELIK-DYPRGLPLDLIKSYLYQLLQALDFLH--SNGIIHRDLKPENILI-NLELGQLKLADFGLARSFTS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIY-QYIQSRFYRSPEVLLGM-PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahildqapkarkf 385
Cdd:cd05118   155 PPYtPYVATRWYRAPEVLLGAkPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTP-------------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 386 feklpdgtwnlkktkdgkreykppgtrklhnilgvetggpggrragesghtvadylKFKDLILRMLDYDPKTRIQPYYAL 465
Cdd:cd05118   221 --------------------------------------------------------EALDLLSKMLKYDPAKRITASQAL 244

                  ....*
gi 1113820495 466 QHSFF 470
Cdd:cd05118   245 AHPYF 249
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
150-469 3.90e-90

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 285.88  E-value: 3.90e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEmKYYIVHLKRHFMFRNHLCLVF 229
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENAD-EFNFVRAYECFQHKNHTCLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSA--IKIVDFGSSCQLGQ 307
Cdd:cd14211    80 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLK--SLGLIHADLKPENIMLVDPVRQPyrVKVIDFGSASHVSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIYQ-YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFF 386
Cdd:cd14211   158 AVCStYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAEHLLNAATKTSRFF 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 387 EKLPDGT---WNLKKTKDGKREY--KPPGTRK-----LHNILGVetGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPK 456
Cdd:cd14211   238 NRDPDSPyplWRLKTPEEHEAETgiKSKEARKyifncLDDMAQV--NGPSDLEGSELLAEKADRREFIDLLKRMLTIDQE 315
                         330
                  ....*....|...
gi 1113820495 457 TRIQPYYALQHSF 469
Cdd:cd14211   316 RRITPGEALNHPF 328
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
139-470 1.06e-79

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: 258.26  E-value: 1.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRH 218
Cdd:cd14134     3 IYKPGDLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAAKIEIDVLETLAEKDPNGKSHCVQLRDW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCN---------- 288
Cdd:cd14134    83 FDYRGHMCIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLH--DLKLTHTDLKPENILLVDsdyvkvynpk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 289 -------PKRSAIKIVDFGSSCqlgqriYQY------IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGA 355
Cdd:cd14134   161 kkrqirvPKSTDIKLIDFGSAT------FDDeyhssiVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTH 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 356 NEVDQMNKIVEVLGIPPAHILDQAPKARKFFE----KLpdgTWNlKKTKDGK--REYKPPGTRKLHnilgvetggpggrr 429
Cdd:cd14134   235 DNLEHLAMMERILGPLPKRMIRRAKKGAKYFYfyhgRL---DWP-EGSSSGRsiKRVCKPLKRLML-------------- 296
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1113820495 430 agesgHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14134   297 -----LVDPEHRLLFDLIRKMLEYDPSKRITAKEALKHPFF 332
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
149-470 2.25e-77

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: 251.76  E-value: 2.25e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRV-EQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCL 227
Cdd:cd14135     1 RYRVYGYLGKGVFSNVVRARDLArGNQEVAIKIIRNNELMHKAGLKELEILKKLNDADPDDKKHCIRLLRHFEHKNHLCL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRNTNfRGVSLNLT--RKFAQQMCTALLFLAtpELSIIHCDLKPENILLcNPKRSAIKIVDFGSSCQL 305
Cdd:cd14135    81 VFESLSMNLREVLKKYG-KNVGLNIKavRSYAQQLFLALKHLK--KCNILHADIKPDNILV-NEKKNTLKLCDFGSASDI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 G-QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEvDQMNK-IVEVLGIPPAHILdqapKAR 383
Cdd:cd14135   157 GeNEITPYLVSRFYRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTN-NHMLKlMMDLKGKFPKKML----RKG 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 384 KFFEKLPDGTWNLKKT---KDGKREY-------KPpgTRKLHNILGvetggpGGRRAGESGHTVAdyLKFKDLILRMLDY 453
Cdd:cd14135   232 QFKDQHFDENLNFIYRevdKVTKKEVrrvmsdiKP--TKDLKTLLI------GKQRLPDEDRKKL--LQLKDLLDKCLML 301
                         330
                  ....*....|....*..
gi 1113820495 454 DPKTRIQPYYALQHSFF 470
Cdd:cd14135   302 DPEKRITPNEALQHPFI 318
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
150-469 2.09e-75

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 247.25  E-value: 2.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEmKYYIVHLKRHFMFRNHLCLVF 229
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENAD-EFNFVRAYECFQHRNHTCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSA--IKIVDFGSSCQLGQ 307
Cdd:cd14229    81 EMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKS--LGLIHADLKPENIMLVDPVRQPyrVKVIDFGSASHVSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RI-YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFF 386
Cdd:cd14229   159 TVcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNVGTKTSRFF 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 387 EKLPDG---TWNLKKTKDGKRE--YKPPGTRK-----LHNILGVE--TGGPGGRRAGESghtvADYLKFKDLILRMLDYD 454
Cdd:cd14229   239 CRETDApysSWRLKTLEEHEAEtgMKSKEARKyifnsLDDIAHVNmvMDLEGSDLLAEK----ADRREFVALLKKMLLID 314
                         330
                  ....*....|....*
gi 1113820495 455 PKTRIQPYYALQHSF 469
Cdd:cd14229   315 ADLRITPADTLSHPF 329
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
150-470 6.56e-74

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 240.12  E-value: 6.56e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA--FLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLCL 227
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIkkDRERILREIKILKKLK-HP-----NIVRLYDVFEDEDKLYL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  228 VFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQL- 305
Cdd:smart00220  75 VMEYCEGgDLFDLLKKR--GRLSEDEARFYLRQILSALEYLH--SKGIVHRDLKPENILLDEDGH--VKLADFGLARQLd 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  306 -GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVevlgippahildqapkaRK 384
Cdd:smart00220 149 pGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI-----------------GK 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  385 FFEKLPDGTWNLKKTkdgkreykppgtrklhnilgvetggpggrragesghtvadylkFKDLILRMLDYDPKTRIQPYYA 464
Cdd:smart00220 212 PKPPFPPPEWDISPE-------------------------------------------AKDLIRKLLVKDPEKRLTAEEA 248

                   ....*.
gi 1113820495  465 LQHSFF 470
Cdd:smart00220 249 LQHPFF 254
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
140-470 3.12e-71

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 235.55  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 140 VKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDT--EMKYYIVHLKR 217
Cdd:cd14136     2 VKIGEVYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAALDEIKLLKCVREADPkdPGREHVVQLLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFR----NHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLCNPKrSA 293
Cdd:cd14136    82 DFKHTgpngTHVCMVFEVLGPNLLKLIKRYNYRGIPLPLVKKIARQVLQGLDYLHT-KCGIIHTDIKPENVLLCISK-IE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 IKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF---SGAN---EVDQMNKIVEV 367
Cdd:cd14136   160 VKIADLGNACWTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFdphSGEDysrDEDHLALIIEL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 368 LGIPPAHILDQAPKARKFFeklpdgtwnlkkTKDGK----REYKPpgtRKLHNILgvetggpggRRAGESGHTVADylKF 443
Cdd:cd14136   240 LGRIPRSIILSGKYSREFF------------NRKGElrhiSKLKP---WPLEDVL---------VEKYKWSKEEAK--EF 293
                         330       340
                  ....*....|....*....|....*..
gi 1113820495 444 KDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14136   294 ASFLLPMLEYDPEKRATAAQCLQHPWL 320
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
148-473 2.94e-68

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 228.82  E-value: 2.94e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEmKYYIVHLKRHFMFRNHLCL 227
Cdd:cd14227    15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESAD-DYNFVRAYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSA--IKIVDFGSSCQL 305
Cdd:cd14227    94 VFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKS--LGLIHADLKPENIMLVDPSRQPyrVKVIDFGSASHV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRI-YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARK 384
Cdd:cd14227   172 SKAVcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 385 FFEKLPDGT---WNLKKTKDGKRE--YKPPGTRK-LHNIL------GVETGGPGGRRAGESghtvADYLKFKDLILRMLD 452
Cdd:cd14227   252 FFNRDTDSPyplWRLKTPEDHEAEtgIKSKEARKyIFNCLddmaqvNMTTDLEGSDMLVEK----ADRREFIDLLKKMLT 327
                         330       340
                  ....*....|....*....|.
gi 1113820495 453 YDPKTRIQPYYALQHSFFKKT 473
Cdd:cd14227   328 IDADKRITPIETLNHPFVTMT 348
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
148-473 6.74e-68

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 228.05  E-value: 6.74e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEmKYYIVHLKRHFMFRNHLCL 227
Cdd:cd14228    15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENAD-EYNFVRSYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSA--IKIVDFGSSCQL 305
Cdd:cd14228    94 VFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKS--LGLIHADLKPENIMLVDPVRQPyrVKVIDFGSASHV 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRI-YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARK 384
Cdd:cd14228   172 SKAVcSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTSR 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 385 FFEKLPD---GTWNLKKTKDGKRE--YKPPGTRK-LHNIL------GVETGGPGGRRAGESghtvADYLKFKDLILRMLD 452
Cdd:cd14228   252 FFNRDPNlgyPLWRLKTPEEHELEtgIKSKEARKyIFNCLddmaqvNMSTDLEGTDMLAEK----ADRREYIDLLKKMLT 327
                         330       340
                  ....*....|....*....|.
gi 1113820495 453 YDPKTRIQPYYALQHSFFKKT 473
Cdd:cd14228   328 IDADKRITPLKTLNHPFVTMT 348
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
149-471 1.13e-65

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: 219.68  E-value: 1.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNqaqievRLLELMN--KHDtemkyYIVHLKRHFMFR---- 222
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKN------RELQIMRrlKHP-----NIVKLKYFFYSSgekk 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 --NHLCLVFEMLSYNLYDLLR--NTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcNPKRSAIKIVD 298
Cdd:cd14137    74 deVYLNLVMEYMPETLYRVIRhySKNKQTIPIIYVKLYSYQLFRGLAYLHS--LGICHRDIKPQNLLV-DPETGVLKLCD 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQL--GQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIP-PAH 374
Cdd:cd14137   151 FGSAKRLvpGEPNVSYICSRYYRAPELIFGATdYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPtREQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 375 ILDQAPKARKFfeKLPDgtwnlkktkdgkreYKPPGTRKLHNilgvetggpggrragesGHTVADylkFKDLILRMLDYD 454
Cdd:cd14137   231 IKAMNPNYTEF--KFPQ--------------IKPHPWEKVFP-----------------KRTPPD---AIDLLSKILVYN 274
                         330
                  ....*....|....*..
gi 1113820495 455 PKTRIQPYYALQHSFFK 471
Cdd:cd14137   275 PSKRLTALEALAHPFFD 291
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
150-470 9.80e-58

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: 198.09  E-value: 9.80e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA---FLNQAQIEVRLL-ELmnKHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEeegIPSTALREISLLkEL--KHP-----NIVKLLDVIHTENKL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNtNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSScql 305
Cdd:cd07829    74 YLVFEYCDQDLKKYLDK-RPGPLPPNLIKSIMYQLLRGLAYCHSH--RILHRDLKPQNLLI--NRDGVLKLADFGLA--- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 gqRIYQY--------IQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahil 376
Cdd:cd07829   146 --RAFGIplrtytheVVTLWYRAPEILLGSKhYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTP----- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 dqAPKARKFFEKLPDGTWNLKktkdgKREYKPpgtrkLHNILGVEtgGPGGRragesghtvadylkfkDLILRMLDYDPK 456
Cdd:cd07829   219 --TEESWPGVTKLPDYKPTFP-----KWPKND-----LEKVLPRL--DPEGI----------------DLLSKMLQYNPA 268
                         330
                  ....*....|....
gi 1113820495 457 TRIQPYYALQHSFF 470
Cdd:cd07829   269 KRISAKEALKHPYF 282
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
139-470 6.42e-54

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


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 189.06  E-value: 6.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVE-QEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKR 217
Cdd:cd14214     4 VCRIGDWLQERYEIVGDLGEGTFGKVVECLDHARgKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSiiHCDLKPENILLCNP-------- 289
Cdd:cd14214    84 WFNFHGHMCIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLT--HTDLKPENILFVNSefdtlyne 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 290 ---------KRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd14214   162 sksceeksvKNTSIRVADFGSATFDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREH 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 361 MNKIVEVLGIPPAHILDQAPKARKFFEKlpDGTWNlKKTKDG---KREYKPPGTRKLHNILgvetggpggrragesghtv 437
Cdd:cd14214   242 LVMMEKILGPIPSHMIHRTRKQKYFYKG--SLVWD-ENSSDGryvSENCKPLMSYMLGDSL------------------- 299
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1113820495 438 aDYLKFKDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14214   300 -EHTQLFDLLRRMLEFDPALRITLKEALLHPFF 331
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
150-470 1.21e-51

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: 181.19  E-value: 1.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAF--------LNqaqiEVRLLELMNKHDTemkyyIVHLKRHFMF 221
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIK--KMKKKFysweecmnLR----EVKSLRKLNEHPN-----IVKLKEVFRE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRsaIKIVDFGs 301
Cdd:cd07830    70 NDELYFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHK--HGFFHRDLKPENLLVSGPEV--VKIADFG- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 scqLGQRI-----Y-QYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAH 374
Cdd:cd07830   145 ---LAREIrsrppYtDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQ 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 375 ILDQAPK-ARKFFEKLPdgtwnlkktkdgkrEYKPPgtrKLHNILgvetggPggrragesgHTVADYLkfkDLILRMLDY 453
Cdd:cd07830   222 DWPEGYKlASKLGFRFP--------------QFAPT---SLHQLI------P---------NASPEAI---DLIKDMLRW 266
                         330
                  ....*....|....*..
gi 1113820495 454 DPKTRIQPYYALQHSFF 470
Cdd:cd07830   267 DPKKRPTASQALQHPYF 283
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
149-476 1.57e-51

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: 182.34  E-value: 1.57e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNkkAFlnQAQI-------EVRLLELMnKHDtemkyYIVHLKRhfMF 221
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISN--VF--DDLIdakrilrEIKILRHL-KHE-----NIIGLLD--IL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 R-------NHLCLVFEMLSYNLYDLLRNtnfrgvSLNLTRKFAQ----QMCTALLFL--AtpelSIIHCDLKPENILL-- 286
Cdd:cd07834    69 RppspeefNDVYIVTELMETDLHKVIKS------PQPLTDDHIQyflyQILRGLKYLhsA----GVIHRDLKPSNILVns 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 287 -CNpkrsaIKIVDFG----SSCQLGQRIY-QYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVD 359
Cdd:cd07834   139 nCD-----LKICDFGlargVDPDEDKGFLtEYVVTRWYRAPELLLSSKkYTKAIDIWSVGCIFAELLTRKPLFPGRDYID 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 360 QMNKIVEVLGIPPAHILDQ--APKARKFFEKLPdgtwnlkktkdgKREyKPPGTRKLHNIlgvetggpggrragesghtv 437
Cdd:cd07834   214 QLNLIVEVLGTPSEEDLKFisSEKARNYLKSLP------------KKP-KKPLSEVFPGA-------------------- 260
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1113820495 438 adYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADE 476
Cdd:cd07834   261 --SPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDP 297
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
148-374 2.90e-49

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: 174.81  E-value: 2.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK---IIKNKKAFLNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNH 224
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkfkESEDDEDVKKTALREVKVLRQL-RHEN-----IVNLKEAFRRKGR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYNLYDLLrNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFG---- 300
Cdd:cd07833    75 LYLVFEYVERTLLELL-EASPGGLPPDAVRSYIWQLLQAIAYCH--SHNIIHRDIKPENILV--SESGVLKLCDFGfara 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 301 SSCQLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLG-IPPAH 374
Cdd:cd07833   150 LTARPASPLTDYVATRWYRAPELLVGdTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGpLPPSH 225
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
139-470 7.89e-49

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 175.21  E-value: 7.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYD-RVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKR 217
Cdd:cd14215     3 IYRSGDWLQERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPENKNLCVQMFD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSiiHCDLKPENILLCNP-------- 289
Cdd:cd14215    83 WFDYHGHMCISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLT--HTDLKPENILFVNSdyeltynl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 290 ---------KRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd14215   161 ekkrdersvKSTAIRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 361 MNKIVEVLGIPPAHILDQAPKARKFFEKLPDgtWNlKKTKDGKreYKPPGTRKLHNILGVETggpggrragESGHtvady 440
Cdd:cd14215   241 LAMMERILGPIPSRMIRKTRKQKYFYHGRLD--WD-ENTSAGR--YVRENCKPLRRYLTSEA---------EEHH----- 301
                         330       340       350
                  ....*....|....*....|....*....|
gi 1113820495 441 lKFKDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14215   302 -QLFDLIESMLEYEPSKRLTLAAALKHPFF 330
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
139-470 2.13e-48

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 173.88  E-value: 2.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 139 IVKNGEKWMDRYEIDSLIGKGSFGQVVKAYD-RVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKR 217
Cdd:cd14213     3 ICQSGDVLRARYEIVDTLGEGAFGKVVECIDhKMGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNSTFRCVQMLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSiiHCDLKPENILLC--------NP 289
Cdd:cd14213    83 WFDHHGHVCIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLT--HTDLKPENILFVqsdyvvkyNP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 290 KR---------SAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd14213   161 KMkrdertlknPDIKVVDFGSATYDDEHHSTLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 361 MNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPpgtrkLHNILGVETggpggrragesghtvADY 440
Cdd:cd14213   241 LAMMERILGPLPKHMIQKTRKRKYFHHDQLDWDEHSSAGRYVRRRCKP-----LKEFMLSQD---------------VDH 300
                         330       340       350
                  ....*....|....*....|....*....|
gi 1113820495 441 LKFKDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14213   301 EQLFDLIQKMLEYDPAKRITLDEALKHPFF 330
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
150-470 1.09e-46

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: 167.45  E-value: 1.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQAQI----EVRLLELMNKHDTemkyyIVHLKRHFMFRNH- 224
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIK--CMKKHFKSLEQVnnlrEIQALRRLSPHPN-----ILRLIEVLFDRKTg 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 -LCLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnpKRSAIKIVDFGSSC 303
Cdd:cd07831    74 rLALVFELMDMNLYELIKGRK-RPLPEKRVKNYMYQLLKSLDHMH--RNGIFHRDIKPENILI---KDDILKLADFGSCR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QLGQR--IYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAP 380
Cdd:cd07831   148 GIYSKppYTEYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVLKKFR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 381 KARKFFEKLPdgtwnlKKtkdgkreyKPPGTRKLHNILGVEtggpggrragesghtvadylkFKDLILRMLDYDPKTRIQ 460
Cdd:cd07831   228 KSRHMNYNFP------SK--------KGTGLRKLLPNASAE---------------------GLDLLKKLLAYDPDERIT 272
                         330
                  ....*....|
gi 1113820495 461 PYYALQHSFF 470
Cdd:cd07831   273 AKQALRHPYF 282
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
149-476 3.33e-46

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: 168.12  E-value: 3.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQ--AQI---EVRLLELMNKHDTEMKYYIVHlkrhfmfR- 222
Cdd:cd07852     8 RYEILKKLGKGAYGIVWKAIDKKTGEVVALK--KIFDAFRNAtdAQRtfrEIMFLQELNDHPNIIKLLNVI-------Ra 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 ---NHLCLVFEMLSYNLYDLLRntnfRGVSLNLTRKF-AQQMCTALLFLATPELsiIHCDLKPENILL---CNpkrsaIK 295
Cdd:cd07852    79 endKDIYLVFEYMETDLHAVIR----ANILEDIHKQYiMYQLLKALKYLHSGGV--IHRDLKPSNILLnsdCR-----VK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 296 IVDFG---SSCQLGQRIYQ-----YIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd07852   148 LADFGlarSLSQLEEDDENpvltdYVATRWYRAPEILLGSTrYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 367 VLGIPPAHILD--QAPKARKFFEKLPdgtwnlkktkdgkreykPPGTRKLHNILgvetggpggrragesGHTVADYLkfk 444
Cdd:cd07852   228 VIGRPSAEDIEsiQSPFAATMLESLP-----------------PSRPKSLDELF---------------PKASPDAL--- 272
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1113820495 445 DLILRMLDYDPKTRIQPYYALQHSF---FKKTADE 476
Cdd:cd07852   273 DLLKKLLVFNPNKRLTAEEALRHPYvaqFHNPADE 307
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
148-476 5.56e-44

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: 162.08  E-value: 5.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK--------IIKNKKAFLnqaqiEVRLLELMNkHD-------------T 206
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKklsrpfqsAIHAKRTYR-----ELRLLKHMK-HEnviglldvftpasS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 207 EMKYYIVHLKRHFMFRnhlclvfemlsynlyDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL 286
Cdd:cd07851    89 LEDFQDVYLVTHLMGA---------------DLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSA--GIIHRDLKPSNLAV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 287 cNpKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd07851   152 -N-EDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIM 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 366 EVLGIPPAHILD--QAPKARKFFEKLPdgtwnLKKTKDgkreykppgtrkLHNILgvetggpggrrageSGHTVadylKF 443
Cdd:cd07851   230 NLVGTPDEELLKkiSSESARNYIQSLP-----QMPKKD------------FKEVF--------------SGANP----LA 274
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1113820495 444 KDLILRMLDYDPKTRIQPYYALQHSFFKKTADE 476
Cdd:cd07851   275 IDLLEKMLVLDPDKRITAAEALAHPYLAEYHDP 307
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
156-345 2.05e-43

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: 156.28  E-value: 2.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHLCLVFEMLS 233
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPkeKLKKLLEELLREIEILKKLNHP------NIVKLYDVFETENFLYLVMEYCE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 Y-NLYDLLRNtNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQLGQ----- 307
Cdd:cd00180    75 GgSLKDLLKE-NKGPLSEEEALSILRQLLSALEYLH--SNGIIHRDLKPENILLDSDGT--VKLADFGLAKDLDSddsll 149
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1113820495 308 RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd00180   150 KTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
149-471 2.40e-43

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 158.89  E-value: 2.40e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKN---KKAF--LNQAQI-EVRLL-ELmnKHDTemkyyIVHLKRHFMF 221
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLgerKEAKdgINFTALrEIKLLqEL--KHPN-----IIGLLDVFGH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGS 301
Cdd:cd07841    74 KSNINLVFEFMETDLEKVIKDKSIV-LTPADIKSYMLMTLRGLEYLH--SNWILHRDLKPNNLLI--ASDGVLKLADFGL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQLGQ--RIY--QYIqSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahIL 376
Cdd:cd07841   149 ARSFGSpnRKMthQVV-TRWYRAPELLFGARhYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTP---TE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 DQAPKARkffeKLPDGTwnlkktkdgkrEYKP-PGTrKLHNILGVetggpggrrAGEsghtvaDYLkfkDLILRMLDYDP 455
Cdd:cd07841   225 ENWPGVT----SLPDYV-----------EFKPfPPT-PLKQIFPA---------ASD------DAL---DLLQRLLTLNP 270
                         330
                  ....*....|....*.
gi 1113820495 456 KTRIQPYYALQHSFFK 471
Cdd:cd07841   271 NKRITARQALEHPYFS 286
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
150-470 3.43e-43

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: 157.82  E-value: 3.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQI-EVRLLELMNKHDTEmkyYIVHLKR--HFMFRNH 224
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRvpLSEEGIPLSTIrEIALLKQLESFEHP---NVVRLLDvcHGPRTDR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 ---LCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRsaIKIVDFGS 301
Cdd:cd07838    78 elkLTLVFEHVDQDLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSH--RIVHRDLKPQNILVTSDGQ--VKLADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 ScqlgqRIYQYiQSRF--------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA 373
Cdd:cd07838   154 A-----RIYSF-EMALtsvvvtlwYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 374 hilDQAPKarkffeklpdgtwNLKKTKDGKREYKPPGTRKLhnilgVETGGPGGrragesghtvadylkfKDLILRMLDY 453
Cdd:cd07838   228 ---EEWPR-------------NSALPRSSFPSYTPRPFKSF-----VPEIDEEG----------------LDLLKKMLTF 270
                         330
                  ....*....|....*..
gi 1113820495 454 DPKTRIQPYYALQHSFF 470
Cdd:cd07838   271 NPHKRISAFEALQHPYF 287
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
150-470 1.07e-42

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: 156.57  E-value: 1.07e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKN---KKAFLNQAQIEVRLLELMNkHDTEMKYY-IVHLKRHFMFRNHL 225
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMeneKEGFPITAIREIKLLQKLD-HPNVVRLKeIVTSKGSAKYKGSI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNpkRSAIKIVDFGSScql 305
Cdd:cd07840    80 YMVFEYMDHDLTGLLDNPEVK-FTESQIKCYMKQLLEGLQYLHSN--GILHRDIKGSNILINN--DGVLKLADFGLA--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 gqRIYQYIQSR---------FYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAhi 375
Cdd:cd07840   152 --RPYTKENNAdytnrvitlWYRPPELLLGATrYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTE-- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 376 lDQAPKarkfFEKLPdgTWNLKKTkdgKREYKppgtrklhnilgvetggpggRRAGESGHTVADYlKFKDLILRMLDYDP 455
Cdd:cd07840   228 -ENWPG----VSDLP--WFENLKP---KKPYK--------------------RRLREVFKNVIDP-SALDLLDKLLTLDP 276
                         330
                  ....*....|....*
gi 1113820495 456 KTRIQPYYALQHSFF 470
Cdd:cd07840   277 KKRISADQALQHEYF 291
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
149-469 2.79e-42

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: 154.56  E-value: 2.79e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI---EVRLLELMNkHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMlrrEIEILKRLD-HP-----NIVKLYEVFEDDKNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLS-YNLYD-LLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKR-SAIKIVDFGSS 302
Cdd:cd05117    75 YLVMELCTgGELFDrIVKKGSF---SEREAAKIMKQILSAVAYLH--SQGIVHRDLKPENILLASKDPdSPIKIIDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQLGQRIYQY--IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIvevlgippahildqap 380
Cdd:cd05117   150 KIFEEGEKLKtvCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKI---------------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 381 karkffeklpdgtwnlkktKDGKREYKPPgtrklhnilgvetggpggrrageSGHTVADylKFKDLILRMLDYDPKTRIQ 460
Cdd:cd05117   214 -------------------LKGKYSFDSP-----------------------EWKNVSE--EAKDLIKRLLVVDPKKRLT 249

                  ....*....
gi 1113820495 461 PYYALQHSF 469
Cdd:cd05117   250 AAEALNHPW 258
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
149-470 3.45e-42

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: 155.18  E-value: 3.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF---LNQAQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEggiPNQALREIKALQACQGHP-----YVVKLRDVFPHGTGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSScql 305
Cdd:cd07832    76 VLVFEYMLSSLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMH--ANRIMHRDLKPANLLISS--TGVLKIADFGLA--- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 gqRIY------QY---IQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahI 375
Cdd:cd07832   148 --RLFseedprLYshqVATRWYRAPELLYGSRkYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTP---N 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 376 LDQAPKarkfFEKLPDGtwnlkktkdGKREYKP-PGTRkLHNILgvetggPGGRRAGesghtvadylkfKDLILRMLDYD 454
Cdd:cd07832   223 EKTWPE----LTSLPDY---------NKITFPEsKGIR-LEEIF------PDCSPEA------------IDLLKGLLVYN 270
                         330
                  ....*....|....*.
gi 1113820495 455 PKTRIQPYYALQHSFF 470
Cdd:cd07832   271 PKKRLSAEEALRHPYF 286
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
148-476 7.92e-41

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 152.91  E-value: 7.92e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMN--KHDTemkyyIVHLKRHFM----- 220
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRhfKHDN-----IIAIRDILRpkvpy 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 --FRnHLCLVFEMLSYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENiLLCNpKRSAIKIVD 298
Cdd:cd07855    80 adFK-DVYVVLDLMESDLHHIIHSD--QPLTLEHIRYFLYQLLRGLKYIHSA--NVIHRDLKPSN-LLVN-ENCELKIGD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FG-----SSCQLGQRIY--QYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGI 370
Cdd:cd07855   153 FGmarglCTSPEEHKYFmtEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 371 PPAHILDQ--APKARKFFEKLPDgtwnlkktkdgkreyKPPgtRKLHNILgvetggPGGRRagesgHTVadylkfkDLIL 448
Cdd:cd07855   233 PSQAVINAigADRVRRYIQNLPN---------------KQP--VPWETLY------PKADQ-----QAL-------DLLS 277
                         330       340
                  ....*....|....*....|....*...
gi 1113820495 449 RMLDYDPKTRIQPYYALQHSFFKKTADE 476
Cdd:cd07855   278 QMLRFDPSERITVAEALQHPFLAKYHDP 305
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
148-470 1.92e-40

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 150.45  E-value: 1.92e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA---F----LNQAQIevrLLELmnKHDTemkyyIVHLKRHFM 220
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEkegFpitsLREINI---LLKL--QHPN-----IVTVKEVVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRN--HLCLVFEMLSYNLYDLLrNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVD 298
Cdd:cd07843    75 GSNldKIYMVMEYVEHDLKSLM-ETMKQPFLQSEVKCLMLQLLSGVAHLH--DNWILHRDLKTSNLLLNN--RGILKICD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQLGQRIYQYIQ---SRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAH 374
Cdd:cd07843   150 FGLAREYGSPLKPYTQlvvTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 375 ILDQapkarkfFEKLPdgtwNLKKTKDGKREYKPPGTRKLHNILgvetggpggrraGESGHtvadylkfkDLILRMLDYD 454
Cdd:cd07843   230 IWPG-------FSELP----GAKKKTFTKYPYNQLRKKFPALSL------------SDNGF---------DLLNRLLTYD 277
                         330
                  ....*....|....*.
gi 1113820495 455 PKTRIQPYYALQHSFF 470
Cdd:cd07843   278 PAKRISAEDALKHPYF 293
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
156-470 6.16e-40

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 148.59  E-value: 6.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd07835     7 IGEGTYGVVYKARDKLTGEIVALKKIRletEDEGVPSTAIREISLLKELN-HP-----NIVRLLDVVHSENKLYLVFEFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQY 312
Cdd:cd07835    81 DLDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHR--VLHRDLKPQNLLI--DTEGALKLADFGLARAFGVPVRTY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 313 ---IQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAhilDQAPKArkffEK 388
Cdd:cd07835   157 theVVTLWYRAPEILLGSKhYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDE---DVWPGV----TS 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 389 LPDgtwnlkkTKDGKREYKPPGTRKLhnilgVETGGPGGRragesghtvadylkfkDLILRMLDYDPKTRIQPYYALQHS 468
Cdd:cd07835   230 LPD-------YKPTFPKWARQDLSKV-----VPSLDEDGL----------------DLLSQMLVYDPAKRISAKAALQHP 281

                  ..
gi 1113820495 469 FF 470
Cdd:cd07835   282 YF 283
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
150-475 7.44e-40

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 152.88  E-value: 7.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNkhdtemkyyIVHLKRHFM---FRNH-- 224
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHIN---------IIFLKDYYYtecFKKNek 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 ---LCLVFEMLSYNLYDLLR--NTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENiLLCNPKRSAIKIVDF 299
Cdd:PTZ00036  139 nifLNVVMEFIPQTVHKYMKhyARNNHALPLFLVKLYSYQLCRALAYIHSK--FICHRDLKPQN-LLIDPNTHTLKLCDF 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 GSSCQL--GQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAhil 376
Cdd:PTZ00036  216 GSAKNLlaGQRSVSYICSRFYRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTPTE--- 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 DQAPKARKFFE--KLPDgtwnlKKTKDGKREYkPPGTRKlhnilgvetggpggrragesghtvaDYLKFkdlILRMLDYD 454
Cdd:PTZ00036  293 DQLKEMNPNYAdiKFPD-----VKPKDLKKVF-PKGTPD-------------------------DAINF---ISQFLKYE 338
                         330       340
                  ....*....|....*....|.
gi 1113820495 455 PKTRIQPYYALQHSFFKKTAD 475
Cdd:PTZ00036  339 PLKRLNPIEALADPFFDDLRD 359
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
149-375 7.89e-40

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: 147.28  E-value: 7.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-KNKKAFLNQAQI--EVRLLELMNkHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIdKSKLKEEIEEKIkrEIEIMKLLN-HP-----NIIKLYEVIETENKI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRntNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGSS-- 302
Cdd:cd14003    75 YLVMEYASGgELFDYIV--NNGRLSEDEARRFFQQLISAVDYCH--SNGIVHRDLKLENILLDKNGN--LKIIDFGLSne 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 303 CQLGQRIYQYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHI 375
Cdd:cd14003   149 FRGGSLLKTFCGTPAYAAPEVLLGRKYDgPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHL 222
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
149-382 1.29e-38

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: 144.27  E-value: 1.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK----NKKAFLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNH 224
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRpelaEDEEFRERFLREARALARLS-HP-----NIVRVYDVGEDDGR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLS-YNLYDLLRntnfRGVSLNLTRK--FAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGS 301
Cdd:cd14014    75 PYIVMEYVEgGSLADLLR----ERGPLPPREAlrILAQIADALAAAH--RAGIVHRDIKPANILLTEDGR--VKLTDFGI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQLGQ----RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILD 377
Cdd:cd14014   147 ARALGDsgltQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNP 226

                  ....*
gi 1113820495 378 QAPKA 382
Cdd:cd14014   227 DVPPA 231
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
148-373 1.27e-37

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: 142.06  E-value: 1.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNkhdTEMKYYIVHLKRHFMFRNHLCL 227
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLR---TLKQENIVELKEAFRRRGKLYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNpkRSAIKIVDFGSSCQLGQ 307
Cdd:cd07848    78 VFEYVEKNMLELLEEMP-NGVPPEKVRSYIYQLIKAIHWCHKND--IVHRDIKPENLLISH--NDVLKLCDFGFARNLSE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 ----RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA 373
Cdd:cd07848   153 gsnaNYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPA 222
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
149-470 1.57e-37

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 142.02  E-value: 1.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNK--HDTEMKYYIVHLKRHFMFRN 223
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRvqtNEDGLPLSTVREVALLKRLEAfdHPNIVRLMDVCATSRTDRET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNpkRSAIKIVDFGSSc 303
Cdd:cd07863    81 KVTLVFEHVDQDLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHAN--CIVHRDLKPENILVTS--GGQVKLADFGLA- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 qlgqRIYQY-------IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAhil 376
Cdd:cd07863   156 ----RIYSCqmaltpvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPE--- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 DQAPKArkffEKLPDGTwnlkktkdgkreYKPPGTRKLHNILGVETggpggrragESGhtvadylkfKDLILRMLDYDPK 456
Cdd:cd07863   229 DDWPRD----VTLPRGA------------FSPRGPRPVQSVVPEIE---------ESG---------AQLLLEMLTFNPH 274
                         330
                  ....*....|....
gi 1113820495 457 TRIQPYYALQHSFF 470
Cdd:cd07863   275 KRISAFRALQHPFF 288
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
149-475 2.95e-37

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: 142.61  E-value: 2.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQA-QI--EVRLLELMNKHDtemkyyIVHLKrHFM----- 220
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDAtRIlrEIKLLRLLRHPD------IVEIK-HIMlppsr 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 --FRNhLCLVFEMLSYNLYDLLRNTNfrgvslNLTRK----FAQQMCTALLFLATPelSIIHCDLKPENILL-CNPKrsa 293
Cdd:cd07859    74 reFKD-IYVVFELMESDLHQVIKAND------DLTPEhhqfFLYQLLRALKYIHTA--NVFHRDLKPKNILAnADCK--- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 IKIVDFG----SSCQLGQRIY--QYIQSRFYRSPEvLLG---MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd07859   142 LKICDFGlarvAFNDTPTAIFwtDYVATRWYRAPE-LCGsffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLI 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 365 VEVLGIPPAHILDQA--PKARKFFEKLpdgtwnlkktkdgkREYKP-PGTRKLHNilgvetggpggrragesghtvADYL 441
Cdd:cd07859   221 TDLLGTPSPETISRVrnEKARRYLSSM--------------RKKQPvPFSQKFPN---------------------ADPL 265
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1113820495 442 KFKdLILRMLDYDPKTRIQPYYALQHSFFKKTAD 475
Cdd:cd07859   266 ALR-LLERLLAFDPKDRPTAEEALADPYFKGLAK 298
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
149-476 4.55e-37

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: 141.77  E-value: 4.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYD--RVEQEWVAIKIIKN---KKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFrN 223
Cdd:cd07857     1 RYELIKELGQGAYGIVCSARNaeTSEEETVAIKKITNvfsKKILAKRALRELKLLRHFRGHKNITCLYDMDIVFPGNF-N 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNLYDLLRNtnfrGVSLNLT--RKFAQQMCTALLFLATPelSIIHCDLKPENiLLCNPKrSAIKIVDFGS 301
Cdd:cd07857    80 ELYLYEELMEADLHQIIRS----GQPLTDAhfQSFIYQILCGLKYIHSA--NVLHRDLKPGN-LLVNAD-CELKICDFGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SC-------QLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA 373
Cdd:cd07857   152 ARgfsenpgENAGFMTEYVATRWYRAPEIMLSfQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 374 HILDQ--APKARKFFEKLPdgtwnlkktkdgkreyKPPGtRKLHNILgvetggPGgrragesghtvADYLKFkDLILRML 451
Cdd:cd07857   232 ETLSRigSPKAQNYIRSLP----------------NIPK-KPFESIF------PN-----------ANPLAL-DLLEKLL 276
                         330       340
                  ....*....|....*....|....*...
gi 1113820495 452 DYDPKTRIQPYYALQHSF---FKKTADE 476
Cdd:cd07857   277 AFDPTKRISVEEALEHPYlaiWHDPDDE 304
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
149-471 6.74e-37

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 141.40  E-value: 6.74e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQ-----AQIEVRLLELMN---------------KHDTEM 208
Cdd:cd07850     1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIK--KLSRPFQNVthakrAYRELVLMKLVNhkniigllnvftpqkSLEEFQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 209 KYYIVhlkRHFMFRNhLCLVFEM------LSYNLYdllrntnfrgvslnltrkfaqQMCTALLFLATPelSIIHCDLKPE 282
Cdd:cd07850    79 DVYLV---MELMDAN-LCQVIQMdldherMSYLLY---------------------QMLCGIKHLHSA--GIIHRDLKPS 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 283 NILLcnPKRSAIKIVDFGSSCQLGQ--RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd07850   132 NIVV--KSDCTLKILDFGLARTAGTsfMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQ 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 361 MNKIVEVLGIPPAHILDQ-APKARKFFEKLPdgtwnlkktkdgkrEYKPPGTRKL--HNILGVETGGPGGRRAGESghtv 437
Cdd:cd07850   210 WNKIIEQLGTPSDEFMSRlQPTVRNYVENRP--------------KYAGYSFEELfpDVLFPPDSEEHNKLKASQA---- 271
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1113820495 438 adylkfKDLILRMLDYDPKTRIQPYYALQHSFFK 471
Cdd:cd07850   272 ------RDLLSKMLVIDPEKRISVDDALQHPYIN 299
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
156-470 1.04e-36

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 139.56  E-value: 1.04e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd07860     8 IGEGTYGVVYKARNKLTGEVVALKKIRldtETEGVPSTAIREISLLKELNHPN------IVKLLDVIHTENKLYLVFEFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQY 312
Cdd:cd07860    82 HQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHR--VLHRDLKPQNLLI--NTEGAIKLADFGLARAFGVPVRTY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 313 ---IQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPahildqapkarkffEK 388
Cdd:cd07860   158 theVVTLWYRAPEILLGCKyYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPD--------------EV 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 389 LPDGTWNLKKTKDGKREYKPPGTRKLhnilgVETGGPGGRragesghtvadylkfkDLILRMLDYDPKTRIQPYYALQHS 468
Cdd:cd07860   224 VWPGVTSMPDYKPSFPKWARQDFSKV-----VPPLDEDGR----------------DLLSQMLHYDPNKRISAKAALAHP 282

                  ..
gi 1113820495 469 FF 470
Cdd:cd07860   283 FF 284
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
140-470 7.97e-36

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 139.01  E-value: 7.97e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 140 VKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTE--MKYYIVHLKR 217
Cdd:cd14216     2 VKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETALDEIKLLKSVRNSDPNdpNREMVVQLLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFR----NHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLC------ 287
Cdd:cd14216    82 DFKISgvngTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIRQVLQGLDYLHT-KCRIIHTDIKPENILLSvneqyi 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 288 ----------------------NPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd14216   161 rrlaaeatewqrnflvnplepkNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 346 HTGEPLF---SGAN---EVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDgtwnLKKTKdgkrEYKPPGtrkLHNILG 419
Cdd:cd14216   241 ATGDYLFephSGEDysrDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGD----LKHIT----KLKPWG---LFEVLV 309
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 420 VETGGPGGRRAGesghtvadylkFKDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14216   310 EKYEWSQEEAAG-----------FTDFLLPMLELIPEKRATAAECLRHPWL 349
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
156-479 1.19e-35

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 137.89  E-value: 1.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNkkAFLNQAQI-----EVRLLELMnKHDTemkyyIVHLK--------RHFmfr 222
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKIAN--AFDNRIDAkrtlrEIKLLRHL-DHEN-----VIAIKdimppphrEAF--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLSYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL---CNpkrsaIKIVDF 299
Cdd:cd07858    82 NDVYIVYELMDTDLHQIIRSS--QTLSDDHCQYFLYQLLRGLKYIHSA--NVLHRDLKPSNLLLnanCD-----LKICDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 G---SSCQLGQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHI 375
Cdd:cd07858   153 GlarTTSEKGDFMTEYVVTRWYRAPELLLNCSeYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEED 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 376 LD--QAPKARKFFEKLPdgtwnlkktkdgkREYKPPGTRKLHNIlgvetggpggrragesgHTVAdylkfKDLILRMLDY 453
Cdd:cd07858   233 LGfiRNEKARRYIRSLP-------------YTPRQSFARLFPHA-----------------NPLA-----IDLLEKMLVF 277
                         330       340
                  ....*....|....*....|....*.
gi 1113820495 454 DPKTRIQPYYALQHSFFKKTADEGTN 479
Cdd:cd07858   278 DPSKRITVEEALAHPYLASLHDPSDE 303
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
155-388 3.83e-35

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: 134.19  E-value: 3.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIK---IIKNKKAFLNQAQIEVRLLELMnKHDTEMKYYIVHLKRhfmfrNHLCLVFEM 231
Cdd:cd06606     7 LLGKGSFGSVYLALNLDTGELMAVKeveLSGDSEEELEALEREIRILSSL-KHPNIVRYLGTERTE-----NTLNIFLEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSY-NLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQLGQrIY 310
Cdd:cd06606    81 VPGgSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLH--SNGIVHRDIKGANILVDS--DGVVKLADFGCAKRLAE-IA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 311 QYIQSR------FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSG-ANEVDQMNKIVEVLGIP--PAHIldqAPK 381
Cdd:cd06606   154 TGEGTKslrgtpYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEPPpiPEHL---SEE 230

                  ....*..
gi 1113820495 382 ARKFFEK 388
Cdd:cd06606   231 AKDFLRK 237
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
156-389 6.27e-35

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: 133.41  E-value: 6.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLN----QAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLCLVFE- 230
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRkeveHTLNERNILERVN-HP-----FIVKLHYAFQTEEKLYLVLDy 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQL---GQ 307
Cdd:cd05123    75 VPGGELFSHLSK--EGRFPEERARFYAAEIVLALEYLH--SLGIIYRDLKPENILLD--SDGHIKLTDFGLAKELssdGD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE-VLGIPPahilDQAPKARKFF 386
Cdd:cd05123   149 RTYTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKsPLKFPE----YVSPEAKSLI 224

                  ...
gi 1113820495 387 EKL 389
Cdd:cd05123   225 SGL 227
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
148-382 7.73e-35

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 138.99  E-value: 7.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK----NKKAFLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRN 223
Cdd:COG0515     7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRpelaADPEARERFRREARALARLN-HP-----NIVRVYDVGEEDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLS-YNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGSS 302
Cdd:COG0515    81 RPYLVMEYVEgESLADLLRRR--GPLPPAEALRILAQLAEALAAAH--AAGIVHRDIKPANILLTPDGR--VKLIDFGIA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQLGQ----RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ 378
Cdd:COG0515   155 RALGGatltQTGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPD 234

                  ....
gi 1113820495 379 APKA 382
Cdd:COG0515   235 LPPA 238
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
147-475 8.29e-35

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 134.18  E-value: 8.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMnKHDTEMKYY-IVHLKRHfmfr 222
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRleqEDEGVPSTAIREISLLKEM-QHGNIVRLQdVVHSEKR---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 nhLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENiLLCNPKRSAIKIVDFGSS 302
Cdd:PLN00009   76 --LYLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHR--VLHRDLKPQN-LLIDRRTNALKLADFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQLGQRIYQY---IQSRFYRSPEVLLGM-PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahildq 378
Cdd:PLN00009  151 RAFGIPVRTFtheVVTLWYRAPEILLGSrHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTP------- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 379 apkarkfFEKLPDGTWNLKKTKDGKREYKPPGTRKLhnilgVETGGPGGrragesghtvadylkfKDLILRMLDYDPKTR 458
Cdd:PLN00009  224 -------NEETWPGVTSLPDYKSAFPKWPPKDLATV-----VPTLEPAG----------------VDLLSKMLRLDPSKR 275
                         330
                  ....*....|....*..
gi 1113820495 459 IQPYYALQHSFFKKTAD 475
Cdd:PLN00009  276 ITARAALEHEYFKDLGD 292
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
156-470 9.71e-35

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 133.76  E-value: 9.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRLLELMN--KHDTEMKYY-IVHLKrhfmfrNHLCLVFEML 232
Cdd:cd07836     8 LGEGTYATVYKGRNRTTGEIVALKEI-HLDAEEGTPSTAIREISLMKelKHENIVRLHdVIHTE------NKLMLVFEYM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SYNLYDLLR-NTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQ 311
Cdd:cd07836    81 DKDLKKYMDtHGVRGALDPNTVKSFTYQLLKGIAFCH--ENRVLHRDLKPQNLLI--NKRGELKLADFGLARAFGIPVNT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 312 Y---IQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahildqapkarkffe 387
Cdd:cd07836   157 FsneVVTLWYRAPDVLLGsRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTP---------------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 388 klPDGTW-NLKKTKDGKREYKPPGTRKLHNILgvetggPGGRRAGesghtvadylkfKDLILRMLDYDPKTRIQPYYALQ 466
Cdd:cd07836   221 --TESTWpGISQLPEYKPTFPRYPPQDLQQLF------PHADPLG------------IDLLHRLLQLNPELRISAHDALQ 280

                  ....
gi 1113820495 467 HSFF 470
Cdd:cd07836   281 HPWF 284
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
148-469 1.31e-34

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: 135.12  E-value: 1.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMnKHDTEMKYYIVHLKRHFMFRNHL 225
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfEHQTYCLRTLREIKILLRF-KHENIIGILDIQRPPTFESFKDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNfrgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL---CNpkrsaIKIVDFG-- 300
Cdd:cd07849    84 YIVQELMETDLYKLIKTQH---LSNDHIQYFLYQILRGLKYIHSA--NVLHRDLKPSNLLLntnCD-----LKICDFGla 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 -----SSCQLGQrIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAH 374
Cdd:cd07849   154 riadpEHDHTGF-LTEYVATRWYRAPEIMLNSKgYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 375 ILD--QAPKARKFFEKLPdgtwnlKKTKDGKREYKPPgtrklHNILGVetggpggrragesghtvadylkfkDLILRMLD 452
Cdd:cd07849   233 DLNciISLKARNYIKSLP------FKPKVPWNKLFPN-----ADPKAL------------------------DLLDKMLT 277
                         330
                  ....*....|....*..
gi 1113820495 453 YDPKTRIQPYYALQHSF 469
Cdd:cd07849   278 FNPHKRITVEEALAHPY 294
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
149-471 1.50e-34

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 134.89  E-value: 1.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYE-IDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK---------AFLNQAQIE---VRLLELMN--KHDTEMKYYIV 213
Cdd:PTZ00024    9 RYIqKGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEisndvtkdrQLVGMCGIHfttLRELKIMNeiKHENIMGLVDV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 214 HLKRHFmfrnhLCLVFEMLSYNLYDLLrNTNFRgvslnLTRkfAQQMCTAL-LFLATPEL---SIIHCDLKPENILLcnP 289
Cdd:PTZ00024   89 YVEGDF-----INLVMDIMASDLKKVV-DRKIR-----LTE--SQVKCILLqILNGLNVLhkwYFMHRDLSPANIFI--N 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 290 KRSAIKIVDFGSSCQLGQRIY-------QYIQSR----------FYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPL 351
Cdd:PTZ00024  154 SKGICKIADFGLARRYGYPPYsdtlskdETMQRReemtskvvtlWYRAPELLMGAEkYHFAVDMWSVGCIFAELLTGKPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 352 FSGANEVDQMNKIVEVLGIPPAhilDQAPKARkffeKLPDGTwnlkktkdgkrEYKPPGTRKLHNILgvetggpggrrag 431
Cdd:PTZ00024  234 FPGENEIDQLGRIFELLGTPNE---DNWPQAK----KLPLYT-----------EFTPRKPKDLKTIF------------- 282
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1113820495 432 esGHTVADYLkfkDLILRMLDYDPKTRIQPYYALQHSFFK 471
Cdd:PTZ00024  283 --PNASDDAI---DLLQSLLKLNPLERISAKEALKHEYFK 317
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
148-390 1.52e-34

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: 133.32  E-value: 1.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII---KNKKAFLNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNH 224
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFlesEDDKMVKKIAMREIKMLKQL-RHEN-----LVNLIEVFRRKKR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILlcNPKRSAIKIVDFGSSCQ 304
Cdd:cd07846    75 WYLVFEFVDHTVLDDLEKYP-NGLDESRVRKYLFQILRGIDFCHSH--NIIHRDIKPENIL--VSQSGVVKLCDFGFART 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 L--GQRIY-QYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGippahilDQAP 380
Cdd:cd07846   150 LaaPGEVYtDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLG-------NLIP 222
                         250
                  ....*....|
gi 1113820495 381 KARKFFEKLP 390
Cdd:cd07846   223 RHQELFQKNP 232
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
156-471 5.28e-34

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: 132.49  E-value: 5.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQI-EVRLLeLMNKHDTemkyyIVHLKrHFMFRNHL---CLVF 229
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKVRmdNERDGIPISSLrEITLL-LNLRHPN-----IVELK-EVVVGKHLdsiFLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNLYDLLRN--TNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSScqlgq 307
Cdd:cd07845    88 EYCEQDLASLLDNmpTPF---SESQVKCLMLQLLRGLQYLH--ENFIIHRDLKVSNLLLTD--KGCLKIADFGLA----- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIYQYIQ--------SRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHI--- 375
Cdd:cd07845   156 RTYGLPAkpmtpkvvTLWYRAPELLLGCTtYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESIwpg 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 376 LDQAPKARKFfeKLPDGTWNLKKTKDGKreykppgtrklhnilgvetggpggrrAGESGHTVADYLkfkdlilrmLDYDP 455
Cdd:cd07845   236 FSDLPLVGKF--TLPKQPYNNLKHKFPW--------------------------LSEAGLRLLNFL---------LMYDP 278
                         330
                  ....*....|....*.
gi 1113820495 456 KTRIQPYYALQHSFFK 471
Cdd:cd07845   279 KKRATAEEALESSYFK 294
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
149-366 2.40e-33

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: 129.12  E-value: 2.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-------KNKKaflnQAQIEVRLLELMNkHDtemkyYIVHLKRHFMF 221
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIdlsnmseKERE----EALNEVKLLSKLK-HP-----NIVKYYESFEE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEmlsY----NLYDLLRNTNFRGVSL---NLTRKFAQqMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAI 294
Cdd:cd08215    71 NGKLCIVME---YadggDLAQKIKKQKKKGQPFpeeQILDWFVQ-ICLALKYLH--SRKILHRDLKTQNIFLT--KDGVV 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 295 KIVDFGSSCQLgQRIYQYIQSR----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd08215   143 KLGDFGISKVL-ESTTDLAKTVvgtpYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVK 217
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
147-471 3.00e-33

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: 129.97  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFlnQAQIEVRLLELMNKHDTEMKYYIVhlkrhfmFRNHL- 225
Cdd:cd14132    17 QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKK--KIKREIKILQNLRGGPNIVKLLDV-------VKDPQs 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 ---CLVFEMLSynlydllrNTNFRGVSLNLT----RKFAQQMCTALLFlaTPELSIIHCDLKPENILlCNPKRSAIKIVD 298
Cdd:cd14132    88 ktpSLIFEYVN--------NTDFKTLYPTLTdydiRYYMYELLKALDY--CHSKGIMHRDVKPHNIM-IDHEKRKLRLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGsscqL------GQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTG-EPLFSGANEVDQMNKIVEVLGI 370
Cdd:cd14132   157 WG----LaefyhpGQEYNVRVASRYYKGPELLVDYQyYDYSLDMWSLGCMLASMIFRkEPFFHGHDNYDQLVKIAKVLGT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 371 ppAHILDQapkARKFFEKLPDGTWNL--KKTKDGKREYKPPGTRKLHNILGVetggpggrragesghtvadylkfkDLIL 448
Cdd:cd14132   233 --DDLYAY---LDKYGIELPPRLNDIlgRHSKKPWERFVNSENQHLVTPEAL------------------------DLLD 283
                         330       340
                  ....*....|....*....|...
gi 1113820495 449 RMLDYDPKTRIQPYYALQHSFFK 471
Cdd:cd14132   284 KLLRYDHQERITAKEAMQHPYFD 306
PTZ00284 PTZ00284
protein kinase; Provisional
149-373 3.36e-33

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 133.94  E-value: 3.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRN-HLCL 227
Cdd:PTZ00284  130 RFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDAKIEIQFMEKVRQADPADRFPLMKIQRYFQNETgHMCI 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYD-LLRNTNFRgvslnlTRKFAQ---QMCTALLFLATpELSIIHCDLKPENILL--------------CNP 289
Cdd:PTZ00284  210 VMPKYGPCLLDwIMKHGPFS------HRHLAQiifQTGVALDYFHT-ELHLMHTDLKPENILMetsdtvvdpvtnraLPP 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 290 KRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLG 369
Cdd:PTZ00284  283 DPCRVRICDLGGCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLMEKTLG 362

                  ....
gi 1113820495 370 IPPA 373
Cdd:PTZ00284  363 RLPS 366
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
140-467 4.11e-33

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 131.29  E-value: 4.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 140 VKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTE--MKYYIVHLKR 217
Cdd:cd14218     2 VKIGDLFNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKCVRDSDPSdpKRETIVQLID 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFRN----HLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLC------ 287
Cdd:cd14218    82 DFKISGvngvHVCMVLEVLGHQLLKWIIKSNYQGLPLPCVKSILRQVLQGLDYLHT-KCKIIHTDIKPENILMCvdegyv 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 288 ----------------NPKRSA----------------------IKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPY 329
Cdd:cd14218   161 rrlaaeatiwqqagapPPSGSSvsfgasdflvnplepqnadkirVKIADLGNACWVHKHFTEDIQTRQYRALEVLIGAEY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 330 DLAIDMWSLGCILVEMHTGEPLF---SGAN---EVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDgtwnLKKTKDgk 403
Cdd:cd14218   241 GTPADIWSTACMAFELATGDYLFephSGEDytrDEDHIAHIVELLGDIPPHFALSGRYSREYFNRRGE----LRHIKN-- 314
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 404 reYKPPGtrkLHNILGVETGGPggrragesghtVADYLKFKDLILRMLDYDPKTRIQPYYALQH 467
Cdd:cd14218   315 --LKHWG---LYEVLVEKYEWP-----------LEQAAQFTDFLLPMMEFLPEKRATAAQCLQH 362
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
150-353 5.27e-33

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: 128.09  E-value: 5.27e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK-NKKAFLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLCLV 228
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINlESKEKKESILNEIAILKKCK-HP-----NIVKYYGSYLKKDELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSY-NLYDLLRNTNfrgVSLNLT-RKF-AQQMCTALLFLAtpELSIIHCDLKPENILLcnpKRSA-IKIVDFGSSCQ 304
Cdd:cd05122    76 MEFCSGgSLKDLLKNTN---KTLTEQqIAYvCKEVLKGLEYLH--SHGIIHRDIKAANILL---TSDGeVKLIDFGLSAQ 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 305 L---GQRIYQyIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFS 353
Cdd:cd05122   148 LsdgKTRNTF-VGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYS 198
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
150-389 9.59e-33

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: 127.72  E-value: 9.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIK------IIKNKKAflNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRN 223
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldkrhIIKEKKV--KYVTIEKEVLSRLA-HP-----GIVKLYYTFQDES 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNlyDLLRNTNFRGvSLNL--TRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRsaIKIVDFGS 301
Cdd:cd05581    75 KLYFVLEYAPNG--DLLEYIRKYG-SLDEkcTRFYTAEIVLALEYLHS--KGIIHRDLKPENILLDEDMH--IKITDFGT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQLG------------QRIYQYIQSR---F-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQM 361
Cdd:cd05581   148 AKVLGpdsspestkgdaDSQIAYNQARaasFvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTF 227
                         250       260
                  ....*....|....*....|....*....
gi 1113820495 362 NKIVEV-LGIPPahilDQAPKARKFFEKL 389
Cdd:cd05581   228 QKIVKLeYEFPE----NFPPDAKDLIQKL 252
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
156-372 1.27e-32

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: 126.50  E-value: 1.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYdrveqeW----VAIKIIKNKK---AFLNQAQIEVRLLELMNkHDTemkyyIVHLKRHFMFRNHLCLV 228
Cdd:cd13999     1 IGSGSFGEVYKGK------WrgtdVAIKKLKVEDdndELLKEFRREVSILSKLR-HPN-----IVQFIGACLSPPPLCIV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSY-NLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQLGQ 307
Cdd:cd13999    69 TEYMPGgSLYDLLHKKKIP-LSWSLRLKIALDIARGMNYLHSP--PIIHRDLKSLNILLDENFT--VKIADFGLSRIKNS 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 308 -------RIYQYIqsrfYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPP 372
Cdd:cd13999   144 ttekmtgVVGTPR----WMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPP 211
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
148-391 1.35e-32

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: 127.87  E-value: 1.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK---------IIKnKKAFLnqaqiEVRLLELMnKHDTemkyyIVHLKRH 218
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkfveseddpVIK-KIALR-----EIRMLKQL-KHPN-----LVNLIEV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLrNTNFRGVSLNLTRKFAQQMCTALLFlaTPELSIIHCDLKPENILLCnpKRSAIKIVD 298
Cdd:cd07847    69 FRRKRKLHLVFEYCDHTVLNEL-EKNPRGVPEHLIKKIIWQTLQAVNF--CHKHNCIHRDVKPENILIT--KQGQIKLCD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQL---GQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLG-IPPA 373
Cdd:cd07847   144 FGFARILtgpGDDYTDYVATRWYRAPELLVGdTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGdLIPR 223
                         250       260
                  ....*....|....*....|
gi 1113820495 374 HIldQAPKARKFFE--KLPD 391
Cdd:cd07847   224 HQ--QIFSTNQFFKglSIPE 241
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
148-470 2.68e-32

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 127.49  E-value: 2.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII---KNKKAFLNQAQIEVRLLELMnKHDTemkyyIVHL--------K 216
Cdd:cd07865    12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmeNEKEGFPITALREIKILQLL-KHEN-----VVNLieicrtkaT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 217 RHFMFRNHLCLVFEMLSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCnpKRSAIKI 296
Cdd:cd07865    86 PYNRYKGSIYLVFEFCEHDLAGLLSNKNVK-FTLSEIKKVMKMLLNGLYYIHRNK--ILHRDMKAANILIT--KDGVLKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 297 VDFG-------SSCQLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVL 368
Cdd:cd07865   161 ADFGlarafslAKNSQPNRYTNRVVTLWYRPPELLLGeRDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLC 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 369 G-IPPahilDQAPKARKF--FEK--LPDGtwnlkkTKDGKREYKPPGTRKLHNIlgvetggpggrragesghtvadylkf 443
Cdd:cd07865   241 GsITP----EVWPGVDKLelFKKmeLPQG------QKRKVKERLKPYVKDPYAL-------------------------- 284
                         330       340
                  ....*....|....*....|....*..
gi 1113820495 444 kDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd07865   285 -DLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
156-470 4.69e-32

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 126.00  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLL-ELmnKHDTemkyyIVHLKRHFMFRNHLCLVFEM 231
Cdd:cd07861     8 IGEGTYGVVYKGRNKKTGQIVAMKKIRlesEEEGVPSTAIREISLLkEL--QHPN-----IVCLEDVLMQENRLYLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYNL---YDLLRNTNFrgVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLG-- 306
Cdd:cd07861    81 LSMDLkkyLDSLPKGKY--MDAELVKSYLYQILQGILFCHSRR--VLHRDLKPQNLLI--DNKGVIKLADFGLARAFGip 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 307 QRIYQY-IQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQApkark 384
Cdd:cd07861   155 VRVYTHeVVTLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGV----- 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 385 ffEKLPDgtwnlkktkdgkreYKPPGTRKLHNILGVETggpggRRAGESGhtvadylkfKDLILRMLDYDPKTRIQPYYA 464
Cdd:cd07861   230 --TSLPD--------------YKNTFPKWKKGSLRTAV-----KNLDEDG---------LDLLEKMLIYDPAKRISAKKA 279

                  ....*.
gi 1113820495 465 LQHSFF 470
Cdd:cd07861   280 LVHPYF 285
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
149-470 4.75e-32

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 127.02  E-value: 4.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAY--DRVEQEWVAIKIIKNKKAF---LNQAQI-EVRLL-ELMNKHdtemkyyIVHLKRHFMF 221
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKrkNGKDGKEYAIKKFKGDKEQytgISQSACrEIALLrELKHEN-------VVSLVEVFLE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLC--LVFEmlsYNLYDLL------RNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL--CNPKR 291
Cdd:cd07842    74 HADKSvyLLFD---YAEHDLWqiikfhRQAKRVSIPPSMVKSLLWQILNGIHYLH--SNWVLHRDLKPANILVmgEGPER 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 292 SAIKIVDFGsscqLGQRIYQYIQSRF----------YRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANE--- 357
Cdd:cd07842   149 GVVKIGDLG----LARLFNAPLKPLAdldpvvvtiwYRAPELLLGARhYTKAIDIWAIGCIFAELLTLEPIFKGREAkik 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 358 ------VDQMNKIVEVLGIPPAhilDQAPKarkfFEKLPDGTWNLKKTKdgKREYKPPGTRKLHNILGVEtgGPGGRrag 431
Cdd:cd07842   225 ksnpfqRDQLERIFEVLGTPTE---KDWPD----IKKMPEYDTLKSDTK--ASTYPNSLLAKWMHKHKKP--DSQGF--- 290
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1113820495 432 esghtvadylkfkDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd07842   291 -------------DLLRKLLEYDPTKRITAEEALEHPYF 316
Pkinase pfam00069
Protein kinase domain;
150-470 7.04e-32

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 123.51  E-value: 7.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA---FLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLC 226
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIkkkKDKNILREIKILKKLN-HP-----NIVRLYDAFEDKDNLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALlflatpelsiihcdlkpENillcnpkrsaikivdfgsscql 305
Cdd:pfam00069  75 LVLEYVEGgSLFDLLSEK--GAFSEREAKFIMKQILEGL-----------------ES---------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNkivevlgippaHILDQAPKARKF 385
Cdd:pfam00069 114 GSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYE-----------LIIDQPYAFPEL 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 386 FEKLPDgtwnlkktkdgkreykppgtrklhnilgvetggpggrragesghtvadylKFKDLILRMLDYDPKTRIQPYYAL 465
Cdd:pfam00069 183 PSNLSE--------------------------------------------------EAKDLLKKLLKKDPSKRLTATQAL 212

                  ....*
gi 1113820495 466 QHSFF 470
Cdd:pfam00069 213 QHPWF 217
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
156-376 6.23e-31

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 121.95  E-value: 6.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKII---KNKKAFLNQAQIEVRLLELMnKHDtemkyYIVHLKRHFMFRNHLCLVFEml 232
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkKLNKKLQENLESEIAILKSI-KHP-----NIVRLYDVQKTEDFIYLVLE-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 sY----NLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL-CNPKRSAIKIVDFGSScqlgq 307
Cdd:cd14009    73 -YcaggDLSQYIRK--RGRLPEAVARHFMQQLASGLKFLR--SKNIIHRDLKPQNLLLsTSGDDPVLKIADFGFA----- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 riyQYIQ----------SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI---VEVLGIPPAH 374
Cdd:cd14009   143 ---RSLQpasmaetlcgSPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIersDAVIPFPIAA 219

                  ..
gi 1113820495 375 IL 376
Cdd:cd14009   220 QL 221
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
140-470 4.80e-30

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 122.45  E-value: 4.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 140 VKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTE--MKYYIVHLKR 217
Cdd:cd14217     4 VKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLRCVRESDPEdpNKDMVVQLID 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HF----MFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLC------ 287
Cdd:cd14217    84 DFkisgMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPIRCVKSIIRQVLQGLDYLHS-KCKIIHTDIKPENILMCvddayv 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 288 -------------------------------------NPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYD 330
Cdd:cd14217   163 rrmaaeatewqkagapppsgsavstapdllvnpldprNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 331 LAIDMWSLGCILVEMHTGEPLF---SG---ANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKlpdgtwnlkktKDGKR 404
Cdd:cd14217   243 TPADIWSTACMAFELATGDYLFephSGedySRDEDHIAHIIELLGCIPRHFALSGKYSREFFNR-----------RGELR 311
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 405 EYKPPGTRKLHNILGVETGGPggrrAGESGHtvadylkFKDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14217   312 HITKLKPWSLFDVLVEKYGWP----HEDAAQ-------FTDFLIPMLEMVPEKRASAGECLRHPWL 366
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
148-470 6.23e-30

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 120.32  E-value: 6.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNKhdtemKYYIVHLKRHFMFRNH 224
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRlemEEEGVPSTALREVSLLQMLSQ-----SIYIVRLLDVEHVEEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 ----LCLVFEMLSYNL---YDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcNPKRSAIKIV 297
Cdd:cd07837    76 gkplLYLVFEYLDTDLkkfIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSH--GVMHRDLKPQNLLV-DKQKGLLKIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 298 DFGSSCQLGQRIYQY---IQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA 373
Cdd:cd07837   153 DLGLGRAFTIPIKSYtheIVTLWYRAPEVLLGSThYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 374 HILDQAPKARKFFEkLPdgtwnlkktkdgkrEYKPPGTRKLhnilgVETGGPGGrragesghtvadylkfKDLILRMLDY 453
Cdd:cd07837   233 EVWPGVSKLRDWHE-YP--------------QWKPQDLSRA-----VPDLEPEG----------------VDLLTKMLAY 276
                         330
                  ....*....|....*..
gi 1113820495 454 DPKTRIQPYYALQHSFF 470
Cdd:cd07837   277 DPAKRISAKAALQHPYF 293
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
148-475 8.61e-30

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 121.21  E-value: 8.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMnKHDTEMKYYIVHLKRHFMFR-N 223
Cdd:cd07880    15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYrpfQSELFAKRAYRELRLLKHM-KHENVIGLLDVFTPDLSLDRfH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNLYDLLRNTNfrgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENilLCNPKRSAIKIVDFGSSC 303
Cdd:cd07880    94 DFYLVMPFMGTDLGKLMKHEK---LSEDRIQFLVYQMLKGLKYIHAA--GIIHRDLKPGN--LAVNEDCELKILDFGLAR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILD--QAP 380
Cdd:cd07880   167 QTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQklQSE 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 381 KARKFFEKLPDgtwnLKKtKDgkreykppgtrkLHNILgvetggpggrragesghTVADYLKFKdLILRMLDYDPKTRIQ 460
Cdd:cd07880   247 DAKNYVKKLPR----FRK-KD------------FRSLL-----------------PNANPLAVN-VLEKMLVLDAESRIT 291
                         330
                  ....*....|....*
gi 1113820495 461 PYYALQHSFFKKTAD 475
Cdd:cd07880   292 AAEALAHPYFEEFHD 306
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
148-475 9.61e-30

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: 120.91  E-value: 9.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK--------IIKNKKAFLnqaqiEVRLLELMnKHDTEMKYYIVHL-KRH 218
Cdd:cd07877    17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKklsrpfqsIIHAKRTYR-----ELRLLKHM-KHENVIGLLDVFTpARS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRntnfrgvSLNLTRKFAQ----QMCTALLFLATPElsIIHCDLKPENilLCNPKRSAI 294
Cdd:cd07877    91 LEEFNDVYLVTHLMGADLNNIVK-------CQKLTDDHVQfliyQILRGLKYIHSAD--IIHRDLKPSN--LAVNEDCEL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 295 KIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA 373
Cdd:cd07877   160 KILDFGLARHTDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 374 HILDQAP--KARKFFEKLPdgtwnlkktkdgkreYKPpgTRKLHNILgvetggpggrrAGESGHTVadylkfkDLILRML 451
Cdd:cd07877   240 ELLKKISseSARNYIQSLT---------------QMP--KMNFANVF-----------IGANPLAV-------DLLEKML 284
                         330       340
                  ....*....|....*....|....
gi 1113820495 452 DYDPKTRIQPYYALQHSFFKKTAD 475
Cdd:cd07877   285 VLDSDKRITAAQALAHAYFAQYHD 308
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
148-469 1.20e-29

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 120.37  E-value: 1.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQAqievrlleLMNKHDTEMKyyivhLKRHFMFRNHLCL 227
Cdd:cd07856    10 TRYSDLQPVGMGAFGLVCSARDQLTGQNVAVK--KIMKPFSTPV--------LAKRTYRELK-----LLKHLRHENIISL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 -------------VFEMLSYNLYDLLRNtnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL---CNpkr 291
Cdd:cd07856    75 sdifisplediyfVTELLGTDLHRLLTS---RPLEKQFIQYFLYQILRGLKYVHSA--GVIHRDLKPSNILVnenCD--- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 292 saIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGI 370
Cdd:cd07856   147 --LKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGT 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 371 PPAHILDQ--APKARKFFEKLPdgtwnlkktkdgKREYKPPGTRklhnilgVETGGPGGrragesghtvadylkfKDLIL 448
Cdd:cd07856   225 PPDDVINTicSENTLRFVQSLP------------KRERVPFSEK-------FKNADPDA----------------IDLLE 269
                         330       340
                  ....*....|....*....|.
gi 1113820495 449 RMLDYDPKTRIQPYYALQHSF 469
Cdd:cd07856   270 KMLVFDPKKRISAAEALAHPY 290
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
148-475 1.26e-29

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: 120.54  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI---EVRLLELMnKHDTEMKYYIVHLK----RHFm 220
Cdd:cd07878    15 ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRtyrELRLLKHM-KHENVIGLLDVFTPatsiENF- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 frNHLCLVFEMLSYNLYDLLRntnFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFG 300
Cdd:cd07878    93 --NEVYLVTNLMGADLNNIVK---CQKLSDEHVQFLIYQLLRGLKYIHSA--GIIHRDLKPSNVAV--NEDCELRILDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 SSCQLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ- 378
Cdd:cd07878   164 LARQADDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKi 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 379 -APKARKFFEKLPDgtwnlKKTKDGKREYKPPgtrklhNILGVetggpggrragesghtvadylkfkDLILRMLDYDPKT 457
Cdd:cd07878   244 sSEHARKYIQSLPH-----MPQQDLKKIFRGA------NPLAI------------------------DLLEKMLVLDSDK 288
                         330
                  ....*....|....*...
gi 1113820495 458 RIQPYYALQHSFFKKTAD 475
Cdd:cd07878   289 RISASEALAHPYFSQYHD 306
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
149-470 4.19e-29

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: 117.53  E-value: 4.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHfmfrnhL 225
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRlddDDEGVPSSALREICLLKELKHKNIVRLYDVLHSDKK------L 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQL 305
Cdd:cd07839    75 TLVFEYCDQDLKKYFDSCNGD-IDPEIVKSFMFQLLKGLAFCH--SHNVLHRDLKPQNLLI--NKNGELKLADFGLARAF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQY---IQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEM-HTGEPLFSGANEVDQMNKIVEVLGIPPAhilDQAP 380
Cdd:cd07839   150 GIPVRCYsaeVVTLWYRPPDVLFGAKlYSTSIDMWSAGCIFAELaNAGRPLFPGNDVDDQLKRIFRLLGTPTE---ESWP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 381 KarkfFEKLPDgtwnlkktkdgkreYKP----PGTRKLHNIlgVETGGPGGRragesghtvadylkfkDLILRMLDYDPK 456
Cdd:cd07839   227 G----VSKLPD--------------YKPypmyPATTSLVNV--VPKLNSTGR----------------DLLQNLLVCNPV 270
                         330
                  ....*....|....
gi 1113820495 457 TRIQPYYALQHSFF 470
Cdd:cd07839   271 QRISAEEALQHPYF 284
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
156-470 8.51e-29

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 116.71  E-value: 8.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnkkafLNQ-------AQIEVRLLE------LMNKHDtemkyyIVHLKRHfmfr 222
Cdd:cd07844     8 LGEGSYATVYKGRSKLTGQLVALKEIR-----LEHeegapftAIREASLLKdlkhanIVTLHD------IIHTKKT---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 nhLCLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFG-- 300
Cdd:cd07844    73 --LTLVFEYLDTDLKQYMDDCG-GGLSMHNVRLFLFQLLRGLAYCH--QRRVLHRDLKPQNLLISE--RGELKLADFGla 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 SSCQLGQRIYQY-IQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEV-DQMNKIVEVLGIPPAhilD 377
Cdd:cd07844   146 RAKSVPSKTYSNeVVTLWYRPPDVLLGsTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVeDQLHKIFRVLGTPTE---E 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 378 QAPKARKFFEKLPDGTwnlkktkdgkREYKPpgtRKLHNILGVETGGPGGrragesghtvadylkfKDLILRMLDYDPKT 457
Cdd:cd07844   223 TWPGVSSNPEFKPYSF----------PFYPP---RPLINHAPRLDRIPHG----------------EELALKFLQYEPKK 273
                         330
                  ....*....|...
gi 1113820495 458 RIQPYYALQHSFF 470
Cdd:cd07844   274 RISAAEAMKHPYF 286
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
143-469 1.76e-28

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 116.06  E-value: 1.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 143 GEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHF 219
Cdd:cd07864     2 GKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRldnEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKQDA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 M-FRNH---LCLVFEMLSYNLYDLLRN--TNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSA 293
Cdd:cd07864    82 LdFKKDkgaFYLVFEYMDHDLMGLLESglVHF---SEDHIKSFMKQLLEGLNYCH--KKNFLHRDIKCSNILLNN--KGQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 IKIVDFGSScqlgqRIYQYIQSR---------FYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNK 363
Cdd:cd07864   155 IKLADFGLA-----RLYNSEESRpytnkvitlWYRPPELLLGEErYGPAIDVWSCGCILGELFTKKPIFQANQELAQLEL 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 364 IVEVLGIPpahildqAPKARKFFEKLPdgTWNLKKTkdgKREYKppgtRKLHNilgvetggpggrragESGHTVADYLkf 443
Cdd:cd07864   230 ISRLCGSP-------CPAVWPDVIKLP--YFNTMKP---KKQYR----RRLRE---------------EFSFIPTPAL-- 276
                         330       340
                  ....*....|....*....|....*.
gi 1113820495 444 kDLILRMLDYDPKTRIQPYYALQHSF 469
Cdd:cd07864   277 -DLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
147-470 4.99e-28

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 115.10  E-value: 4.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK--IIKNKK-AFLNQAQIEVRLLELMNkHDT-----EMKYyiVHLKRH 218
Cdd:cd07866     7 LRDYEILGKLGEGTFGEVYKARQIKTGRVVALKkiLMHNEKdGFPITALREIKILKKLK-HPNvvpliDMAV--ERPDKS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVD 298
Cdd:cd07866    84 KRKRGSVYMVTPYMDHDLSGLLENPSVK-LTESQIKCYMLQLLEGINYLH--ENHILHRDIKAANILIDN--QGILKIAD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FG-------------SSCQLGQRIY-QYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNK 363
Cdd:cd07866   159 FGlarpydgpppnpkGGGGGGTRKYtNLVVTRWYRPPELLLGERrYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 364 IVEVLGIPPAHILdqaPKARkffeKLPdGTWNLKKTKDGKREYKppgtrklhnilgvetggpggRRAGESGHTVADYLKf 443
Cdd:cd07866   239 IFKLCGTPTEETW---PGWR----SLP-GCEGVHSFTNYPRTLE--------------------ERFGKLGPEGLDLLS- 289
                         330       340
                  ....*....|....*....|....*..
gi 1113820495 444 kdlilRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd07866   290 -----KLLSLDPYKRLTASDALEHPYF 311
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
148-389 7.89e-28

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: 115.46  E-value: 7.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLE--LMNKHDTEmkyYIVHLKRHFMFRNHL 225
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILR-KSDMLKREQIAHVRAErdILADADSP---WIVRLHYAFQDEDHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLS----YNL---YDLLRNTnfrgvslnLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVD 298
Cdd:cd05573    77 YLVMEYMPggdlMNLlikYDVFPEE--------TARFYIAELVLALDSLH--KLGFIHRDIKPDNILL--DADGHIKLAD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGSSCQL---GQRIYQYIQSRF-----------------------------YRSPEVLLGMPYDLAIDMWSLGCILVEMH 346
Cdd:cd05573   145 FGLCTKMnksGDRESYLNDSVNtlfqdnvlarrrphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEML 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 347 TGEPLFSGANEVDQMNKIV---EVLGIPPAHilDQAPKARKFFEKL 389
Cdd:cd05573   225 YGFPPFYSDSLVETYSKIMnwkESLVFPDDP--DVSPEAIDLIRRL 268
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
148-366 1.92e-27

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: 111.96  E-value: 1.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII----KNKKAFLN-QAQIEVrLLELmnKHDTemkyyIVHLKRHFMFR 222
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkrgKSEKELRNlRQEIEI-LRKL--NHPN-----IIEMLDSFETK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLSYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFG-- 300
Cdd:cd14002    73 KEFVVVTEYAQGELFQILEDD--GTLPEEEVRSIAKQLVSALHYLHSNR--IIHRDMKPQNILI--GKGGVVKLCDFGfa 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 301 SSCQLGQRIYQYIQ-SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14002   147 RAMSCNTLVLTSIKgTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVK 213
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
150-471 2.27e-27

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: 111.41  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkKAFLNQAQIEVRLL---ELMN--KHDtemkyYIVHLKRHFMFRNH 224
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVIS--KSQLQKSGLEHQLRreiEIQShlRHP-----NILRLYGYFEDKKR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLL-RNTNFrgvSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRsaIKIVDFGSS 302
Cdd:cd14007    75 IYLILEYAPNgELYKELkKQKRF---DEKEAAKYIYQLALALDYLHSK--NIIHRDIKPENILLGSNGE--LKLADFGWS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQLgqriyqyIQSR---F-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVlgippaH 374
Cdd:cd14007   148 VHA-------PSNRrktFcgtldYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNV------D 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 375 IldqapkarKFFEKLPDGtwnlkktkdgkreykppgtrklhnilgvetggpggrragesghtvadylkFKDLILRMLDYD 454
Cdd:cd14007   215 I--------KFPSSVSPE--------------------------------------------------AKDLISKLLQKD 236
                         330
                  ....*....|....*..
gi 1113820495 455 PKTRIQPYYALQHSFFK 471
Cdd:cd14007   237 PSKRLSLEQVLNHPWIK 253
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
156-460 2.83e-27

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: 111.88  E-value: 2.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRLLEL---MNKHDTE---MK----YYIVHLKRHF--MFRN 223
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIF-NKSRLRKRREGKNDRGKIknaLDDVRREiaiMKkldhPNIVRLYEVIddPESD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYN-LYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSS 302
Cdd:cd14008    80 KLYLVLEYCEGGpVMELDSGDRVPPLPEETARKYFRDLVLGLEYLH--ENGIVHRDIKPENLLL--TADGTVKISDFGVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 cQLGQRIYQYIQSR-----FYrSPEVLLG--MPYD-LAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVevlgippah 374
Cdd:cd14008   156 -EMFEDGNDTLQKTagtpaFL-APELCDGdsKTYSgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQ--------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 375 ildqapkarkffeklpdgtwnlkktkDGKREYKPPGTrklhniLGVEtggpggrragesghtvadylkFKDLILRMLDYD 454
Cdd:cd14008   225 --------------------------NQNDEFPIPPE------LSPE---------------------LKDLLRRMLEKD 251

                  ....*.
gi 1113820495 455 PKTRIQ 460
Cdd:cd14008   252 PEKRIT 257
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
147-469 7.84e-27

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 112.87  E-value: 7.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQ-----AQIEVRLLELMNKHDTEMKYYIVHLKRHFMF 221
Cdd:cd07874    16 LKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIK--KLSRPFQNQthakrAYRELVLMKCVNHKNIISLLNVFTPQKSLEE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSYNLYDLLRntnfrgVSLNLTRK--FAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd07874    94 FQDVYLVMELMDANLCQVIQ------MELDHERMsyLLYQMLCGIKHLHSA--GIIHRDLKPSNIVV--KSDCTLKILDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 GSSCQLGQRIYQ--YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIP-PAHIL 376
Cdd:cd07874   164 GLARTAGTSFMMtpYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPcPEFMK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 DQAPKARKFFEKLPdgtwnlkktkdgkrEYKPPGTRKLHnilgvetggPGGRRAGESGHTVADYLKFKDLILRMLDYDPK 456
Cdd:cd07874   244 KLQPTVRNYVENRP--------------KYAGLTFPKLF---------PDSLFPADSEHNKLKASQARDLLSKMLVIDPA 300
                         330
                  ....*....|...
gi 1113820495 457 TRIQPYYALQHSF 469
Cdd:cd07874   301 KRISVDEALQHPY 313
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
143-471 1.09e-26

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 111.79  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 143 GEKWMDRYEIdsliGKGSFGQVVKAYDRVEQEWVAIK-IIKNKKAFLNQAQIEVRLLELMNkHDTEMKYYIV-------- 213
Cdd:cd07854     4 GSRYMDLRPL----GCGSNGLVFSAVDSDCDKRVAVKkIVLTDPQSVKHALREIKIIRRLD-HDNIVKVYEVlgpsgsdl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 214 --HLKRHFMFRNhLCLVFEMLSYNLYDLLRNTNfrgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcNPKR 291
Cdd:cd07854    79 teDVGSLTELNS-VYIVQEYMETDLANVLEQGP---LSEEHARLFMYQLLRGLKYIHSA--NVLHRDLKPANVFI-NTED 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 292 SAIKIVDFGSSCQLGQR------IYQYIQSRFYRSPEVLLGmP--YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNK 363
Cdd:cd07854   152 LVLKIGDFGLARIVDPHyshkgyLSEGLVTKWYRSPRLLLS-PnnYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 364 IVEvlGIPPAHILDQAPKARKFFEKLPDGTWNLKktkdgkreykppgtRKLHNILgvetggpggrrAGESGHTVadylkf 443
Cdd:cd07854   231 ILE--SVPVVREEDRNELLNVIPSFVRNDGGEPR--------------RPLRDLL-----------PGVNPEAL------ 277
                         330       340
                  ....*....|....*....|....*...
gi 1113820495 444 kDLILRMLDYDPKTRIQPYYALQHSFFK 471
Cdd:cd07854   278 -DFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
149-389 1.25e-26

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: 109.87  E-value: 1.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQA-----QIEVRLLELMNkHDTemkyyIVHLKRHFMFRN 223
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKnlqlfQREINILKSLE-HPG-----IVRLIDWYEDDQ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSAIKIVDFGSS 302
Cdd:cd14098    75 HIYLVMEYVEGgDLMDFI--MAWGAIPEQHARELTKQILEAMAYTHS--MGITHRDLKPENILITQDDPVIVKISDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 --CQLGQRIYQYIQSRFYRSPEVLLGMP------YDLAIDMWSLGCILVEMHTGEPLFSGanevDQMNKIVEVLG----- 369
Cdd:cd14098   151 kvIHTGTFLVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDG----SSQLPVEKRIRkgryt 226
                         250       260
                  ....*....|....*....|
gi 1113820495 370 IPPAHILDQAPKARKFFEKL 389
Cdd:cd14098   227 QPPLVDFNISEEAIDFILRL 246
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
147-469 1.80e-26

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 111.66  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQAQIE-----------------VRLLELMNKHDTEMK 209
Cdd:cd07876    20 LKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVK--KLSRPFQNQTHAKrayrelvllkcvnhkniISLLNVFTPQKSLEE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 210 YYIVHLKRHFMFRN-----HLCLVFEMLSYNLYdllrntnfrgvslnltrkfaqQMCTALLFLATPelSIIHCDLKPENI 284
Cdd:cd07876    98 FQDVYLVMELMDANlcqviHMELDHERMSYLLY---------------------QMLCGIKHLHSA--GIIHRDLKPSNI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 285 LLcnPKRSAIKIVDFG--SSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMN 362
Cdd:cd07876   155 VV--KSDCTLKILDFGlaRTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWN 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 363 KIVEVLGIPPAHILDQ-APKARKFFEKLPdgtwnlkktkdgkreyKPPGtrklhniLGVETGGPGGRRAGESGHTVADYL 441
Cdd:cd07876   233 KVIEQLGTPSAEFMNRlQPTVRNYVENRP----------------QYPG-------ISFEELFPDWIFPSESERDKLKTS 289
                         330       340
                  ....*....|....*....|....*...
gi 1113820495 442 KFKDLILRMLDYDPKTRIQPYYALQHSF 469
Cdd:cd07876   290 QARDLLSKMLVIDPDKRISVDEALRHPY 317
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
150-356 2.61e-26

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: 108.81  E-value: 2.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVE--QEWVAIKIIKNKKA---FLNQ---AQIEVrLLELMNKHdtemkyyIVHLKRHFMF 221
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKSglKEKVACKIIDKKKApkdFLEKflpRELEI-LRKLRHPN-------IIQVYSIFER 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEmlsynlY----DLLRNTNFRG-VSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKI 296
Cdd:cd14080    74 GSKVFIFME------YaehgDLLEYIQKRGaLSESQARIWFRQLALAVQYLH--SLDIAHRDLKCENILLD--SNNNVKL 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 297 VDFGSSCQLGQRIYQ-----YIQSRFYRSPEVLLGMPYDLAI-DMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14080   144 SDFGFARLCPDDDGDvlsktFCGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMPFDDSN 209
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
156-364 2.73e-26

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: 108.53  E-value: 2.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQ-EWVAIKIIKNKKafLNQAQIEVRLLE--LMNKHDTEmkyYIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd14121     3 LGSGTYATVYKAYRKSGArEVVAVKCVSKSS--LNKASTENLLTEieLLKKLKHP---HIVELKDFQWDEEHIYLIMEYC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SY-NLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQL--GQRI 309
Cdd:cd14121    78 SGgDLSRFIRS--RRTLPESTVRRFLQQLASALQFLR--EHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLkpNDEA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 310 YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd14121   154 HSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKI 208
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
156-389 3.03e-26

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: 108.84  E-value: 3.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEvrllELMNKHDTEMKY---YIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIK-KRDMIRKNQVD----SVLAERNILSQAqnpFVVKLYYSFQGKKNLYLVMEYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SY-NLYDLLRNTNfrgvSL--NLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ--LGQ 307
Cdd:cd05579    76 PGgDLYSLLENVG----ALdeDVARIYIAEIVLALEYLH--SHGIIHRDLKPDNILI--DANGHLKLTDFGLSKVglVRR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIYQYIQSRF----------------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVlGIP 371
Cdd:cd05579   148 QIKLSIQKKSngapekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNG-KIE 226
                         250
                  ....*....|....*...
gi 1113820495 372 PAHILDQAPKARKFFEKL 389
Cdd:cd05579   227 WPEDPEVSDEAKDLISKL 244
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
147-469 4.31e-26

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 110.52  E-value: 4.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQ-----AQIEVRLLELMNKHDTEMKYYIVHLKRHFMF 221
Cdd:cd07875    23 LKRYQNLKPIGSGAQGIVCAAYDAILERNVAIK--KLSRPFQNQthakrAYRELVLMKCVNHKNIIGLLNVFTPQKSLEE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSYNLYDLLRntnfrgVSLNLTRK--FAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd07875   101 FQDVYIVMELMDANLCQVIQ------MELDHERMsyLLYQMLCGIKHLHSA--GIIHRDLKPSNIVV--KSDCTLKILDF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 GSSCQLGQRIYQ--YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIP-PAHIL 376
Cdd:cd07875   171 GLARTAGTSFMMtpYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPcPEFMK 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 DQAPKARKFFEKLPdgtwnlkktkdgkrEYKPPGTRKLHnilgvetggPGGRRAGESGHTVADYLKFKDLILRMLDYDPK 456
Cdd:cd07875   251 KLQPTVRTYVENRP--------------KYAGYSFEKLF---------PDVLFPADSEHNKLKASQARDLLSKMLVIDAS 307
                         330
                  ....*....|...
gi 1113820495 457 TRIQPYYALQHSF 469
Cdd:cd07875   308 KRISVDEALQHPY 320
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
149-366 5.45e-26

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: 107.70  E-value: 5.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII---KNKKAFLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQIsleKIPKSDLKSVMGEIDLLKKLN-HP-----NIVKYIGSVKTKDSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFE-MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ 304
Cdd:cd06627    75 YIILEyVENGSLASIIKK--FGKFPESLVAVYIYQVLEGLAYLH--EQGVIHRDIKGANILT--TKDGLVKLADFGVATK 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 305 LG---QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd06627   149 LNeveKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQ 213
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
149-364 5.59e-26

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: 107.86  E-value: 5.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKafLNQAQI-----EVRLLELMNKHdtemkyYIVHLKRHFMFRN 223
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGS--LSQKERedsvnEIRLLASVNHP------NIIRYKEAFLDGN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTNFRGVSL--NLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPkrSAIKIVDFG 300
Cdd:cd08530    73 RLCIVMEYAPFgDLSKLISKRKKKRRLFpeDDIWRIFIQMLRGLKALH--DQKILHRDLKSANILLSAG--DLVKIGDLG 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 301 SSCQL-GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd08530   149 ISKVLkKNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKV 213
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
149-470 7.11e-26

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: 108.20  E-value: 7.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYD---------------RVEQEWVAIKIIKNKKAFLNQAQIE----VRLLEL--MNKHDTE 207
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDlknggrfvalkrvrvQTGEEGMPLSTIREVAVLRHLETFEhpnvVRLFDVctVSRTDRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 208 MKyyivhlkrhfmfrnhLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLC 287
Cdd:cd07862    82 TK---------------LTLVFEHVDQDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHR--VVHRDLKPQNILVT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 288 NPKRsaIKIVDFGSScqlgqRIYQY-------IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd07862   145 SSGQ--IKLADFGLA-----RIYSFqmaltsvVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQ 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 361 MNKIVEVLGIPPAhildqapkarkffEKLPDGTwNLKKTKDGKREYKPpgtrklhnilgVETGGPGGRRAGesghtvady 440
Cdd:cd07862   218 LGKILDVIGLPGE-------------EDWPRDV-ALPRQAFHSKSAQP-----------IEKFVTDIDELG--------- 263
                         330       340       350
                  ....*....|....*....|....*....|
gi 1113820495 441 lkfKDLILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd07862   264 ---KDLLLKCLTFNPAKRISAYSALSHPYF 290
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
156-391 1.29e-25

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 108.07  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnkKAFLNQ------AQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHLCLVF 229
Cdd:cd05570     3 LGKGSFGKVMLAERKKTDELYAIKVLK--KEVIIEdddvecTMTEKRVLALANRHP-----FLTGLHACFQTEDRLYFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSsCQLGQ 307
Cdd:cd05570    76 EYVNGGdlMFHIQRARRF---TEERARFYAAEICLALQFLH--ERGIIYRDLKLDNVLLDA--EGHIKIADFGM-CKEGI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RiYQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPK- 381
Cdd:cd05570   148 W-GGNTTSTFcgtpdYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSi 226
                         250
                  ....*....|
gi 1113820495 382 ARKFFEKLPD 391
Cdd:cd05570   227 LKGLLTKDPA 236
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
156-389 4.43e-25

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: 105.38  E-value: 4.43e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQ----IEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLCLVFE- 230
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQehifSEKEILEECN-SP-----FIVKLYRTFKDKKYLYMLMEy 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSYNLYDLLRNtnfRGvSLNltrKFAQQMCTALLFLATPEL---SIIHCDLKPENILLcnPKRSAIKIVDFGSSCQL-- 305
Cdd:cd05572    75 CLGGELWTILRD---RG-LFD---EYTARFYTACVVLAFEYLhsrGIIYRDLKPENLLL--DSNGYVKLVDFGFAKKLgs 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEvDQM------NKIVEVLGIPPahILDQA 379
Cdd:cd05572   146 GRKTWTFCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDE-DPMkiyniiLKGIDKIEFPK--YIDKN 222
                         250
                  ....*....|
gi 1113820495 380 pkARKFFEKL 389
Cdd:cd05572   223 --AKNLIKQL 230
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
148-356 8.69e-25

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: 104.78  E-value: 8.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK-------AFLNQAQIEvRLLELMNKHDTEmkyYIVHLKRHFM 220
Cdd:cd14084     6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrrEINKPRNIE-TEIEILKKLSHP---CIIKIEDFFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNHLCLVFE-MLSYNLYDllRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLC-NPKRSAIKIVD 298
Cdd:cd14084    82 AEDDYYIVLElMEGGELFD--RVVSNKRLKEAICKLYFYQMLLAVKYLH--SNGIIHRDLKPENVLLSsQEEECLIKITD 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 299 FGSSCQLGQRiyQYIQSR----FYRSPEVLL---GMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14084   158 FGLSKILGET--SLMKTLcgtpTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEY 220
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
156-367 9.50e-25

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: 103.89  E-value: 9.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDR-VEQEWVAiKIIKNKKAFLNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNHLCLVFEMLSY 234
Cdd:cd14006     1 LGRGRFGVVKRCIEKaTGREFAA-KFIPKRDKKKEAVLREISILNQL-QHPR-----IIQLHEAYESPTELVLILELCSG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NlyDLLRNTNFRG-VSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYI 313
Cdd:cd14006    74 G--ELLDRLAERGsLSEEEVRTYMRQLLEGLQYLH--NHHILHLDLKPENILLADRPSPQIKIIDFGLARKLNPGEELKE 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 314 Q--SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV 367
Cdd:cd14006   150 IfgTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISAC 205
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
150-378 1.37e-24

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: 103.65  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-KNKKAFLNQAQI--EVRLLELMNkHDTEMKYYIV---HLKrhfmfrn 223
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIdKTKLDDVSKAHLfqEVRCMKLVQ-HPNVVRLYEVidtQTK------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 hLCLVFEM-LSYNLYD-LLRNTNfrGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpKRSAIKIVDFGS 301
Cdd:cd14074    77 -LYLILELgDGGDMYDyIMKHEN--GLNEDLARKYFRQIVSAISYCH--KLHVVHRDLKPENVVFFE-KQGLVKLTDFGF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQL--GQRIYQYIQSRFYRSPEVLLGMPYDL-AIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ 378
Cdd:cd14074   151 SNKFqpGEKLETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPE 230
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
156-470 1.57e-24

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 104.27  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKII--KNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFrnhlclVFEMLS 233
Cdd:cd07870     8 LGEGSYATVYKGISRINGQLVALKVIsmKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTF------VFEYMH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRNtNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNpkRSAIKIVDFG---SSCQLGQRIY 310
Cdd:cd07870    82 TDLAQYMIQ-HPGGLHPYNVRLFMFQLLRGLAYIHGQH--ILHRDLKPQNLLISY--LGELKLADFGlarAKSIPSQTYS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 311 QYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSG-ANEVDQMNKIVEVLGIPpahildqapkarkffek 388
Cdd:cd07870   157 SEVVTLWYRPPDVLLGaTDYSSALDIWGAGCIFIEMLQGQPAFPGvSDVFEQLEKIWTVLGVP----------------- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 389 lPDGTW-NLKKTKDGKRE-YKPPGTRKLHNILgvetggpggRRAGESGHTvadylkfKDLILRMLDYDPKTRIQPYYALQ 466
Cdd:cd07870   220 -TEDTWpGVSKLPNYKPEwFLPCKPQQLRVVW---------KRLSRPPKA-------EDLASQMLMMFPKDRISAQDALL 282

                  ....
gi 1113820495 467 HSFF 470
Cdd:cd07870   283 HPYF 286
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
156-470 2.02e-24

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 103.94  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHfmfrnhLCLVFEMLS 233
Cdd:cd07871    13 LGEGTYATVFKGRSKLTENLVALKEIRleHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERC------LTLVFEYLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFG--SSCQLGQRIY- 310
Cdd:cd07871    87 SDLKQYLDNCG-NLMSMHNVKIFMFQLLRGLSYCH--KRKILHRDLKPQNLLI--NEKGELKLADFGlaRAKSVPTKTYs 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 311 QYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahildqapkarkffekl 389
Cdd:cd07871   162 NEVVTLWYRPPDVLLGsTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTP------------------ 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 390 PDGTWNLKKTKDGKREYKPPGTRK---LHNILGVETGGpggrragesghtvadylkfKDLILRMLDYDPKTRIQPYYALQ 466
Cdd:cd07871   224 TEETWPGVTSNEEFRSYLFPQYRAqplINHAPRLDTDG-------------------IDLLSSLLLYETKSRISAEAALR 284

                  ....
gi 1113820495 467 HSFF 470
Cdd:cd07871   285 HSYF 288
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
149-478 5.64e-24

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 103.83  E-value: 5.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNkHDTEMKYYIVHLKRHFMfrNHL 225
Cdd:cd07879    16 RYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpfQSEIFAKRAYRELTLLKHMQ-HENVIGLLDVFTSAVSG--DEF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRntnFRGVSL--NLTRKFAQQMCTALLFLATPelSIIHCDLKPENilLCNPKRSAIKIVDFGSSC 303
Cdd:cd07879    93 QDFYLVMPYMQTDLQK---IMGHPLseDKVQYLVYQMLCGLKYIHSA--GIIHRDLKPGN--LAVNEDCELKILDFGLAR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahildqapkA 382
Cdd:cd07879   166 HADAEMTGYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVP----------G 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 383 RKFFEKLPDgtwnlkktKDGKREYK--PPGTRKLHNILgVETGGPGGrragesghtvadylkfKDLILRMLDYDPKTRIQ 460
Cdd:cd07879   236 PEFVQKLED--------KAAKSYIKslPKYPRKDFSTL-FPKASPQA----------------VDLLEKMLELDVDKRLT 290
                         330       340
                  ....*....|....*....|
gi 1113820495 461 PYYALQHSFFK--KTADEGT 478
Cdd:cd07879   291 ATEALEHPYFDsfRDADEET 310
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
151-372 1.22e-23

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: 101.13  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIevrLLELMNKHDTEMKYyIVHLKRHFMFRNHLCLVFE 230
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRKQL---LRELKTLRSCESPY-VVKCYGAFYKEGEISIVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 -MLSYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLcNpKRSAIKIVDFGSSCQLGQRI 309
Cdd:cd06623    80 yMDGGSLADLLKKV--GKIPEPVLAYIARQILKGLDYLHT-KRHIIHRDIKPSNLLI-N-SKGEVKIADFGISKVLENTL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 310 YQ---YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPP 372
Cdd:cd06623   155 DQcntFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPP 220
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
150-470 1.45e-23

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: 100.79  E-value: 1.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA----FLNQAQIEVRLLELMNkHDTEMKYYIVhlkrhFMFRNHL 225
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLskesVLMKVEREIAIMKLIE-HPNVLKLYDV-----YENKKYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFG--SS 302
Cdd:cd14081    77 YLVLEYVSGgELFDYLVKK--GRLTEKEARKFFRQIISALDYCH--SHSICHRDLKPENLLL--DEKNNIKIADFGmaSL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQLGQRIYQYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGANevdqmnkivevlgippahildqapk 381
Cdd:cd14081   151 QPEGSLLETSCGSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFDDDN------------------------- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 382 ARKFFEKLPDGTWNLKktkdgkrEYKPPGTrklhnilgvetggpggrragesghtvadylkfKDLILRMLDYDPKTRIQP 461
Cdd:cd14081   206 LRQLLEKVKRGVFHIP-------HFISPDA--------------------------------QDLLRRMLEVNPEKRITI 246

                  ....*....
gi 1113820495 462 YYALQHSFF 470
Cdd:cd14081   247 EEIKKHPWF 255
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
150-356 1.95e-23

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: 100.31  E-value: 1.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-------KNKKAFLNqaqiEVRLL-ELmnKHDTEMKYY--IVHLKRHF 219
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIdygkmseKEKQQLVS----EVNILrEL--KHPNIVRYYdrIVDRANTT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFrnhlcLVFEmlsY----NLYDLLRN--TNFRGVSLNLTRKFAQQMCTALLFLATPELS---IIHCDLKPENILLCnpK 290
Cdd:cd08217    76 LY-----IVME---YceggDLAQLIKKckKENQYIPEEFIWKIFTQLLLALYECHNRSVGggkILHRDLKPANIFLD--S 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 291 RSAIKIVDFGSSCQLGQRIYQ---YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd08217   146 DNNVKLGDFGLARVLSHDSSFaktYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAAN 214
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
150-364 4.81e-23

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: 99.26  E-value: 4.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNqaqIEvRLLELMNKHDTEmkyYIVHLKRHFMFRNHLCLVF 229
Cdd:cd06612     5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQE---II-KEISILKQCDSP---YIVKYYGSYFKNTDLWIVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYN-LYDLLRNTNFRgvslnLTRK----FAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ 304
Cdd:cd06612    78 EYCGAGsVSDIMKITNKT-----LTEEeiaaILYQTLKGLEYLHS--NKKIHRDIKAGNILL--NEEGQAKLADFGVSGQ 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 305 LGQRIYQ---YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd06612   149 LTDTMAKrntVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMI 211
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
150-365 4.87e-23

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 99.02  E-value: 4.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIK---IIKNKKAFLNQAQIEVRLLELMNkHDTEMKYYivhlkRHFMFRNHLC 226
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKqidISRMSRKMREEAIDEARVLSKLN-SPYVIKYY-----DSFVDKGKLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQL 305
Cdd:cd08529    76 IVMEYAENgDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKK--ILHRDIKSMNIFL--DKGDNVKIGDLGVAKIL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 306 GQRI---YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd08529   152 SDTTnfaQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIV 214
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
156-350 7.29e-23

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: 98.44  E-value: 7.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKII----KNKKAFLNqaqiEVRLLElMNKHDTEMKYYIVHLkrhfmFRNHLCLVFEM 231
Cdd:cd06614     8 IGEGASGEVYKATDRATGKEVAIKKMrlrkQNKELIIN----EILIMK-ECKHPNIVDYYDSYL-----VGDELWVVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYN-LYDLLRNTNFRgvsLNLTR--KFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQR 308
Cdd:cd06614    78 MDGGsLTDIITQNPVR---MNESQiaYVCREVLQGLEYLHS--QNVIHRDIKSDNILL--SKDGSVKLADFGFAAQLTKE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1113820495 309 IyqyiQSR-------FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06614   151 K----SKRnsvvgtpYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEP 195
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
149-359 1.10e-22

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: 98.19  E-value: 1.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK-----NKKAFLNQAQI---EVRLLELMNKHDtemkyYIVHLKRHFM 220
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYksgpnSKDGNDFQKLPqlrEIDLHRRVSRHP-----NIITLHDVFE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNHLCLVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSaIKIVDF 299
Cdd:cd13993    76 TEVAIYIVLEYCPNgDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCH--SLGIYHRDIKPENILLSQDEGT-VKLCDF 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 300 GSSCQlgQRI-YQY-IQSRFYRSPEVL-----LGMPYD-LAIDMWSLGCILVEMHTGEPLFSGANEVD 359
Cdd:cd13993   153 GLATT--EKIsMDFgVGSEFYMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPWKIASESD 218
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
151-477 2.09e-22

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: 99.82  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFLNQAQI-----EVRLLELMnKHDTEMKYYIVHLKRHFMFRNHL 225
Cdd:cd07853     3 EPDRPIGYGAFGVVWSVTDPRDGKRVALK--KMPNVFQNLVSCkrvfrELKMLCFF-KHDNVLSALDILQPPHIDPFEEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRsaIKIVDFG----- 300
Cdd:cd07853    80 YVVTELMQSDLHKIIVSP--QPLSSDHVKVFLYQILRGLKYLHSA--GILHRDIKPGNLLVNSNCV--LKICDFGlarve 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 ---SSCQLGQRIYqyiqSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPahiL 376
Cdd:cd07853   154 epdESKHMTQEVV----TQYYRAPEILMGSRhYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPS---L 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 377 DQAPKARkffeklpdgtwnlkktkDGKREY------KPPGTRKLHNILGVETggpggrragesgHTVAdylkfkDLILRM 450
Cdd:cd07853   227 EAMRSAC-----------------EGARAHilrgphKPPSLPVLYTLSSQAT------------HEAV------HLLCRM 271
                         330       340
                  ....*....|....*....|....*..
gi 1113820495 451 LDYDPKTRIQPYYALQHSFFkktaDEG 477
Cdd:cd07853   272 LVFDPDKRISAADALAHPYL----DEG 294
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
156-392 2.10e-22

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: 97.75  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKII-KNKKAFLNQaqiEVRLLELMnKHDTEMKYYivhlkRHFMFRNHLCLVFEM-LS 233
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTIEFVAIKCVdKSKRPEVLN---EVRLTHEL-KHPNVLKFY-----EWYETSNHLWLVVEYcTG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQLGQRIYQYI 313
Cdd:cd14010    79 GDLETLLRQD--GNLPESSVRKFGRDLVRGLHYIHS--KGIIYCDLKPSNILLDGNGT--LKLSDFGLARREGEILKELF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 314 Q-------------------SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEvlGIPPAH 374
Cdd:cd14010   153 GqfsdegnvnkvskkqakrgTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILN--EDPPPP 230
                         250
                  ....*....|....*...
gi 1113820495 375 ILDQAPKARKFFEKLPDG 392
Cdd:cd14010   231 PPKVSSKPSPDFKSLLKG 248
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
156-407 2.15e-22

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: 97.55  E-value: 2.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSY- 234
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIKVLK-KSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSS--CQLGQRIYQY 312
Cdd:cd05611    83 DCASLIKTLG--GLPEDWAKQYIAEVVLGVEDLH--QRGIIHRDIKPENLLIDQ--TGHLKLTDFGLSrnGLEKRHNKKF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 313 IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSgANEVDQMNKIVE--VLGIPPAHILDQAPKARKFFEKLP 390
Cdd:cd05611   157 VGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFH-AETPDAVFDNILsrRINWPEEVKEFCSPEAVDLINRLL 235
                         250
                  ....*....|....*..
gi 1113820495 391 DGTWNLKKTKDGKREYK 407
Cdd:cd05611   236 CMDPAKRLGANGYQEIK 252
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
156-470 3.98e-22

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 97.38  E-value: 3.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHfmfrnhLCLVFEMLS 233
Cdd:cd07873    10 LGEGTYATVYKGRSKLTDNLVALKEIRleHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKS------LTLVFEYLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRNTnfrGVSLNL--TRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFG--SSCQLGQRI 309
Cdd:cd07873    84 KDLKQYLDDC---GNSINMhnVKLFLFQLLRGLAYCHRRK--VLHRDLKPQNLLI--NERGELKLADFGlaRAKSIPTKT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 310 Y-QYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahildqapkarkffe 387
Cdd:cd07873   157 YsNEVVTLWYRPPDILLGsTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTP---------------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 388 klPDGTWNLKKTKDGKREYKPPGTRK--LHNilgvetggpGGRRAGESGhtvadylkfKDLILRMLDYDPKTRIQPYYAL 465
Cdd:cd07873   221 --TEETWPGILSNEEFKSYNYPKYRAdaLHN---------HAPRLDSDG---------ADLLSKLLQFEGRKRISAEEAM 280

                  ....*
gi 1113820495 466 QHSFF 470
Cdd:cd07873   281 KHPYF 285
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
149-366 4.81e-22

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 96.85  E-value: 4.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHLCLV 228
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRN------ILRLHESFESHEELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLS-YNLYDLLRNTNFRGVSLNLTrKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQL-- 305
Cdd:cd14104    75 FEFISgVDIFERITTARFELNEREIV-SYVRQVCEALEFLHSK--NIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLkp 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 306 GQRI-YQYIQSRFYrSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14104   152 GDKFrLQYTSAEFY-APEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRN 212
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
149-356 6.13e-22

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: 95.92  E-value: 6.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK----AFLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNH 224
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKiedeQDMVRIRREIEIMSSLN-HP-----HIIRIYEVFENKDK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL---CNpkrsaIKIVDFG 300
Cdd:cd14073    76 IVIVMEYASGgELYDYISER--RRLPEREARRIFRQIVSAVHYCH--KNGVVHRDLKLENILLdqnGN-----AKIADFG 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 301 SS--CQLGQRIYQYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14073   147 LSnlYSKDKLLQTFCGSPLYASPEIVNGTPYQgPEVDCWSLGVLLYTLVYGTMPFDGSD 205
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
156-355 8.04e-22

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: 95.84  E-value: 8.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGqVVKAYDRVEQE---WVAIKIIKNKKAFLNQAQIEVRLLE-------LMNKHDTEMKYYIVHLKRHFmfrnhl 225
Cdd:cd13994     1 IGKGATS-VVRIVTKKNPRsgvLYAVKEYRRRDDESKRKDYVKRLTSeyiisskLHHPNIVKVLDLCQDLHGKW------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLS-YNLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQ 304
Cdd:cd13994    74 CLVMEYCPgGDLFTLIEKAD--SLSLEEKDCFFKQILRGVAYLH--SHGIAHRDLKPENILLD--EDGVLKLTDFGTAEV 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 305 LG-----QRIYQY--IQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGA 355
Cdd:cd13994   148 FGmpaekESPMSAglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPWRSA 206
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
149-330 1.03e-21

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: 95.60  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAfLNQAQIEVRLLELMNKHD--TEMKYYIVHLKRHFMfrnhlc 226
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSK-HPQLEYEAKVYKLLQGGPgiPRLYWFGQEGDYNVM------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 lVFEMLSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL-CNPKRSAIKIVDFGSscql 305
Cdd:cd14016    74 -VMDLLGPSLEDLFNKCGRK-FSLKTVLMLADQMISRLEYLH--SKGYIHRDIKPENFLMgLGKNSNKVYLIDFGL---- 145
                         170       180
                  ....*....|....*....|....*
gi 1113820495 306 gqriyqyiqSRFYRSPEVLLGMPYD 330
Cdd:cd14016   146 ---------AKKYRDPRTGKHIPYR 161
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
156-350 1.13e-21

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: 95.45  E-value: 1.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNkHDTEMKYYIVHLkrHfmfRNHLCLVFEML 232
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIRfqdNDPKTIKEIADEMKVLEGLD-HPNLVRYYGVEV--H---REEVYIFMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQ 311
Cdd:cd06626    82 QEgTLEELLRHG--RILDEAVIRVYTLQLLEGLAYLH--ENGIVHRDIKPANIFL--DSNGLIKLGDFGSAVKLKNNTTT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1113820495 312 YIQSRF--------YRSPEVLLG---MPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06626   156 MAPGEVnslvgtpaYMAPEVITGnkgEGHGRAADIWSLGCVVLEMATGKR 205
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
155-379 3.27e-21

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 93.96  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKII----KNKKAF--LNQAQIEVRLLELMNkHDTEMKYYIVhLKRhfmfRNHLCLV 228
Cdd:cd06625     7 LLGQGAFGQVYLCYDADTGRELAVKQVeidpINTEASkeVKALECEIQLLKNLQ-HERIVQYYGC-LQD----EKSLSIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSY-NLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILlcnpkRSA---IKIVDFGSSCQ 304
Cdd:cd06625    81 MEYMPGgSVKDEIKAYG--ALTENVTRKYTRQILEGLAYLHSNM--IVHRDIKGANIL-----RDSngnVKLGDFGASKR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 L-----GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIP--PAHILD 377
Cdd:cd06625   152 LqticsSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPqlPPHVSE 231

                  ..
gi 1113820495 378 QA 379
Cdd:cd06625   232 DA 233
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
150-366 4.86e-21

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: 94.18  E-value: 4.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQI-----EVRLLELMNkHDtemkyYIVHLKRHFMFRNH 224
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILK-KAKIIKLKQVehvlnEKRILSEVR-HP-----FIVNLLGSFQDDRN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTN-FrgvSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCnpKRSAIKIVDFGSS 302
Cdd:cd05580    76 LYMVMEYVPGgELFSLLRRSGrF---PNDVAKFYAAEVVLALEYLHS--LDIVYRDLKPENLLLD--SDGHIKITDFGFA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 303 CQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05580   149 KRVKDRTYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILE 212
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
148-353 7.56e-21

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 93.14  E-value: 7.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKR-HFMFRNHLC 226
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIKKdPPGGDDQLW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTNFRGVSL--NLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGSSC 303
Cdd:cd06608    86 LVMEYCGGgSVTDLVKGLRKKGKRLkeEWIAYILRETLRGLAYLH--ENKVIHRDIKGQNILLTEEAE--VKLVDFGVSA 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 304 QLG---QRIYQYIQSRFYRSPEVLLGM-----PYDLAIDMWSLGCILVEMHTGEPLFS 353
Cdd:cd06608   162 QLDstlGRRNTFIGTPYWMAPEVIACDqqpdaSYDARCDVWSLGITAIELADGKPPLC 219
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-366 9.78e-21

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 92.43  E-value: 9.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI--EVRLLELMnKHDTemkyyIVHLKRHFMFRNHL 225
Cdd:cd14083     3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKEDSLenEIAVLRKI-KHPN-----IVQLLDIYESKSHL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLS-YNLYDLLRNtnfRGvslNLTRKFA----QQMCTALLFLAtpELSIIHCDLKPENILLCNP-KRSAIKIVDF 299
Cdd:cd14083    77 YLVMELVTgGELFDRIVE---KG---SYTEKDAshliRQVLEAVDYLH--SLGIVHRDLKPENLLYYSPdEDSKIMISDF 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 300 G-SSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14083   149 GlSKMEDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILK 216
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
150-345 1.01e-20

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: 92.74  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI--EVRLL-ELMNKHdtemkyyIVHLkrHFMFRNHLC 226
Cdd:cd13996     8 FEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVlrEVKALaKLNHPN-------IVRY--YTAWVEEPP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEM---LSYNLYDLLRNTN-----FRGVSLNLTRkfaqQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSaIKIVD 298
Cdd:cd13996    79 LYIQMelcEGGTLRDWIDRRNsssknDRKLALELFK----QILKGVSYIH--SKGIVHRDLKPSNIFLDNDDLQ-VKIGD 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 299 FGSSCQLGQ-------------RIYQYIQSR----FYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd13996   152 FGLATSIGNqkrelnnlnnnnnGNTSNNSVGigtpLYASPEQLDGENYNEKADIYSLGIILFEM 215
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
156-471 1.52e-20

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 93.13  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHfmfrnhLCLVFEMLS 233
Cdd:cd07872    14 LGEGTYATVFKGRSKLTENLVALKEIRleHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKS------LTLVFEYLD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFG--SSCQLGQRIY- 310
Cdd:cd07872    88 KDLKQYMDDCG-NIMSMHNVKIFLYQILRGLAYCH--RRKVLHRDLKPQNLLI--NERGELKLADFGlaRAKSVPTKTYs 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 311 QYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPpahildqapkarkffekl 389
Cdd:cd07872   163 NEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTP------------------ 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 390 PDGTWNLKKTKDGKREYKPPGTRKLHNIlgveTGGPggrRAGESGhtvadylkfKDLILRMLDYDPKTRIQPYYALQHSF 469
Cdd:cd07872   225 TEETWPGISSNDEFKNYNFPKYKPQPLI----NHAP---RLDTEG---------IELLTKFLQYESKKRISAEEAMKHAY 288

                  ..
gi 1113820495 470 FK 471
Cdd:cd07872   289 FR 290
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
148-416 1.54e-20

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 92.79  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNK-KAFLNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHLC 226
Cdd:cd06644    12 EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKsEEELEDYMVEIEILATCNHP------YIVKLLGAFYWDGKLW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQ-- 304
Cdd:cd06644    86 IMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHS--MKIIHRDLKAGNVLLT--LDGDIKLADFGVSAKnv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 -LGQRIYQYIQSRFYRSPEVLL-----GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEvlGIPPAhiLDQ 378
Cdd:cd06644   162 kTLQRRDSFIGTPYWMAPEVVMcetmkDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAK--SEPPT--LSQ 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1113820495 379 APKARKFFEKLpdgtwnLKKTKDGKREYKPPGTRKLHN 416
Cdd:cd06644   238 PSKWSMEFRDF------LKTALDKHPETRPSAAQLLEH 269
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
156-357 2.39e-20

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


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 92.83  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQ-----AQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05592     3 LGKGSFGKVMLAELKGTNQYFAIKALK-KDVVLEDddvecTMIERRVLALASQHP-----FLTHLFCTFQTESHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLsyNLYDLLRNTNFRG-VSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQlgQRI 309
Cdd:cd05592    77 YL--NGGDLMFHIQQSGrFDEDRARFYGAEIICGLQFLHSR--GIIYRDLKLDNVLL--DREGHIKIADFGM-CK--ENI 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 310 YQYIQ-SRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANE 357
Cdd:cd05592   148 YGENKaSTFcgtpdYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDE 201
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
156-389 2.90e-20

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: 91.43  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQ----AQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHLCLVFEM 231
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKgetmALNEKIILEKVSSP------FIVSLAYAFETKDKLCLVLTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 -----LSYNLYdllrNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQL- 305
Cdd:cd05577    75 mnggdLKYHIY----NVGTRGFSEARAIFYAAEIICGLEHLH--NRFIVYRDLKPENILL--DDHGHVRISDLGLAVEFk 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 -GQRIYQYIQSRFYRSPEVLL-GMPYDLAIDMWSLGCILVEMHTGEPLFSG------ANEVDQMnkiveVLGIPPAHILD 377
Cdd:cd05577   147 gGKKIKGRVGTHGYMAPEVLQkEVAYDFSVDWFALGCMLYEMIAGRSPFRQrkekvdKEELKRR-----TLEMAVEYPDS 221
                         250
                  ....*....|..
gi 1113820495 378 QAPKARKFFEKL 389
Cdd:cd05577   222 FSPEARSLCEGL 233
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
148-352 4.84e-20

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 90.31  E-value: 4.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII--------KNKKAFLNQAQIEVRLlelMNKHdtemkyyIVHLKRHF 219
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVpkssltkpKQREKLKSEIKIHRSL---KHPN-------IVKFHDCF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVD 298
Cdd:cd14099    71 EDEENVYILLELCSNgSLMELLKRR--KALTEPEVRYFMRQILSGVKYLH--SNRIIHRDLKLGNLFLDENMN--VKIGD 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 299 FGSSCQL---GQRIY------QYIqsrfyrSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14099   145 FGLAARLeydGERKKtlcgtpNYI------APEVLEKKKgHSFEVDIWSLGVILYTLLVGKPPF 202
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
145-401 5.29e-20

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 90.67  E-value: 5.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KWMDryeiDSLIGKGSFGQVVKAYDRVEQEWVAIKII----------KNKKAFLNQAQIEVRLL-ELMNKHdtemkyyIV 213
Cdd:cd06628     1 KWIK----GALIGSGSFGSVYLGMNASSGELMAVKQVelpsvsaenkDRKKSMLDALQREIALLrELQHEN-------IV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 214 HLKRHFMFRNHLCLVFEML-SYNLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNpkRS 292
Cdd:cd06628    70 QYLGSSSDANHLNIFLEYVpGGSVATLL--NNYGAFEESLVRNFVRQILKGLNYLHNR--GIIHRDIKGANILVDN--KG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 293 AIKIVDFGSSCQL----------GQRIyQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQMN 362
Cdd:cd06628   144 GIKISDFGISKKLeanslstknnGARP-SLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQ 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1113820495 363 KIVEVLGI----PPAHILDQapkARKFFEKLPDGTWNLKKTKD 401
Cdd:cd06628   220 AIFKIGENasptIPSNISSE---ARDFLEKTFEIDHNKRPTAD 259
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
150-364 7.39e-20

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: 90.05  E-value: 7.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA---FLNQ---AQIEV-------RLLELMNKHDTEMKYYIVhlk 216
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKApedYLQKflpREIEVikglkhpNLICFYEAIETTSRVYII--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 217 rhfmfrnhlclvfeM-LSYN--LYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSA 293
Cdd:cd14162    79 --------------MeLAENgdLLDYIRKNGA--LPEPQARRWFRQLVAGVEYCHS--KGVVHRDLKCENLLL--DKNNN 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 294 IKIVDFGSSC-----QLGQRIYQ--YIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd14162   139 LKITDFGFARgvmktKDGKPKLSetYCGSYAYASPEILRGIPYDpFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQV 217
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
149-364 2.19e-19

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 88.81  E-value: 2.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRvEQEWVAIKII-------KNKKAFLNqaqiEVRLLELMNKHDtemkyYIVHLKRH--F 219
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVLNP-KKKIYALKRVdlegadeQTLQSYKN----EIELLKKLKGSD-----RIIQLYDYevT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkrSAIKIVDF 299
Cdd:cd14131    72 DEDDYLYMVMECGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIH--EEGIVHSDLKPANFLLVK---GRLKLIDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 GsscqlgqrIYQYIQS------RF-------YRSPEVLLGMPYDLAI----------DMWSLGCILVEMHTGEPLFsgAN 356
Cdd:cd14131   147 G--------IAKAIQNdttsivRDsqvgtlnYMSPEAIKDTSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPF--QH 216

                  ....*...
gi 1113820495 357 EVDQMNKI 364
Cdd:cd14131   217 ITNPIAKL 224
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
155-409 2.20e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 89.62  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQ----AQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05620     2 VLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDdvecTMVEKRVLALAWENP-----FLTHLYCTFQTKEHLFFVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLsyNLYDLLRNTNFRGvSLNLTRK--FAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQ---L 305
Cdd:cd05620    77 FL--NGGDLMFHIQDKG-RFDLYRAtfYAAEIVCGLQFLHSK--GIIYRDLKLDNVML--DRDGHIKIADFGM-CKenvF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQ-RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI-VEVLGIPPAHILDQAPKAR 383
Cdd:cd05620   149 GDnRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIrVDTPHYPRWITKESKDILE 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1113820495 384 KFFEKLPDG----TWNLK-----KTKD----GKREYKPP 409
Cdd:cd05620   229 KLFERDPTRrlgvVGNIRghpffKTINwtalEKRELDPP 267
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
150-364 2.72e-19

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: 89.68  E-value: 2.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFG--QVVKayDRVEQEWVAIKIIKnKKAFLNQAQI----EVRllELMNKHDTEmkyYIVHLKRHFMFRN 223
Cdd:cd05601     3 FEVKNVIGRGHFGevQVVK--EKATGDIYAMKVLK-KSETLAQEEVsffeEER--DIMAKANSP---WITKLQYAFQDSE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNlyDLLrntnfrgvSLnLTR---KFAQQMCTalLFLATPELSI--------IHCDLKPENILLcnPKRS 292
Cdd:cd05601    75 NLYLVMEYHPGG--DLL--------SL-LSRyddIFEESMAR--FYLAELVLAIhslhsmgyVHRDIKPENILI--DRTG 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 293 AIKIVDFGSSCQLGQRiyQYIQSRF------YRSPEVLLGM------PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd05601   140 HIKLADFGSAAKLSSD--KTVTSKMpvgtpdYIAPEVLTSMnggskgTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKT 217

                  ....
gi 1113820495 361 MNKI 364
Cdd:cd05601   218 YSNI 221
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
156-367 3.26e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 87.67  E-value: 3.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAflnQAQIEVRL-LELMNK--HDTemkyyIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKA---KDREDVRNeIEIMNQlrHPR-----LLQLYDAFETPREMVLVMEYV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 S-YNLYDLLRNTNFrgvslNLTRK----FAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQ 307
Cdd:cd14103    73 AgGELFERVVDDDF-----ELTERdcilFMRQICEGVQYMH--KQGILHLDLKPENILCVSRTGNQIKIIDFGLARKYDP 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 308 RiyQYIQSRF----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV 367
Cdd:cd14103   146 D--KKLKVLFgtpeFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRA 207
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
150-357 3.60e-19

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 87.99  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI---EVRLLELMNkHDtemkyYIVHLKRHFMFRNHLC 226
Cdd:cd14097     3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLlerEVDILKHVN-HA-----HIIHLEEVFETPKRMY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEML-SYNLYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLC-----NPKRSAIKIVDFG 300
Cdd:cd14097    77 LVMELCeDGELKELLLRKGF--FSENETRHIIQSLASAVAYLHKND--IVHRDLKLENILVKssiidNNDKLNIKVTDFG 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 301 SSCQLGQRIYQYIQSR----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANE 357
Cdd:cd14097   153 LSVQKYGLGEDMLQETcgtpIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSE 213
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-366 3.69e-19

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: 88.16  E-value: 3.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMN-KHDTemkyyIVHLKRHFMFRNHLC 226
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKiKHPN-----IVALDDIYESGGHLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTNF---RGVSlnltrKFAQQMCTALLFLAtpELSIIHCDLKPENILLCN-PKRSAIKIVDFGS 301
Cdd:cd14167    78 LIMQLVSGgELFDRIVEKGFyteRDAS-----KLIFQILDAVKYLH--DMGIVHRDLKPENLLYYSlDEDSKIMISDFGL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 302 SC--QLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14167   151 SKieGSGSVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILK 217
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
156-393 4.76e-19

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 87.42  E-value: 4.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEW-VAIKII--KN--KKAFLNQAQIEVrLLELmnKHDTemkyyIVHLKRHFMFRNHLCLVFE 230
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKPDLpVAIKCItkKNlsKSQNLLGKEIKI-LKEL--SHEN-----VVALLDCQETSSSVYLVME 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRSA-------IKIVDFGSS 302
Cdd:cd14120    73 YCNGgDLADYLQAK--GTLSEDTIRVFLQQIAAAMKALHSK--GIVHRDLKPQNILLSHNSGRKpspndirLKIADFGFA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 cqlgqriyQYIQ----------SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSgANEVDQMNKIVEvlgipp 372
Cdd:cd14120   149 --------RFLQdgmmaatlcgSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQ-AQTPQELKAFYE------ 213
                         250       260
                  ....*....|....*....|.
gi 1113820495 373 ahildqapKARKFFEKLPDGT 393
Cdd:cd14120   214 --------KNANLRPNIPSGT 226
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
148-366 5.95e-19

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: 87.88  E-value: 5.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF-LNQAQ---IEVRLLelmnkhdTEMKY-YIVHLKRHFMFR 222
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIrLKQEQhvhNEKRVL-------KEVSHpFIIRLFWTEHDQ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEML-SYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGS 301
Cdd:cd05612    74 RFLYMLMEYVpGGELFSYLRNS--GRFSNSTGLFYASEIVCALEYLHS--KEIVYRDLKPENILL--DKEGHIKLTDFGF 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 302 SCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05612   148 AKKLRDRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILA 212
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
150-360 6.07e-19

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 87.39  E-value: 6.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII---KNKKAFLNQAQIEVRLLELMNkHDTemkyyIVHLKRHFMFRNHLC 226
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkRAPGDCPENIKKEVCIQKMLS-HKN-----VVRFYGHRREGEFQY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLS-YNLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQl 305
Cdd:cd14069    77 LFLEYASgGELFDKIEPDV--GMPEDVAQFYFQQLMAGLKYLHS--CGITHRDIKPENLLL--DENDNLKISDFGLATV- 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 306 gqriYQY----------IQSRFYRSPEVLLGMPYDLA-IDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd14069   150 ----FRYkgkerllnkmCGTLPYVAPELLAKKKYRAEpVDVWSCGIVLFAMLAGELPWDQPSDSCQ 211
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
148-372 6.26e-19

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 87.76  E-value: 6.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCL 227
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYYKKDVKNGDQLWL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLS-YNLYDLLRNTNFRGVSLNlTRKFAQQMCTALLFLA-TPELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQL 305
Cdd:cd06638    98 VLELCNgGSVTDLVKGFLKRGERME-EPIIAYILHEALMGLQhLHVNKTIHRDVKGNNILLTT--EGGVKLVDFGVSAQL 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 306 GQ---RIYQYIQSRFYRSPEVL-----LGMPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQMNKIVEVLGIPP 372
Cdd:cd06638   175 TStrlRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPLA---DLHPMRALFKIPRNPP 246
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
149-362 6.56e-19

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: 87.33  E-value: 6.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK-----NKKAflNQAQI-EVRLLELMNkHDTEMKYYivhlkRHFMFR 222
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifemmDAKA--RQDCLkEIDLLQQLN-HPNIIKYL-----ASFIEN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLSY-NLYDLLRNTNFRGVSLNLTR--KFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDF 299
Cdd:cd08224    73 NELNIVLELADAgDLSRLIKHFKKQKRLIPERTiwKYFVQLCSALEHMH--SKRIMHRDIKPANVFIT--ANGVVKLGDL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 300 GsscqLGQriyqYIQSR-----------FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGanevDQMN 362
Cdd:cd08224   149 G----LGR----FFSSKttaahslvgtpYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYG----EKMN 210
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
150-390 8.67e-19

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 86.84  E-value: 8.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAF---------LNQAQIEVRLlelmnKHDTemkyyIVHLKRHFM 220
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMI-DKKAMqkagmvqrvRNEVEIHCQL-----KHPS-----ILELYNYFE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCnpKRSAIKIVDFG 300
Cdd:cd14186    72 DSNYVYLVLEMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSH--GILHRDLTLSNLLLT--RNMNIKIADFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 SSCQL---GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILD 377
Cdd:cd14186   148 LATQLkmpHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSR 227
                         250
                  ....*....|....
gi 1113820495 378 QAPK-ARKFFEKLP 390
Cdd:cd14186   228 EAQDlIHQLLRKNP 241
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
149-345 8.85e-19

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 87.37  E-value: 8.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIiknkkaflNQAQIEVRLLELMNKHDTEMKYYIVH--LKRHFMFR---- 222
Cdd:cd13990     1 RYLLLNLLGKGGFSEVYKAFDLVEQRYVACKI--------HQLNKDWSEEKKQNYIKHALREYEIHksLDHPRIVKlydv 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 -----NHLCLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRS-AIKI 296
Cdd:cd13990    73 feidtDSFCTVLEYCDGNDLDFYLKQH-KSIPEREARSIIMQVVSALKYLNEIKPPIIHYDLKPGNILLHSGNVSgEIKI 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 297 VDFGSSCQLGQRIY---------QYIQSRFYRSPEVLLGMPYDLAI----DMWSLGCILVEM 345
Cdd:cd13990   152 TDFGLSKIMDDESYnsdgmeltsQGAGTYWYLPPECFVVGKTPPKIsskvDVWSVGVIFYQM 213
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
148-350 8.95e-19

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: 86.92  E-value: 8.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA----FLNQAQIEVrLLELMNKHDTemKYYIVHLKRHfmfrn 223
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAedeiEDIQQEIQF-LSQCDSPYIT--KYYGSFLKGS----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTNFRGVSLN-LTRkfaqQMCTALLFLATPELsiIHCDLKPENILLCNpkRSAIKIVDFGS 301
Cdd:cd06609    73 KLWIIMEYCGGgSVLDLLKPGPLDETYIAfILR----EVLLGLEYLHSEGK--IHRDIKAANILLSE--EGDVKLADFGV 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 302 SCQLGQRIYQ---YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06609   145 SGQLTSTMSKrntFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEP 196
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
149-385 9.53e-19

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: 86.69  E-value: 9.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII------KNKKAFLNQAQIEVRLLELMnKHDTEMKYYIVHlkrhfMFR 222
Cdd:cd06632     1 RWQKGQLLGSGSFGSVYEGFNGDTGDFFAVKEVslvdddKKSRESVKQLEQEIALLSKL-RHPNIVQYYGTE-----REE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLSY-NLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGS 301
Cdd:cd06632    75 DNLYIFLEYVPGgSIHKLLQR--YGAFEEPVIRLYTRQILSGLAYLHS--RNTVHRDIKGANILV--DTNGVVKLADFGM 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQL-GQR-IYQYIQSRFYRSPEVLL--GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPahILD 377
Cdd:cd06632   149 AKHVeAFSfAKSFKGSPYWMAPEVIMqkNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELPP--IPD 226

                  ....*....
gi 1113820495 378 Q-APKARKF 385
Cdd:cd06632   227 HlSPDAKDF 235
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
148-389 9.55e-19

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 87.02  E-value: 9.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDS-LIGKGSFGQVVKAYDRVEQEWVAIKIIKNK---KAFLNQAQIEVRLLELMNKHDtemkyYIVHLKRHFMFRN 223
Cdd:cd14106     7 EVYTVEStPLGRGKFAVVRKCIHKETGKEYAAKFLRKRrrgQDCRNEILHEIAVLELCKDCP-----RVVNLHEVYETRS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSA-IKIVDFGS 301
Cdd:cd14106    82 ELILILELAAGgELQTLLDEEE--CLTEADVRRLMRQILEGVQYLH--ERNIVHLDLKPQNILLTSEFPLGdIKLCDFGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV-LGIPPAHILDQ 378
Cdd:cd14106   158 SRVIgeGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCnLDFPEELFKDV 237
                         250
                  ....*....|.
gi 1113820495 379 APKARKFFEKL 389
Cdd:cd14106   238 SPLAIDFIKRL 248
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
149-356 1.01e-18

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: 86.61  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI--EVRLLELMNKHDtemkyyIVHLKRHFMFRNHLC 226
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMIenEVAILRRVKHPN------IVQLIEEYDTDTELY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTNfrgvslNLTRKFAQQM----CTALLFLAtpELSIIHCDLKPENILLCNPK--RSAIKIVDF 299
Cdd:cd14095    75 LVMELVKGgDLFDAITSST------KFTERDASRMvtdlAQALKYLH--SLSIVHRDIKPENLLVVEHEdgSKSLKLADF 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 300 GSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14095   147 GLATEVKEPLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPD 203
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
148-366 1.13e-18

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: 87.07  E-value: 1.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-KNKKAFLNQAQ---IEVRLLELMNKHdtemkyYIVHLKRHFMFRN 223
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILdKQKVVKLKQVEhtlNEKRILQAINFP------FLVKLEYSFKDNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSS 302
Cdd:cd14209    75 NLYMVMEYVPGgEMFSHLRRI--GRFSEPHARFYAAQIVLAFEYLH--SLDLIYRDLKPENLLI--DQQGYIKVTDFGFA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 303 CQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14209   149 KRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVS 212
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
150-364 1.20e-18

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: 86.37  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAY-DRVEQEwVAIKIIKNKKA-------FLNQaqiEVRLLELMNkHDTEMKYYivhlkrhfmf 221
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYsERLKCN-VAIKIIDKKKApddfvekFLPR---ELEILARLN-HKSIIKTY---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 rnhlcLVFEMLSYNLY---------DLLRNTNFRG-VSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKR 291
Cdd:cd14165    68 -----EIFETSDGKVYivmelgvqgDLLEFIKLRGaLPEDVARKMFHQLSSAIKYCH--ELDIVHRDLKCENLLL--DKD 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 292 SAIKIVDFGSSCQL-----GQRIYQ--YIQSRFYRSPEVLLGMPYDLAI-DMWSLGCILVEMHTGEPLFSGANeVDQMNK 363
Cdd:cd14165   139 FNIKLTDFGFSKRClrdenGRIVLSktFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSN-VKKMLK 217

                  .
gi 1113820495 364 I 364
Cdd:cd14165   218 I 218
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
149-389 1.33e-18

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: 86.43  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDtemkyYIVHLKRHFMFRNHLCLV 228
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELNVLRRV-RHT-----NIIQLIEVFETKERVYMV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLS-YNLYD-LLRNTNFrgvSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPK-RSAIKIVDFGSSCQL 305
Cdd:cd14087    76 MELATgGELFDrIIAKGSF---TERDATRVLQMVLDGVKYLHG--LGITHRDLKPENLLYYHPGpDSKIMITDFGLASTR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQYIQSRF----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV-LGIPPAHILDQAP 380
Cdd:cd14087   151 KKGPNCLMKTTCgtpeYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAkYSYSGEPWPSVSN 230

                  ....*....
gi 1113820495 381 KARKFFEKL 389
Cdd:cd14087   231 LAKDFIDRL 239
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
149-389 1.58e-18

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 86.27  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEID----SLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI--EVRLLELMNkHDTEMKYYIVHLKRHFMFr 222
Cdd:cd14046     3 RYLTDfeelQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNSRIlrEVMLLSRLN-HQHVVRYYQAWIERANLY- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 nhlclvFEM---LSYNLYDLLRNTNFRGVSlNLTRKFaQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd14046    81 ------IQMeycEKSTLRDLIDSGLFQDTD-RLWRLF-RQILEGLAYIH--SQGIIHRDLKPVNIFL--DSNGNVKIGDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 G----------SSCQLGQRIYQYIQSR-----------FYRSPEVLLGMP--YDLAIDMWSLGCILVEMhtGEPLFSGAN 356
Cdd:cd14046   149 GlatsnklnveLATQDINKSTSAALGSsgdltgnvgtaLYVAPEVQSGTKstYNEKVDMYSLGIIFFEM--CYPFSTGME 226
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1113820495 357 EVDQMNKIVEVLG-IPPAHILDQAPKARKFFEKL 389
Cdd:cd14046   227 RVQILTALRSVSIeFPPDFDDNKHSKQAKLIRWL 260
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
150-357 1.58e-18

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 86.50  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLiGKGSFGQVVKAYDRVEQEWVAIKIIKNK----KAFLNQAQIEVRLLELMNKhdtemkYYIVHLKRHFMFRNHL 225
Cdd:cd05607     5 YEFRVL-GKGGFGEVCAVQVKNTGQMYACKKLDKKrlkkKSGEKMALLEKEILEKVNS------PFIVSLAYAFETKTHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLS-----YNLYdllrNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL-CNpkrSAIKIVDF 299
Cdd:cd05607    78 CLVMSLMNggdlkYHIY----NVGERGIEMERVIFYSAQITCGILHLH--SLKIVYRDMKPENVLLdDN---GNCRLSDL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 GSSCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANE 357
Cdd:cd05607   149 GLAVEVkeGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKE 208
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
156-389 1.59e-18

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: 87.37  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFL--NQAQ---IEVRLLeLMN-KHDtemkyYIVHLkrHFMFRNHLCLVF 229
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVL-QKKAILkrNEVKhimAERNVL-LKNvKHP-----FLVGL--HYSFQTKDKLYF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 eMLSY-N----LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQ 304
Cdd:cd05575    74 -VLDYvNggelFFHLQRERHF---PEPRARFYAAEIASALGYLH--SLNIIYRDLKPENILL--DSQGHVVLTDFGL-CK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 LGQRIyQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANeVDQM-NKIV-EVLGIPPaHIld 377
Cdd:cd05575   145 EGIEP-SDTTSTFcgtpeYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRD-TAEMyDNILhKPLRLRT-NV-- 219
                         250
                  ....*....|..
gi 1113820495 378 qAPKARKFFEKL 389
Cdd:cd05575   220 -SPSARDLLEGL 230
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
150-366 1.82e-18

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: 86.97  E-value: 1.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDS---LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMNKHDTEMKYYIVHLKRHfmfrnHLC 226
Cdd:cd14092     5 YELDLreeALGDGSFSVCRKCVHKKTGQEFAVKIVSRRL----DTSREVQLLRLCQGHPNIVKLHEVFQDEL-----HTY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYN-LYDLLR-NTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSA-IKIVDFGSSC 303
Cdd:cd14092    76 LVMELLRGGeLLERIRkKKRF---TESEASRIMRQLVSAVSFMH--SKGVVHRDLKPENLLFTDEDDDAeIKIVDFGFAR 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 304 QLGQRiyQYIQSR-F---YRSPEVLLGMP----YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14092   151 LKPEN--QPLKTPcFtlpYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMK 219
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
148-470 1.87e-18

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


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 86.67  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHfmfrnhL 225
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRlqEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKET------L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLrNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPkrSAIKIVDFGSSCQL 305
Cdd:cd07869    79 TLVFEYVHTDLCQYM-DKHPGGLHPENVKLFLFQLLRGLSYIH--QRYILHRDLKPQNLLISDT--GELKLADFGLARAK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQY---IQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEV-DQMNKIVEVLGIPPAhilDQAP 380
Cdd:cd07869   154 SVPSHTYsneVVTLWYRPPDVLLGsTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIqDQLERIFLVLGTPNE---DTWP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 381 KARKFFEKLPDgTWNLKKTKDGKREYKppgtrKLHNILGVEtggpggrragesghtvadylkfkDLILRMLDYDPKTRIQ 460
Cdd:cd07869   231 GVHSLPHFKPE-RFTLYSPKNLRQAWN-----KLSYVNHAE-----------------------DLASKLLQCFPKNRLS 281
                         330
                  ....*....|
gi 1113820495 461 PYYALQHSFF 470
Cdd:cd07869   282 AQAALSHEYF 291
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
148-470 1.94e-18

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: 85.87  E-value: 1.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII---------KNKKAFLNQAQIEVRLLELMNKHDtemkyYIVHLKRH 218
Cdd:cd14093     3 AKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIditgeksseNEAEELREATRREIEILRQVSGHP-----NIIELHDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEML-SYNLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRsaIKIV 297
Cdd:cd14093    78 FESPTFIFLVFELCrKGELFDYL--TEVVTLSEKKTRRIMRQLFEAVEFLHS--LNIVHRDLKPENILLDDNLN--VKIS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 298 DFGSSCQL--GQRIYQYIQSRFYRSPEVL-----LGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEvlg 369
Cdd:cd14093   152 DFGFATRLdeGEKLRELCGTPGYLAPEVLkcsmyDNAPgYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIME--- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 370 ippahildqapkarkffeklpdgtwnlkktkdGKREYKPPgtrKLHNIlgvetggpggrragesGHTVadylkfKDLILR 449
Cdd:cd14093   229 --------------------------------GKYEFGSP---EWDDI----------------SDTA------KDLISK 251
                         330       340
                  ....*....|....*....|.
gi 1113820495 450 MLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14093   252 LLVVDPKKRLTAEEALEHPFF 272
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
150-356 2.21e-18

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 85.52  E-value: 2.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIknKKAFLNQAQI-----EVRLLELMNkHDTEMKYYIVhlkrhFMFRNH 224
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKII--DKSQLDEENLkkiyrEVQIMKMLN-HPHIIKLYQV-----METKDM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSS- 302
Cdd:cd14071    74 LYLVTEYASNgEIFDYL--AQHGRMSEKEARKKFWQILSAVEYCHK--RHIVHRDLKAENLLL--DANMNIKIADFGFSn 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 303 -CQLGQRIYQYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14071   148 fFKPGELLKTWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGST 203
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-352 2.59e-18

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 85.94  E-value: 2.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF---LNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNH 224
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSardHQKLEREARICRLL-KHPN-----IVRLHDSISEEGF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLrntnfrgvslnLTRKF---------AQQMCTALLFlaTPELSIIHCDLKPENILLCNP-KRSA 293
Cdd:cd14086    75 HYLVFDLVTGgELFEDI-----------VAREFyseadashcIQQILESVNH--CHQNGIVHRDLKPENLLLASKsKGAA 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 294 IKIVDFGSSCQL---GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14086   142 VKLADFGLAIEVqgdQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPF 203
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
150-358 2.68e-18

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 87.78  E-value: 2.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkKAFLNQAQiEVRllELMNKHD---TEMKYYIVHLKRHFMFRNHLC 226
Cdd:cd05600    13 FQILTQVGQGGYGSVFLARKKDTGEICALKIMK--KKVLFKLN-EVN--HVLTERDiltTTNSPWLVKLLYAFQDPENVY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEmlsY----NLYDLLRNTnfrGV-SLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGS 301
Cdd:cd05600    88 LAME---YvpggDFRTLLNNS---GIlSEEHARFYIAEMFAAISSLH--QLGYIHRDLKPENFLI--DSSGHIKLTDFGL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SC----------------------------------------QLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCI 341
Cdd:cd05600   158 ASgtlspkkiesmkirleevkntafleltakerrniyramrkEDQNYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCI 237
                         250
                  ....*....|....*....
gi 1113820495 342 LVEMHTGEPLFSG--ANEV 358
Cdd:cd05600   238 LFECLVGFPPFSGstPNET 256
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
148-372 3.99e-18

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: 85.18  E-value: 3.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK-NKKAFLNQAQIEVRLLELMnKHDtemkyYIVHLKRHFMFRNHLC 226
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQiESEEELEDFMVEIDILSEC-KHP-----NIVGLYEAYFYENKLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLG 306
Cdd:cd06611    79 ILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLH--SHKVIHRDLKAGNILLT--LDGDVKLADFGVSAKNK 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 307 ---QRIYQYIQSRFYRSPEVLL-----GMPYDLAIDMWSLGCILVEMHTGEPlfsGANEVDQMNKIVEVLGIPP 372
Cdd:cd06611   155 stlQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEP---PHHELNPMRVLLKILKSEP 225
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
155-366 4.04e-18

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 85.43  E-value: 4.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQA-QIEVRLLELMnKHDTemkyyIVHLKRHFMFRNHLCLVFEMLS 233
Cdd:cd14166    10 VLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSlENEIAVLKRI-KHEN-----IVTLEDIYESTTHYYLVMQLVS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 Y-NLYDLLRNtnfRGVslnLTRKFA----QQMCTALLFLAtpELSIIHCDLKPENILLCNP-KRSAIKIVDFGSSCQLGQ 307
Cdd:cd14166    84 GgELFDRILE---RGV---YTEKDAsrviNQVLSAVKYLH--ENGIVHRDLKPENLLYLTPdENSKIMITDFGLSKMEQN 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIYQY-IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14166   156 GIMSTaCGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKE 215
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
150-342 4.83e-18

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 84.81  E-value: 4.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-KNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHfmfrNHLCLV 228
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIpRASNAGLKKEREKRLEKEISRDIRTIREAALSSLLNH----PHICRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLS-----YNLYD------LLRNTNFRG-VSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKI 296
Cdd:cd14077    79 RDFLRtpnhyYMLFEyvdggqLLDYIISHGkLKEKQARKFARQIASALDYLHRN--SIVHRDLKIENILI--SKSGNIKI 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1113820495 297 VDFGSSCQLGQR--IYQYIQSRFYRSPEVLLGMPY-DLAIDMWSLGCIL 342
Cdd:cd14077   155 IDFGLSNLYDPRrlLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVL 203
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
149-359 6.36e-18

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 84.29  E-value: 6.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEID--SLIGKGSFGQVVKAYDRVEQEW-VAIKIIKNKKAFLNQAQI--EVRLLELMnKHDTemkyyIVHLKRHFMFRN 223
Cdd:cd14202     1 KFEFSrkDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLgkEIKILKEL-KHEN-----IVALYDFQEIAN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL-------CNPKRSAIK 295
Cdd:cd14202    75 SVYLVMEYCNGgDLADYLHTM--RTLSEDTIRLFLQQIAGAMKMLHSK--GIIHRDLKPQNILLsysggrkSNPNNIRIK 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 296 IVDFGSScqlgqriyQYIQ----------SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVD 359
Cdd:cd14202   151 IADFGFA--------RYLQnnmmaatlcgSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD 216
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
145-352 6.39e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 85.64  E-value: 6.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KW-MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLE---LMnkhdtEMKY-YIVHLKRHF 219
Cdd:PTZ00263   14 SWkLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK-KREILKMKQVQHVAQEksiLM-----ELSHpFIVNMMCSF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFE-MLSYNLYDLLRNTnfrGVSLNLTRKF-AQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIV 297
Cdd:PTZ00263   88 QDENRVYFLLEfVVGGELFTHLRKA---GRFPNDVAKFyHAELVLAFEYLH--SKDIIYRDLKPENLLL--DNKGHVKVT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 298 DFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:PTZ00263  161 DFGFAKKVPDRTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
148-394 6.63e-18

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 84.69  E-value: 6.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNK-KAFLNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHLC 226
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKsEEELEDYMVEIDILASCDHP------NIVKLLDAFYYENNLW 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPkrSAIKIVDFGSSCQ-- 304
Cdd:cd06643    79 ILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLH--ENKIIHRDLKAGNILFTLD--GDIKLADFGVSAKnt 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 -LGQRIYQYIQSRFYRSPEVLL-----GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE----VLGIPPAH 374
Cdd:cd06643   155 rTLQRRDSFIGTPYWMAPEVVMcetskDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKseppTLAQPSRW 234
                         250       260
                  ....*....|....*....|
gi 1113820495 375 ILDQAPKARKFFEKLPDGTW 394
Cdd:cd06643   235 SPEFKDFLRKCLEKNVDARW 254
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
155-408 6.68e-18

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 85.62  E-value: 6.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEV-----RLLELMNKHDtemkyYIVHLKRHFMFRNHLCLVF 229
Cdd:cd05591     2 VLGKGSFGKVMLAERKGTDEVYAIKVLK-KDVILQDDDVDCtmtekRILALAAKHP-----FLTALHSCFQTKDRLFFVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLsyNLYDLL-RNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQLG-- 306
Cdd:cd05591    76 EYV--NGGDLMfQIQRARKFDEPRARFYAAEVTLALMFLHRH--GVIYRDLKLDNILL--DAEGHCKLADFGM-CKEGil 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 307 --QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV------------------- 365
Cdd:cd05591   149 ngKTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILhddvlypvwlskeavsilk 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 366 --------EVLGIPPAHILDQAPKARKFFEKLpdgTWNLKKTKDGKREYKP 408
Cdd:cd05591   229 afmtknpaKRLGCVASQGGEDAIRQHPFFREI---DWEALEQRKVKPPFKP 276
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
149-389 7.08e-18

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: 84.31  E-value: 7.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK-IIKNKKAFLNQAQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNH--- 224
Cdd:cd13985     1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKrMYFNDEEQLRVAIKEIEIMKRLCGHP-----NIVQYYDSAILSSEgrk 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 -LCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRsaIKIVDFGSSC 303
Cdd:cd13985    76 eVLLLMEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSNTGR--FKLCDFGSAT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QlgQRIYQYIQSRF--------------YRSPEVL---LGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVdqmnKIVE 366
Cdd:cd13985   154 T--EHYPLERAEEVniieeeiqknttpmYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESSKL----AIVA 227
                         250       260
                  ....*....|....*....|....
gi 1113820495 367 V-LGIPPAHIldQAPKARKFFEKL 389
Cdd:cd13985   228 GkYSIPEQPR--YSPELHDLIRHM 249
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
150-366 7.21e-18

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 84.48  E-value: 7.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRV-EQEWVAIK-IIKNKKAFLNQAQ----------IEVRLLELMNKHDTEMKYYivhlkR 217
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSnGQTLLALKeINMTNPAFGRTEQerdksvgdiiSEVNIIKEQLRHPNIVRYY-----K 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFRNHLCLVFEMLS----YNLYDLLRNTNFRGVSLNLTRKFAQqMCTALLFLATpELSIIHCDLKPENILLCNPKRsa 293
Cdd:cd08528    77 TFLENDRLYIVMELIEgaplGEHFSSLKEKNEHFTEDRIWNIFVQ-MVLALRYLHK-EKQIVHRDLKPNNIMLGEDDK-- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 294 IKIVDFGSSCQLG---QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd08528   153 VTITDFGLAKQKGpesSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVE 228
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
149-391 7.47e-18

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: 83.99  E-value: 7.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA----FLNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNH 224
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVaregMVEQIKREIAIMKLL-RHPN-----IVELHEVMATKTK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLrNTNFRgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNpkRSAIKIVDFGSSC 303
Cdd:cd14663    75 IFFVMELVTGgELFSKI-AKNGR-LKEDKARKYFQQLIDAVDYCHSR--GVFHRDLKPENLLLDE--DGNLKISDFGLSA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 -----QLGQRIYQYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHIld 377
Cdd:cd14663   149 lseqfRQDGLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWF-- 226
                         250
                  ....*....|....
gi 1113820495 378 qAPKARKFFEKLPD 391
Cdd:cd14663   227 -SPGAKSLIKRILD 239
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
155-365 7.97e-18

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: 85.45  E-value: 7.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQiEVRLLELMNKHDTEMKY-YIVHLkrHFMFRNHLCLVFEMLS 233
Cdd:cd05602    14 VIGKGSFGKVLLARHKSDEKFYAVKVLQ-KKAILKKKE-EKHIMSERNVLLKNVKHpFLVGL--HFSFQTTDKLYFVLDY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YN----LYDLLRNTNFRGVSlnlTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFG---SSCQLG 306
Cdd:cd05602    90 INggelFYHLQRERCFLEPR---ARFYAAEIASALGYLHS--LNIVYRDLKPENILL--DSQGHIVLTDFGlckENIEPN 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 307 QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd05602   163 GTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNIL 221
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
149-354 8.55e-18

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: 83.85  E-value: 8.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEwVAIKIIKNKKAFLNQAQIEVRL-LELMNKHDTEmkyYIVHLKRHFMFRNHLCL 227
Cdd:cd14161     4 RYEFLETLGKGTYGRVKKARDSSGRL-VAIKSIRKDRIKDEQDLLHIRReIEIMSSLNHP---HIISVYEVFENSSKIVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL-CNpkrSAIKIVDFGSS--C 303
Cdd:cd14161    80 VMEYASRgDLYDYISER--QRLSELEARHFFRQIVSAVHYCHAN--GIVHRDLKLENILLdAN---GNIKIADFGLSnlY 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 304 QLGQRIYQYIQSRFYRSPEVLLGMPY-DLAIDMWSLGCILVEMHTGEPLFSG 354
Cdd:cd14161   153 NQDKFLQTYCGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDG 204
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
153-388 1.30e-17

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 83.43  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 153 DSLIGKGSFGQVVKAYDR---VEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDTEMKYYivhlkrHFMF---RNHLC 226
Cdd:cd13983     6 NEVLGRGSFKTVYRAFDTeegIEVAWNEIKLRKLPKAERQRFKQEIEILKSL-KHPNIIKFY------DSWEsksKKEVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFE-MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLcNPKRSAIKIVDFGSSCQL 305
Cdd:cd13983    79 FITElMTSGTLKQYLKR--FKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNIFI-NGNTGEVKIGDLGLATLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQ-RIYQYIQSRFYRSPEVLLGMpYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVlGIPPAHiLD--QAPKA 382
Cdd:cd13983   156 RQsFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTS-GIKPES-LSkvKDPEL 232

                  ....*.
gi 1113820495 383 RKFFEK 388
Cdd:cd13983   233 KDFIEK 238
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
149-356 1.59e-17

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: 83.08  E-value: 1.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQ---AQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNHL 225
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEkeaSKKEVILLAKM-KHPN-----IVTFFASFQENGRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNlyDLLRNTNF-RGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAiKIVDFGSSCQ 304
Cdd:cd08225    75 FIVMEYCDGG--DLMKRINRqRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVA-KLGDFGIARQ 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 305 LGQRI---YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd08225   152 LNDSMelaYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNN 206
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
156-389 1.60e-17

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 84.20  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIE-VR----LLELMNKHdtemkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05599     9 IGRGAFGEVRLVRKKDTGHVYAMKKLR-KSEMLEKEQVAhVRaerdILAEADNP------WVVKLYYSFQDEENLYLIME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSY-NLYDLL--RNTnfrgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQ 307
Cdd:cd05599    82 FLPGgDMMTLLmkKDT----LTEEETRFYIAETVLAIESIH--KLGYIHRDIKPDNLLL--DARGHIKLSDFGLCTGLKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIYQY--IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV---EVLGIPP-AHIldqAPK 381
Cdd:cd05599   154 SHLAYstVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwrETLVFPPeVPI---SPE 230

                  ....*...
gi 1113820495 382 ARKFFEKL 389
Cdd:cd05599   231 AKDLIERL 238
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
150-356 1.61e-17

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: 82.99  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA---FLNQaqIEVRLLELMNKHDTEmkyYIVHLKRHFMFRN-HL 225
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRAspdFVQK--FLPRELSILRRVNHP---NIVQMFECIEVANgRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcNPKRSAIKIVDFGSSCQL 305
Cdd:cd14164    77 YIVMEAAATDLLQKIQEVHH--IPKDLARDMFAQMVGAVNYLH--DMNIVHRDLKCENILL-SADDRKIKIADFGFARFV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 306 G---QRIYQYIQSRFYRSPEVLLGMPYDL-AIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14164   152 EdypELSTTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPFDETN 206
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
149-366 1.70e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 82.86  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDR---VEQEWVAIKII------KNKKAflnQAQIEVRLLELMNkHDTEMKYYivhlkRHF 219
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLkatADEELKVLKEIsvgelqPDETV---DANREAKLLSKLD-HPAIVKFH-----DSF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLS-YNLYDLLRNTNFRGvslnltRKFAQQMCTAL---LFLATP---ELSIIHCDLKPENILLcnpKRS 292
Cdd:cd08222    72 VEKESFCIVTEYCEgGDLDDKISEYKKSG------TTIDENQILDWfiqLLLAVQymhERRILHRDLKAKNIFL---KNN 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 293 AIKIVDFGSSCQL---GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd08222   143 VIKVGDFGISRILmgtSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVE 219
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
148-393 2.30e-17

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 83.12  E-value: 2.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCL 227
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPISDVDEEIEAEYNILRSLPNHPNVVKFYGMFYKADQYVGGQLWL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLS-YNLYDLLRNTNFRGVSLNltrkfaQQMCTALLFLATPELS------IIHCDLKPENILLCNpkRSAIKIVDFG 300
Cdd:cd06639   102 VLELCNgGSVTELVKGLLKCGQRLD------EAMISYILYGALLGLQhlhnnrIIHRDVKGNNILLTT--EGGVKLVDFG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 SSCQLGQ---RIYQYIQSRFYRSPEVL-----LGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVlgiPP 372
Cdd:cd06639   174 VSAQLTSarlRRNTSVGTPFWMAPEVIaceqqYDYSYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRN---PP 250
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1113820495 373 AHILDQAPKARKF-----------FEKLPDGT 393
Cdd:cd06639   251 PTLLNPEKWCRGFshfisqclikdFEKRPSVT 282
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
153-400 2.66e-17

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 82.65  E-value: 2.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 153 DSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflNQAQIEVRL-LELMNKHDtemKYYIVHLKRHFMFRNHLCLVFEM 231
Cdd:cd14193     9 EEILGGGRFGQVHKCEEKSSGLKLAAKIIKARS---QKEKEEVKNeIEVMNQLN---HANLIQLYDAFESRNDIVLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSY-NLYDLLRNTNFRGVSLNlTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRiy 310
Cdd:cd14193    83 VDGgELFDRIIDENYNLTELD-TILFIKQICEGIQYMH--QMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPR-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 311 QYIQSRF----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV-LGIPPAHILDQAPKARKF 385
Cdd:cd14193   158 EKLRVNFgtpeFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACqWDFEDEEFADISEEAKDF 237
                         250
                  ....*....|....*..
gi 1113820495 386 FEKL--PDGTWNLKKTK 400
Cdd:cd14193   238 ISKLliKEKSWRMSASE 254
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
147-364 2.80e-17

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 83.82  E-value: 2.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQ----AQIEVRLLELMNKHDtemkyYIVHLKRHFMFR 222
Cdd:cd05619     4 IEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDdvecTMVEKRVLSLAWEHP-----FLTHLFCTFQTK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEML----------SYNLYDLLRNTNFrgvslnltrkfAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRS 292
Cdd:cd05619    79 ENLFFVMEYLnggdlmfhiqSCHKFDLPRATFY-----------AAEIICGLQFLHSK--GIVYRDLKLDNILL--DKDG 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 293 AIKIVDFGSsCQ---LGQ-RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd05619   144 HIKIADFGM-CKenmLGDaKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSI 218
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
155-373 3.79e-17

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: 83.09  E-value: 3.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEV---RLLELMN-KHDtemkyYIVHLkrHFMFRNHLCLVFE 230
Cdd:cd05603     2 VIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHImaeRNVLLKNlKHP-----FLVGL--HYSFQTSEKLYFV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSYN----LYDLLRNTNFRGVSlnlTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQLG 306
Cdd:cd05603    75 LDYVNggelFFHLQRERCFLEPR---ARFYAAEVASAIGYLHS--LNIIYRDLKPENILL--DCQGHVVLTDFGL-CKEG 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 307 ----QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSgANEVDQM--NKIVEVLGIPPA 373
Cdd:cd05603   147 mepeETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFY-SRDVSQMydNILHKPLHLPGG 218
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
154-389 4.32e-17

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 83.22  E-value: 4.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 154 SLIGKGSFG---QVVKAYDRVEQEWVAIKIIKNKKAFLNQ-----AQIEVRLLElMNKHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd05584     2 KVLGKGGYGkvfQVRKTTGSDKGKIFAMKVLKKASIVRNQkdtahTKAERNILE-AVKHP-----FIVDLHYAFQTGGKL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNlyDLLRNTNFRGVSLNLTRKF-AQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFG---S 301
Cdd:cd05584    76 YLILEYLSGG--ELFMHLEREGIFMEDTACFyLAEITLALGHLH--SLGIIYRDLKPENILL--DAQGHVKLTDFGlckE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHIldqAPK 381
Cdd:cd05584   150 SIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYL---TNE 226

                  ....*...
gi 1113820495 382 ARKFFEKL 389
Cdd:cd05584   227 ARDLLKKL 234
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
150-389 5.75e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 81.63  E-value: 5.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK------NKKAFLNQAQIEVRLLELMnKHDTEMKYYivHLKRHFMFRN 223
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQfdpespETSKEVNALECEIQLLKNL-LHERIVQYY--GCLRDPQERT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILlcNPKRSAIKIVDFGSS- 302
Cdd:cd06652    81 LSIFMEYMPGGSIKDQLKS--YGALTENVTRKYTRQILEGVHYLHSN--MIVHRDIKGANIL--RDSVGNVKLGDFGASk 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 -----CQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQMNKIVEVLGIP-----P 372
Cdd:cd06652   155 rlqtiCLSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQPtnpqlP 231
                         250
                  ....*....|....*..
gi 1113820495 373 AHILDQapkARKFFEKL 389
Cdd:cd06652   232 AHVSDH---CRDFLKRI 245
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
150-366 7.28e-17

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 81.48  E-value: 7.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIE--VRLLELMNKHDtemkyyIVHLKRHFMFRNHLCL 227
Cdd:cd14169     5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEAMVEneIAVLRRINHEN------IVSLEDIYESPTHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNlyDLLRNTNFRGvslNLTRKFAQQMCTALLFLAT--PELSIIHCDLKPENILLCNP-KRSAIKIVDFG-SSC 303
Cdd:cd14169    79 AMELVTGG--ELFDRIIERG---SYTEKDASQLIGQVLQAVKylHQLGIVHRDLKPENLLYATPfEDSKIMISDFGlSKI 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 304 QLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14169   154 EAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILK 216
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
149-356 9.67e-17

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: 80.55  E-value: 9.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-------KNKKAFLNqaqiEVRLLELMNkHDTEMKYYivhlkRHFMF 221
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmtkEERQAALN----EVKVLSMLH-HPNIIEYY-----ESFLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcNPKRSAIKIVDFG 300
Cdd:cd08220    71 DKALMIVMEYAPGgTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQ--ILHRDLKTQNILL-NKKRTVVKIGDFG 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 301 SSCQLGQR--IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd08220   148 ISKILSSKskAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAAN 205
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
154-366 9.71e-17

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 82.05  E-value: 9.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 154 SLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkKAFLNQ------AQIEVRLLELMNKhdtemKYYIVHLkrHFMFRNHLCL 227
Cdd:cd05587     2 MVLGKGSFGKVMLAERKGTDELYAIKILK--KDVIIQdddvecTMVEKRVLALSGK-----PPFLTQL--HSCFQTMDRL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRNTNFRGvslnltrKF--------AQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd05587    73 YFVMEYVNGGDLMYHIQQVG-------KFkepvavfyAAEIAVGLFFLHSKG--IIYRDLKLDNVML--DAEGHIKIADF 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 300 GSsCQlgQRIYQYIQSR-F-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05587   142 GM-CK--EGIFGGKTTRtFcgtpdYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIME 211
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
150-359 1.10e-16

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 80.82  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEW-VAIKIIKNKKafLNQAQI----EVRLLELMnKHDTEMKYYIVHlkrhfMFRNH 224
Cdd:cd14201     8 YSRKDLVGHGAFAVVFKGRHRKKTDWeVAIKSINKKN--LSKSQIllgkEIKILKEL-QHENIVALYDVQ-----EMPNS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLsyNLYDLLRNTNFRG-VSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL--CNPKRSA-----IKI 296
Cdd:cd14201    80 VFLVMEYC--NGGDLADYLQAKGtLSEDTIRVFLQQIAAAMRILHSK--GIIHRDLKPQNILLsyASRKKSSvsgirIKI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 297 VDFGSSCQLGQRIY--QYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVD 359
Cdd:cd14201   156 ADFGFARYLQSNMMaaTLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQD 220
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
155-357 1.13e-16

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: 81.19  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI----EVRLLELMNKHdtemkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05631     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAmalnEKRILEKVNSR------FVVSLAYAYETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 M-----LSYNLYDLlRNTNF---RGVSlnltrkFAQQMCTALLFLATPElsIIHCDLKPENILLCNpkRSAIKIVDFGSS 302
Cdd:cd05631    81 ImnggdLKFHIYNM-GNPGFdeqRAIF------YAAELCCGLEDLQRER--IVYRDLKPENILLDD--RGHIRISDLGLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 303 CQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANE 357
Cdd:cd05631   150 VQIpeGETVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKE 206
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
150-342 1.25e-16

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: 80.53  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEI--DSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI---EVRLLELMNkHDTemkyyIVHLKRHFMFRNH 224
Cdd:cd14082     3 YQIfpDEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQlrnEVAILQQLS-HPG-----VVNLECMFETPER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKR-SAIKIVDFGSSC 303
Cdd:cd14082    77 VFVVMEKLHGDMLEMILSSEKGRLPERITKFLVTQILVALRYLHSK--NIVHCDLKPENVLLASAEPfPQVKLCDFGFAR 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1113820495 304 QLGQRIYQ--YIQSRFYRSPEVLLGMPYDLAIDMWSLGCIL 342
Cdd:cd14082   155 IIGEKSFRrsVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 195
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
155-365 1.41e-16

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


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 80.39  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF-LNQAQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHLCLVFEMLS 233
Cdd:cd14192    11 VLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKeREEVKNEINIMNQLNHVN------LIQLYDAFESKTNLTLIMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 Y-NLYDLLRNTNFRGVSLNLTRkFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRiyQY 312
Cdd:cd14192    85 GgELFDRITDESYQLTELDAIL-FTRQICEGVHYLH--QHYILHLDLKPENILCVNSTGNQIKIIDFGLARRYKPR--EK 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 313 IQSRF----YRSPEVLlgmPYDLA---IDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd14192   160 LKVNFgtpeFLAPEVV---NYDFVsfpTDMWSVGVITYMLLSGLSPFLGETDAETMNNIV 216
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
155-352 1.64e-16

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: 81.55  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQ----IEVRLLELMN-KHDtemkyYIVHLKRHFMFRNHLCLVF 229
Cdd:cd05604     3 VIGKGSFGKVLLAKRKRDGKYYAVKVLQ-KKVILNRKEqkhiMAERNVLLKNvKHP-----FLVGLHYSFQTTDKLYFVL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQLGQ 307
Cdd:cd05604    77 DFVNGGelFFHLQRERSF---PEPRARFYAAEIASALGYLHS--INIVYRDLKPENILL--DSQGHIVLTDFGL-CKEGI 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1113820495 308 RIYQ----YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd05604   149 SNSDttttFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPF 197
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
150-373 1.68e-16

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 79.96  E-value: 1.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKA-------YDRVEQEWVAIK-IIKNK--KAFLNqaqiEVRLLELMNKHDtemkyYIVHLKRHF 219
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAedklhdlYDRNKGRLVALKhIYPTSspSRILN----ELECLERLGGSN-----NVSGLITAF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSYNLY-DLLRNTNFRGvslnlTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcNPKRSAIKIVD 298
Cdd:cd14019    74 RNEDQVVAVLPYIEHDDFrDFYRKMSLTD-----IRIYLRNLFKALKHVH--SFGIIHRDVKPGNFLY-NRETGKGVLVD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 FGsscqLGQRIYQYIQ-------SRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGE-PLFSGANEVDQMNKIVEVLG 369
Cdd:cd14019   146 FG----LAQREEDRPEqrapragTRGFRAPEVLFKCPHQtTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATIFG 221

                  ....
gi 1113820495 370 IPPA 373
Cdd:cd14019   222 SDEA 225
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
155-372 2.10e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 80.49  E-value: 2.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIevrLLELmnkhDTEMKY----YIVhlkRHF--MFRNHLCLV 228
Cdd:cd06616    13 EIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEQKRL---LMDL----DVVMRSsdcpYIV---KFYgaLFREGDCWI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 -FEMLSY---NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ 304
Cdd:cd06616    83 cMELMDIsldKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKE-ELKIIHRDVKPSNILL--DRNGNIKLCDFGISGQ 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 305 LGQRIYQYIQS--RFYRSPEVLL----GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEV-DQMNKIVEvlGIPP 372
Cdd:cd06616   160 LVDSIAKTRDAgcRPYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPKWNSVfDQLTQVVK--GDPP 232
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
156-366 2.67e-16

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: 79.40  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVkAYDRVEQE----WVAIKIIKNKKAFLNQAQIEVRLLELMNkHDTEMKYYivhlkRHFMFRNHLCLVFEM 231
Cdd:cd08221     8 LGRGAFGEAV-LYRKTEDNslvvWKEVNLSRLSEKERRDALNEIDILSLLN-HDNIITYY-----NHFLDGESLFIEMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLGQRiY 310
Cdd:cd08221    81 CNGgNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIH--KAGILHRDIKTLNIFLT--KADLVKLGDFGISKVLDSE-S 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 311 Q----YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd08221   156 SmaesIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQ 215
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
151-372 2.80e-16

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: 79.51  E-value: 2.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  151 EIDSLIGKGSFGQVVKAY----DRVEQEWVAIKIIKN------KKAFLNQAQIevrlleLMN-KHDTEMKYYIVHLKRHf 219
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEdaseqqIEEFLREARI------MRKlDHPNIVKLLGVCTEEE- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  220 mfrnHLCLVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVD 298
Cdd:smart00221  75 ----PLMIVMEYMPGgDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLE--SKNFIHRDLAARNCLVGENLV--VKISD 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  299 FGSSCQLGQriYQYI---QSRF-YR--SPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGANEVDQMNKIVE--VLG 369
Cdd:smart00221 147 FGLSRDLYD--DDYYkvkGGKLpIRwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKgyRLP 224

                   ...
gi 1113820495  370 IPP 372
Cdd:smart00221 225 KPP 227
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
150-350 4.06e-16

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: 78.89  E-value: 4.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK-NKKAFLNQAQIEVRLLELMNkHDTEMKYYIVHLKRHFMFrnhLCLV 228
Cdd:cd06613     2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKlEPGDDFEIIQQEISMLKECR-HPNIVAYFGSYLRRDKLW---IVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 F------EMLsYNLYDLLRNTNFRGVSlnltrkfaQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSS 302
Cdd:cd06613    78 YcgggslQDI-YQVTGPLSELQIAYVC--------RETLKGLAYLH--STGKIHRDIKGANILLT--EDGDVKLADFGVS 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 303 CQLGQRIYQ---YIQSRFYRSPEVLL---GMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06613   145 AQLTATIAKrksFIGTPYWMAPEVAAverKGGYDGKCDIWALGITAIELAELQP 198
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
145-379 4.37e-16

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: 78.85  E-value: 4.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KW-MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkKAFLNQAQIEVRLlelmnKHDTEMKYYIVH--LKRHFMF 221
Cdd:cd14116     1 QWaLEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLF--KAQLEKAGVEHQL-----RREVEIQSHLRHpnILRLYGY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSY----NLY-DLLRNTNFRGvslNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNpkRSAIKI 296
Cdd:cd14116    74 FHDATRVYLILEYaplgTVYrELQKLSKFDE---QRTATYITELANALSYCHSK--RVIHRDIKPENLLLGS--AGELKI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 297 VDFGSSCQL-GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHI 375
Cdd:cd14116   147 ADFGWSVHApSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFV 226

                  ....
gi 1113820495 376 LDQA 379
Cdd:cd14116   227 TEGA 230
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
148-353 4.95e-16

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: 78.94  E-value: 4.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK--AFLNQAQIEVRLLELMNkHDTEMKYYIvhlkrHFMFRNHL 225
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKcqTSMDELRKEIQAMSQCN-HPNVVSYYT-----SFVVGDEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRNTNFRGV-SLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILLCNPKrsAIKIVDFGSSC 303
Cdd:cd06610    75 WLVMPLLSGgSLLDIMKSSYPRGGlDEAIIATVLKEVLKGLEYLHSNGQ--IHRDVKAGNILLGEDG--SVKIADFGVSA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 304 QL---GQRI----YQYIQSRFYRSPEVL-LGMPYDLAIDMWSLGCILVEMHTGEPLFS 353
Cdd:cd06610   151 SLatgGDRTrkvrKTFVGTPCWMAPEVMeQVRGYDFKADIWSFGITAIELATGAAPYS 208
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
156-409 5.07e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 78.93  E-value: 5.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIeVRLLELMNKHDTEmkyYIVHLKRHFMFRNHLCLVFE-MLSY 234
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALQKQI-LRELDVLHKCNSP---YIVGFYGAFYSEGDISICMEyMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQ-YI 313
Cdd:cd06605    85 SLDKILKEVG--RIPERILGKIAVAVVKGLIYLHE-KHKIIHRDVKPSNILV--NSRGQVKLCDFGVSGQLVDSLAKtFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 314 QSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNkIVEVLgippAHILDQAPKarkffeKLPDGT 393
Cdd:cd06605   160 GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMM-IFELL----SYIVDEPPP------LLPSGK 228
                         250       260
                  ....*....|....*....|....
gi 1113820495 394 W--------NLKKTKDGKREYKPP 409
Cdd:cd06605   229 FspdfqdfvSQCLQKDPTERPSYK 252
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
220-351 5.23e-16

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: 79.21  E-value: 5.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHL-------CLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcNPKRS 292
Cdd:cd14020    72 VFTNHYsanvpsrCLLLELLDVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHE--GYVHADLKPRNILW-SAEDE 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 293 AIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLL-------GMPYD----LAIDMWSLGCILVEMHTGEPL 351
Cdd:cd14020   149 CFKLIDFGLSFKEGNQDVKYIQTDGYRAPEAELqnclaqaGLQSEtectSAVDLWSLGIVLLEMFSGMKL 218
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
155-366 6.22e-16

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 79.54  E-value: 6.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLE--LMNKHDTEmkyYIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIR-KAHIVSRSEVTHTLAErtVLAQVDCP---FIVPLKFSFQSPEKLYLVLAFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SYN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQLG---- 306
Cdd:cd05585    77 NGGelFHHLQREGRF---DLSRARFYTAELLCALECLH--KFNVIYRDLKPENILL--DYTGHIALCDFGL-CKLNmkdd 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 307 QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05585   149 DKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQ 208
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
150-391 7.27e-16

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: 78.07  E-value: 7.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQI-----EVRLLELMNkHDtemkyYIVHLKRHFMFRNH 224
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYM-NKQKCIEKDSVrnvlnELEILQELE-HP-----FLVNLWYSFQDEED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFE-MLSYNL-YDLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSS 302
Cdd:cd05578    75 MYMVVDlLLGGDLrYHLQQKVKF---SEETVKFYICEIVLALDYLH--SKNIIHRDIKPDNILL--DEQGHVHITDFNIA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF-----SGANEVDQMNKIVEVLgIPPAHI 375
Cdd:cd05578   148 TKLtdGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYeihsrTSIEEIRAKFETASVL-YPAGWS 226
                         250
                  ....*....|....*.
gi 1113820495 376 LDQAPKARKFFEKLPD 391
Cdd:cd05578   227 EEAIDLINKLLERDPQ 242
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
150-471 8.00e-16

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 78.83  E-value: 8.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAflnQAQIEVRLLelmnkhdteMKY----YIVHLKRHFMFRNHL 225
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKR---DPSEEIEIL---------LRYgqhpNIITLRDVYDDGNSV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLsynlydllrntnfRGVSL--NLTRK--FAQQMCTALLFLATPELSIIHC------DLKPENILLCNPKR--SA 293
Cdd:cd14091    70 YLVTELL-------------RGGELldRILRQkfFSEREASAVMKTLTKTVEYLHSqgvvhrDLKPSNILYADESGdpES 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 IKIVDFGSSCQLgqriyqyiqsRF-------------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF-SGANEvd 359
Cdd:cd14091   137 LRICDFGFAKQL----------RAengllmtpcytanFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFaSGPND-- 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 360 qmnkivevlgiPPAHILDQAPKArKFfeKLPDGTWNlkktkdgkreykppgtrklhnilgvetggpggrragesghTVAD 439
Cdd:cd14091   205 -----------TPEVILARIGSG-KI--DLSGGNWD----------------------------------------HVSD 230
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1113820495 440 ylKFKDLILRMLDYDPKTRIQPYYALQHSFFK 471
Cdd:cd14091   231 --SAKDLVRKMLHVDPSQRPTAAQVLQHPWIR 260
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
149-353 9.90e-16

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: 77.66  E-value: 9.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQV---VKAYDRVEqewVAIKIIkNKKAFLNQAQI--------EVRLLELMNKHDTEmkyYIVHLKR 217
Cdd:cd14005     1 QYEVGDLLGKGGFGTVysgVRIRDGLP---VAVKFV-PKSRVTEWAMIngpvpvplEIALLLKASKPGVP---GVIRLLD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFRNHLCLVFE--MLSYNLYDLLRNtnfRGV-SLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcNPKRSAI 294
Cdd:cd14005    74 WYERPDGFLLIMErpEPCQDLFDFITE---RGAlSENLARIIFRQVVEAVRHCH--QRGVLHRDIKDENLLI-NLRTGEV 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 295 KIVDFGSSCQLGQRIYQ-YIQSRFYRSPEVLL-GMPYDLAIDMWSLGCILVEMHTGEPLFS 353
Cdd:cd14005   148 KLIDFGCGALLKDSVYTdFDGTRVYSPPEWIRhGRYHGRPATVWSLGILLYDMLCGDIPFE 208
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
150-371 1.02e-15

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 77.76  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII------KNKKAFLNQAQIEVRLLELMnKHDTEMKYYivHLKRHFMFRN 223
Cdd:cd06653     4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfdpdsQETSKEVNALECEIQLLKNL-RHDRIVQYY--GCLRDPEEKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILlcnpKRSA--IKIVDFGS 301
Cdd:cd06653    81 LSIFVEYMPGGSVKDQLKA--YGALTENVTRRYTRQILQGVSYLHSN--MIVHRDIKGANIL----RDSAgnVKLGDFGA 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 302 S------CQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQMNKIVEVLGIP 371
Cdd:cd06653   153 SkriqtiCMSGTGIKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKIATQP 225
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
149-352 1.23e-15

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: 78.25  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKA-YDRVEQEWVAIKIIKnkKAFLNQAQIEV----RLLELMNKHDTEMKYYIVHLKRHFMFRN 223
Cdd:cd14096     2 NYRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVR--KADLSSDNLKGssraNILKEVQIMKRLSHPNIVKLLDFQESDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYD-LLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL--------CNPKRSA 293
Cdd:cd14096    80 YYYIVLELADGgEIFHqIVRLTYF---SEDLSRHVITQVASAVKYLH--EIGVVHRDIKPENLLFepipfipsIVKLRKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 -----------------------IKIVDFGSSCQLGQRIYQYIQSRF-YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE 349
Cdd:cd14096   155 dddetkvdegefipgvggggigiVKLADFGLSKQVWDSNTKTPCGTVgYTAPEVVKDERYSKKVDMWALGCVLYTLLCGF 234

                  ...
gi 1113820495 350 PLF 352
Cdd:cd14096   235 PPF 237
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
145-357 1.53e-15

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: 78.97  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLELMNKHDTEMKYyIVHLKRHFMFRNH 224
Cdd:cd05593    12 KTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILK-KEVIIAKDEVAHTLTESRVLKNTRHPF-LTSLKYSFQTKDR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSs 302
Cdd:cd05593    90 LCFVMEYVNGGelFFHLSRERVF---SEDRTRFYGAEIVSALDYLHSGK--IVYRDLKLENLML--DKDGHIKITDFGL- 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 CQLG----QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE-PLFSGANE 357
Cdd:cd05593   162 CKEGitdaATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE 221
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
151-347 1.82e-15

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: 76.77  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAY-----DRVEQEwVAIKIIKN------KKAFLNQAQIevrLLELMNKHdtemkyyIVHLKRHF 219
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGTlkgegENTKIK-VAVKTLKEgadeeeREDFLEEASI---MKKLDHPN-------IVKLLGVC 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSY-NLYDLLRNtnfRGVSLNLTRK--FAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKI 296
Cdd:pfam07714  71 TQGEPLYIVTEYMPGgDLLDFLRK---HKRKLTLKDLlsMALQIAKGMEYLE--SKNFVHRDLAARNCLVSENLV--VKI 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 297 VDFGSScQLGQRIYQYIQSR------FYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:pfam07714 144 SDFGLS-RDIYDDDYYRKRGggklpiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFT 199
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
144-470 1.82e-15

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 77.32  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 144 EKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI---------EVRLLELMNKHDTEMKYYIVH 214
Cdd:cd14181     6 KEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSPEQLeevrsstlkEIHILRQVSGHPSIITLIDSY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 215 LKRHFMFrnhlcLVFEMLSY-NLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSA 293
Cdd:cd14181    86 ESSTFIF-----LVFDLMRRgELFDYL--TEKVTLSEKETRSIMRSLLEAVSYLHA--NNIVHRDLKPENILL--DDQLH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 IKIVDFGSSCQL--GQRIYQYIQSRFYRSPEVL-LGMP-----YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd14181   155 IKLSDFGFSCHLepGEKLRELCGTPGYLAPEILkCSMDethpgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 366 EvlgippahildqapkarkffeklpdgtwnlkktkdGKREYKPPgtrklhnilgvetggpggrRAGESGHTVadylkfKD 445
Cdd:cd14181   235 E-----------------------------------GRYQFSSP-------------------EWDDRSSTV------KD 254
                         330       340
                  ....*....|....*....|....*
gi 1113820495 446 LILRMLDYDPKTRIQPYYALQHSFF 470
Cdd:cd14181   255 LISRLLVVDPEIRLTAEQALQHPFF 279
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
141-366 2.20e-15

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 77.78  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 141 KNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMN-KHDTemkyyIVHLKRHF 219
Cdd:cd14168     3 KQVEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKiKHEN-----IVALEDIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSY-NLYDLLRNTNFrgvslnLTRKFA----QQMCTALLFLATpeLSIIHCDLKPENILLCNPKR-SA 293
Cdd:cd14168    78 ESPNHLYLVMQLVSGgELFDRIVEKGF------YTEKDAstliRQVLDAVYYLHR--MGIVHRDLKPENLLYFSQDEeSK 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 294 IKIVDFGSSCQ--LGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14168   150 IMISDFGLSKMegKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK 224
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
118-389 2.68e-15

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 78.90  E-value: 2.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 118 SSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRL 197
Cdd:cd05624    42 SPLRRDKYVSEFLEWAKPFTQLVKEMQLHRDDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKIL-NKWEMLKRAETACFR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 198 LE---LMNKhDTEmkyYIVHLKRHFMFRNHLCLVFEM-LSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLflATPELS 273
Cdd:cd05624   121 EErnvLVNG-DCQ---WITTLHYAFQDENYLYLVMDYyVGGDLLTLLSKFEDK-LPEDMARFYIGEMVLAIH--SIHQLH 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 274 IIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRiyQYIQSRF------YRSPEVLLGM-----PYDLAIDMWSLGCIL 342
Cdd:cd05624   194 YVHRDIKPDNVLL--DMNGHIRLADFGSCLKMNDD--GTVQSSVavgtpdYISPEILQAMedgmgKYGPECDWWSLGVCM 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1113820495 343 VEMHTGEPLFSGANEVDQMNKIV--EVLGIPPAHILDQAPKARKFFEKL 389
Cdd:cd05624   270 YEMLYGETPFYAESLVETYGKIMnhEERFQFPSHVTDVSEEAKDLIQRL 318
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
148-352 3.03e-15

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 77.17  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---NKKAFlnQAQIEVrLLELMNKHdtemkyyIVHLKRHFMFRNH 224
Cdd:cd14085     3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKktvDKKIV--RTEIGV-LLRLSHPN-------IIKLKEIFETPTE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSA-IKIVDFGSS 302
Cdd:cd14085    73 ISLVLELVTGgELFDRIVEKGY--YSERDAADAVKQILEAVAYLH--ENGIVHRDLKPENLLYATPAPDApLKIADFGLS 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 303 CQLGQRIYQ--YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG-EPLF 352
Cdd:cd14085   149 KIVDQQVTMktVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGfEPFY 201
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
155-366 3.24e-15

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 77.35  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQ----AQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05616     7 VLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDdvecTMVEKRVLALSGKPP-----FLTQLHSCFQTMDRLYFVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 M-----LSYNLYDLLRNTNFRGVSlnltrkFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQl 305
Cdd:cd05616    82 YvnggdLMYHIQQVGRFKEPHAVF------YAAEIAIGLFFLQSK--GIIYRDLKLDNVML--DSEGHIKIADFGM-CK- 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 306 gQRIYQYIQSRF------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05616   150 -ENIWDGVTTKTfcgtpdYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIME 215
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
155-358 3.83e-15

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 77.01  E-value: 3.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQI-----EVRLLELMnKHD--TEMKYyivhlkrHFMFRNHLCL 227
Cdd:cd05571     2 VLGKGTFGKVILCREKATGELYAIKILK-KEVIIAKDEVahtltENRVLQNT-RHPflTSLKY-------SFQTNDRLCF 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQL 305
Cdd:cd05571    73 VMEYVNGGelFFHLSRERVF---SEDRTRFYGAEIVLALGYLH--SQGIVYRDLKLENLLL--DKDGHIKITDFGL-CKE 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 306 GQRiYQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE-PLFSGANEV 358
Cdd:cd05571   145 EIS-YGATTKTFcgtpeYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNRDHEV 202
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
149-356 4.53e-15

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: 75.63  E-value: 4.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkKAFLNQAQI-----EVRLLELMNKHDtemkyyIVHLKRHFMFRN 223
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIID--KTQLNPSSLqklfrEVRIMKILNHPN------IVKLFEVIETEK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTNfRGVSLNLTRKFaQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSS 302
Cdd:cd14072    73 TLYLVMEYASGgEVFDYLVAHG-RMKEKEARAKF-RQIVSAVQYCH--QKRIVHRDLKAENLLL--DADMNIKIADFGFS 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 303 CQ--LGQRIYQYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14072   147 NEftPGNKLDTFCGSPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQN 203
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
156-350 4.59e-15

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: 76.04  E-value: 4.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKA-YDRVEQEW--VAIKIIKNKKafLNQAQIE-VRLLELMNK--HDtemkyYIVHL-----KRHfmfrnH 224
Cdd:cd00192     3 LGEGAFGEVYKGkLKGGDGKTvdVAVKTLKEDA--SESERKDfLKEARVMKKlgHP-----NVVRLlgvctEEE-----P 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTNFRGVSLNLTR-------KFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKI 296
Cdd:cd00192    71 LYLVMEYMEGgDLLDFLRKSRPVFPSPEPSTlslkdllSFAIQIAKGMEYLA--SKKFVHRDLAARNCLVGEDLV--VKI 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 297 VDFGsscqLGQRIYQYiqsRFYR------------SPEVLLGMPYDLAIDMWSLGCILVEMHT--GEP 350
Cdd:cd00192   147 SDFG----LSRDIYDD---DYYRkktggklpirwmAPESLKDGIFTSKSDVWSFGVLLWEIFTlgATP 207
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
156-358 4.77e-15

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: 75.88  E-value: 4.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQewVAIKIIK---NKKAFLNQAQIEVRLLELmnKHDTEMKyyIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd13979    11 LGSGGFGSVYKATYKGET--VAVKIVRrrrKNRASRQSFWAELNAARL--RHENIVR--VLAAETGTDFASLGLIIMEYC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 -SYNLYDLLrNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLGQ-RIY 310
Cdd:cd13979    85 gNGTLQQLI-YEGSEPLPLAHRILISLDIARALRFCHSH--GIVHLDVKPANILIS--EQGVCKLCDFGCSVKLGEgNEV 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 311 QYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEV 358
Cdd:cd13979   160 GTPRSHIggtytYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQH 212
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
156-357 5.38e-15

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: 76.24  E-value: 5.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKI-----IKNKKAfLNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05605     8 LGKGGFGEVCACQVRATGKMYACKKlekkrIKKRKG-EAMALNEKQILEKVNSR------FVVSLAYAYETKDALCLVLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLsyNLYDL---LRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQL-- 305
Cdd:cd05605    81 IM--NGGDLkfhIYNMGNPGFEEERAVFYAAEITCGLEHLHS--ERIVYRDLKPENILLDD--HGHVRISDLGLAVEIpe 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 306 GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANE 357
Cdd:cd05605   155 GETIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKE 206
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
156-359 5.55e-15

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 75.94  E-value: 5.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIeVRLLELMNKHDTEmkyYIVHLKRHFMFR-NHLCLVFEMLSY 234
Cdd:cd06620    13 LGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVRKQI-LRELQILHECHSP---YIVSFYGAFLNEnNNIIICMEYMDC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYD-LLRNtnFRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQLGQRIYQ-Y 312
Cdd:cd06620    89 GSLDkILKK--KGPFPEEVLGKIAVAVLEGLTYLYN-VHRIIHRDIKPSNILVNS--KGQIKLCDFGVSGELINSIADtF 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1113820495 313 IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVD 359
Cdd:cd06620   164 VGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDD 210
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
150-379 5.71e-15

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: 75.37  E-value: 5.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLL-----------ELMNKHDTEMKYYIVhlkrh 218
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIESEILiikslshpnivKLFEVYETEKEIYLI----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 fmfrnhlclvfemLSY----NLYDLLRNtnfrgvSLNLTRKFAQQM----CTALLFLATPelSIIHCDLKPENILLC-NP 289
Cdd:cd14185    77 -------------LEYvrggDLFDAIIE------SVKFTEHDAALMiidlCEALVYIHSK--HIVHRDLKPENLLVQhNP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 290 KRS-AIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF-SGANEVDQMNKIVEv 367
Cdd:cd14185   136 DKStTLKLADFGLAKYVTGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFrSPERDQEELFQIIQ- 214
                         250
                  ....*....|....*...
gi 1113820495 368 LG----IPP--AHILDQA 379
Cdd:cd14185   215 LGhyefLPPywDNISEAA 232
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
148-342 8.03e-15

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: 75.11  E-value: 8.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAF---LNQAQIEVRLL-ELMNKHDTEMKYYIVHLKRHFMFRN 223
Cdd:cd14078     3 KYYELHETIGSGGFAKVKLATHILTGEKVAIKIM-DKKALgddLPRVKTEIEALkNLSHQHICRLYHVIETDNKIFMVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HlCLVFEMLSYNL-YDLLRNTNfrgvslnlTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSS 302
Cdd:cd14078    82 Y-CPGGELFDYIVaKDRLSEDE--------ARVFFRQIVSAVAYVHS--QGYAHRDLKPENLLL--DEDQNLKLIDFGLC 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 303 CQ----LGQRIYQYIQSRFYRSPEVLLGMPY-DLAIDMWSLGCIL 342
Cdd:cd14078   149 AKpkggMDHHLETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLL 193
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
150-352 8.27e-15

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: 75.02  E-value: 8.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDS-LIGKGSFGQVVKAYDRVEQEWVAIKIIK-NKKAflnqaQIEVRLLELMNKHDtemkyYIVHLKRHF--MFRNHL 225
Cdd:cd14089     2 YTISKqVLGLGINGKVLECFHKKTGEKFALKVLRdNPKA-----RREVELHWRASGCP-----HIVRIIDVYenTYQGRK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CL--VFEMLSYNlyDLLRNTNFRGVSLNLTRKFAQ---QMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAI-KIVDF 299
Cdd:cd14089    72 CLlvVMECMEGG--ELFSRIQERADSAFTEREAAEimrQIGSAVAHLH--SMNIAHRDLKPENLLYSSKGPNAIlKLTDF 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 300 G------SSCQLGQRIYqyiqSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14089   148 GfakettTKKSLQTPCY----TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPF 202
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
150-366 8.51e-15

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: 74.93  E-value: 8.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNkHDTemkyyIVHLKRHFMFRNHLCLVF 229
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQERDILARLS-HRR-----LTCLLDQFETRKTLILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNlyDLLRNTNFRGVSLNLTRK-FAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQR 308
Cdd:cd14107    78 ELCSSE--ELLDRLFLKGVVTEAEVKlYIQQVLEGIGYLH--GMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPS 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 309 IYQYIQ--SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14107   154 EHQFSKygSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAE 213
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
149-347 8.95e-15

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: 75.01  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLN--QAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNHLC 226
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAveDSRKEAVLLAKM-KHPN-----IVAFKESFEADGHLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNlyDLLRNTNFRGVSL---NLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSC 303
Cdd:cd08219    75 IVMEYCDGG--DLMQKIKLQRGKLfpeDTILQWFVQMCLGVQHIH--EKRVLHRDIKSKNIFLT--QNGKVKLGDFGSAR 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1113820495 304 QL---GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd08219   149 LLtspGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCT 195
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
151-372 9.11e-15

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 74.87  E-value: 9.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  151 EIDSLIGKGSFGQVVKAY-----DRVEQEwVAIKIIKN------KKAFLNQAQIevrlleLMN-KHDTEMKYYIVHLKRH 218
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgkgGKKKVE-VAVKTLKEdaseqqIEEFLREARI------MRKlDHPNVVKLLGVCTEEE 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  219 fmfrnHLCLVFEMLSY-NLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIV 297
Cdd:smart00219  75 -----PLYIVMEYMEGgDLLSYLRKNR-PKLSLSDLLSFALQIARGMEYLE--SKNFIHRDLAARNCLVGENLV--VKIS 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  298 DFGSSCQLGQRIYQYIQSR----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGANEVDQMNKIV--EVLGI 370
Cdd:smart00219 145 DFGLSRDLYDDDYYRKRGGklpiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKngYRLPQ 224

                   ..
gi 1113820495  371 PP 372
Cdd:smart00219 225 PP 226
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
148-355 1.19e-14

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 75.14  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEI-DSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQI--EVRLLELMNKHDTemkyyIVHLKRHFMFRNH 224
Cdd:cd14090     1 DLYKLtGELLGEGAYASVQTCINLYTGKEYAVKII-EKHPGHSRSRVfrEVETLHQCQGHPN-----ILQLIEYFEDDER 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYNlyDLLRNTNFRGvslNLTRKFAQQ----MCTALLFLATPelSIIHCDLKPENILLCNP-KRSAIKIVDF 299
Cdd:cd14090    75 FYLVFEKMRGG--PLLSHIEKRV---HFTEQEASLvvrdIASALDFLHDK--GIAHRDLKPENILCESMdKVSPVKICDF 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 300 --GSSCQLGQRIYQYIQ---------SRFYRSPEVL-----LGMPYDLAIDMWSLGCILVEMHTGEPLFSGA 355
Cdd:cd14090   148 dlGSGIKLSSTSMTPVTtpelltpvgSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGR 219
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
156-369 1.24e-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: 74.62  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEwVAIKIIK--NKKAFLNQAQIEVRLLeLMNKHDTEMKYYIVHLKRHFMfrnhlCLVFE-ML 232
Cdd:cd14066     1 IGSGGFGTVYKGVLENGTV-VAVKRLNemNCAASKKEFLTELEML-GRLRHPNLVRLLGYCLESDEK-----LLVYEyMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SYNLYDLLRNTNFRGV-SLNLTRKFAQQMCTALLFLAT-PELSIIHCDLKPENILL---CNPkrsaiKIVDFGSSCQLGQ 307
Cdd:cd14066    74 NGSLEDRLHCHKGSPPlPWPQRLKIAKGIARGLEYLHEeCPPPIIHGDIKSSNILLdedFEP-----KLTDFGLARLIPP 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 308 RIYQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLG 369
Cdd:cd14066   149 SESVSKTSAVkgtigYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEWVE 215
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
148-352 1.76e-14

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 74.57  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII---------KNKKAFLNQAQI-EVRLLELMNKHDTemkyyIVHLKR 217
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIditgggsfsPEEVQELREATLkEIDILRKVSGHPN-----IIQLKD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMFRNHLCLVFEMLSY-NLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRsaIKI 296
Cdd:cd14182    78 TYETNTFFFLVFDLMKKgELFDYL--TEKVTLSEKETRKIMRALLEVICALHK--LNIVHRDLKPENILLDDDMN--IKL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 297 VDFGSSCQL--GQRIYQYIQSRFYRSPEVL-LGMP-----YDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14182   152 TDFGFSCQLdpGEKLREVCGTPGYLAPEIIeCSMDdnhpgYGKEVDMWSTGVIMYTLLAGSPPF 215
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
149-364 1.85e-14

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: 74.43  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEidsLIGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMNKHDTE--MKYYIVHLKRhfmfrNH 224
Cdd:cd06917     5 RLE---LVGRGSYGAVYRGYHVKTGRVVALKVLNldTDDDDVSDIQKEVALLSQLKLGQPKniIKYYGSYLKG-----PS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTNF--RGVSLnLTRKFAQqmctALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDFGS 301
Cdd:cd06917    77 LWIIMDYCEGgSIRTLMRAGPIaeRYIAV-IMREVLV----ALKFIH--KDGIIHRDIKAANILVTNTGN--VKLCDFGV 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 302 SCQLGQ---RIYQYIQSRFYRSPEVLL-GMPYDLAIDMWSLGCILVEMHTGEPLFSGaneVDQMNKI 364
Cdd:cd06917   148 AASLNQnssKRSTFVGTPYWMAPEVITeGKYYDTKADIWSLGITTYEMATGNPPYSD---VDALRAV 211
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
150-350 1.99e-14

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 74.27  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFR-NHLCLV 228
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHdDQLWLV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEML-SYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLGQ 307
Cdd:cd06636    98 MEFCgAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHK--VIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDR 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 308 ---RIYQYIQSRFYRSPEVLL-----GMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06636   174 tvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAP 224
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
149-356 2.08e-14

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: 73.57  E-value: 2.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiiKNKKAFL-----NQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMF-R 222
Cdd:cd13997     1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVK--KSKKPFRgpkerARALREVEAHAALGQHPNIVRYYSSWEEGGHLYiQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLvfemlSYNLYDLL-RNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGS 301
Cdd:cd13997    79 MELCE-----NGSLQDALeELSPISKLSEAEVWDLLLQVALGLAFIH--SKGIVHLDIKPDNIFISN--KGTCKIGDFGL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 302 SCQLGQRI-YQYIQSRfYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd13997   150 ATRLETSGdVEEGDSR-YLAPELLNENYtHLPKADIFSLGVTVYEAATGEPLPRNGQ 205
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
148-360 2.23e-14

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 73.91  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIE--VRLLELMnKHDTemkyyIVHLKRHFMFRNHL 225
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIEneVSILRRV-KHPN-----IIMLIEEMDTPAEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRNtnfrgvSLNLTRKFAQQM----CTALLFLATpeLSIIHCDLKPENILLCN--PKRSAIKIVD 298
Cdd:cd14184    75 YLVMELVKGgDLFDAITS------STKYTERDASAMvynlASALKYLHG--LCIVHRDIKPENLLVCEypDGTKSLKLGD 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 299 FGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd14184   147 FGLATVVEGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQE 208
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
149-365 2.35e-14

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: 73.69  E-value: 2.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK---IIKNKKAFLNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNHL 225
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKeinISKMSPKEREESRKEVAVLSKM-KHPN-----IVQYQESFEENGNL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNlyDLLRNTNF-RGVSL--NLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFG-- 300
Cdd:cd08218    75 YIVMDYCDGG--DLYKRINAqRGVLFpeDQILDWFVQLCLALKHVH--DRKILHRDIKSQNIFLT--KDGIIKLGDFGia 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 301 ----SSCQLGQriyQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd08218   149 rvlnSTVELAR---TCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKII 214
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
148-360 2.99e-14

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 73.49  E-value: 2.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI--EVRLLELMnKHDTemkyyIVHLKRHFMFRNHL 225
Cdd:cd14183     6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEHMIqnEVSILRRV-KHPN-----IVLLIEEMDMPTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRNTNfrgvslnltrKFAQQMCTALLF-LATP-----ELSIIHCDLKPENILLCNPK--RSAIKI 296
Cdd:cd14183    80 YLVMELVKGgDLFDAITSTN----------KYTERDASGMLYnLASAikylhSLNIVHRDIKPENLLVYEHQdgSKSLKL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 297 VDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEvDQ 360
Cdd:cd14183   150 GDFGLATVVDGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGD-DQ 212
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
150-367 3.09e-14

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 73.42  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSL-IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLN-QAQI--EVRLLELmnkhdTEMKYYIVHLKRHFMFRNHL 225
Cdd:cd14198     9 YILTSKeLGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDcRAEIlhEIAVLEL-----AKSNPRVVNLHEVYETTSEI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLC--NPkRSAIKIVDFGSS 302
Cdd:cd14198    84 ILILEYAAGgEIFNLCVPDLAEMVSENDIIRLIRQILEGVYYLH--QNNIVHLDLKPQNILLSsiYP-LGDIKIVDFGMS 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 303 CQLGQ--RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV 367
Cdd:cd14198   161 RKIGHacELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQV 227
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
147-357 3.35e-14

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 74.68  E-value: 3.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLElmNKHDTEMKY-YIVHLKRHFMFRNHL 225
Cdd:cd05594    24 MNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILK-KEVIVAKDEVAHTLTE--NRVLQNSRHpFLTALKYSFQTHDRL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLcnPKRSAIKIVDFG--- 300
Cdd:cd05594   101 CFVMEYANGGelFFHLSRERVF---SEDRARFYGAEIVSALDYLHS-EKNVVYRDLKLENLML--DKDGHIKITDFGlck 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 301 SSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE-PLFSGANE 357
Cdd:cd05594   175 EGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE 232
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
155-357 3.48e-14

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: 74.27  E-value: 3.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQI-----EVRLLElMNKHDtemkyYIVHLKRHFMFRNHLCLVF 229
Cdd:cd05595     2 LLGKGTFGKVILVREKATGRYYAMKILR-KEVIIAKDEVahtvtESRVLQ-NTRHP-----FLTALKYAFQTHDRLCFVM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSsCQLG- 306
Cdd:cd05595    75 EYANGGelFFHLSRERVF---TEDRARFYGAEIVSALEYLHSRD--VVYRDIKLENLML--DKDGHIKITDFGL-CKEGi 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 307 ---QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE-PLFSGANE 357
Cdd:cd05595   147 tdgATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRlPFYNQDHE 201
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
156-350 3.90e-14

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 73.55  E-value: 3.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnkkafLNQAQIEVRLLE----LMNKHDTE--MKYYIVHLKRhfmfrNHLCLVF 229
Cdd:cd06640    12 IGKGSFGEVFKGIDNRTQQVVAIKIID-----LEEAEDEIEDIQqeitVLSQCDSPyvTKYYGSYLKG-----TKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSY-NLYDLLRNTNFRGVSLNLTRKfaqQMCTALLFLATPELsiIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQ- 307
Cdd:cd06640    82 EYLGGgSALDLLRAGPFDEFQIATMLK---EILKGLDYLHSEKK--IHRDIKAANVLL--SEQGDVKLADFGVAGQLTDt 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 308 --RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06640   155 qiKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEP 199
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
155-366 4.85e-14

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 74.26  E-value: 4.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSY 234
Cdd:cd05615    17 VLGKGSFGKVMLAERKGSDELYAIKILK-KDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 N--LYDLLRNTNFRGVSLNLtrkFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQlgQRIYQY 312
Cdd:cd05615    96 GdlMYHIQQVGKFKEPQAVF---YAAEISVGLFFLH--KKGIIYRDLKLDNVML--DSEGHIKIADFGM-CK--EHMVEG 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 313 IQSRF------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05615   166 VTTRTfcgtpdYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIME 225
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
155-352 4.87e-14

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: 73.13  E-value: 4.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK--------AFLNQAQIevrlLELMNKHdtemkyYIVHLKRHFMFRNHLC 226
Cdd:cd05630     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRikkrkgeaMALNEKQI----LEKVNSR------FVVSLAYAYETKDALC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEM-----LSYNLYDLlrntNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNpkRSAIKIVDFGS 301
Cdd:cd05630    77 LVLTLmnggdLKFHIYHM----GQAGFPEARAVFYAAEICCGLEDLHRER--IVYRDLKPENILLDD--HGHIRISDLGL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 302 SCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd05630   149 AVHVpeGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPF 201
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
147-364 4.92e-14

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 72.62  E-value: 4.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK-----NKKAFLNQAQI--EVRLLELMNKHDTemkyyivhlkrhF 219
Cdd:cd14114     1 YDHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMtphesDKETVRKEIQImnQLHHPKLINLHDA------------F 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSY-NLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVD 298
Cdd:cd14114    69 EDDNEMVLILEFLSGgELFERIAAEHYK-MSEAEVINYMRQVCEGLCHMH--ENNIVHLDIKPENIMCTTKRSNEVKLID 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 299 FGSSCQLG--QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd14114   146 FGLATHLDpkESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNV 213
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
150-350 5.15e-14

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 73.60  E-value: 5.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFM-FRNHLCLV 228
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKNPPgMDDQLWLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEML-SYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLGQ 307
Cdd:cd06637    88 MEFCgAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLH--QHKVIHRDIKGQNVLLT--ENAEVKLVDFGVSAQLDR 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 308 ---RIYQYIQSRFYRSPEVLL-----GMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06637   164 tvgRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAP 214
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
148-364 5.75e-14

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: 72.63  E-value: 5.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNkHDTemkyyIVHLKRHFMFRNHLCL 227
Cdd:cd14108     2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSARRELALLAELD-HKS-----IVRFHDAFEKRRVVII 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLydLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQ 307
Cdd:cd14108    76 VTELCHEEL--LERITKRPTVCESEVRSYMRQLLEGIEYLHQND--VLHLDLKPENLLMADQKTDQVRICDFGNAQELTP 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 308 RIYQYIQ--SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd14108   152 NEPQYCKygTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI 210
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
149-370 6.14e-14

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 72.33  E-value: 6.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVrllelMNkHDTEMKYYIVHLKRHFMFRNHLCLV 228
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREI-----IN-HRSLRHPNIVRFKEVILTPTHLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLS-YNLYDllRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSAIKIVDFG--SSCQL 305
Cdd:cd14665    75 MEYAAgGELFE--RICNAGRFSEDEARFFFQQLISGVSYCHS--MQICHRDLKLENTLLDGSPAPRLKICDFGysKSSVL 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 306 GQRIYQYIQSRFYRSPEVLLGMPYDLAI-DMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE-VLGI 370
Cdd:cd14665   151 HSQPKSTVGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQrILSV 217
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
144-367 7.77e-14

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: 72.52  E-value: 7.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 144 EKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF-----LNQAQIE--VRLLELMNKHDtemkyyIVHLK 216
Cdd:cd14105     1 ENVEDFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasrrgVSREDIEreVSILRQVLHPN------IITLH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 217 RHFMFRNHLCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILL---CNPKrS 292
Cdd:cd14105    75 DVFENKTDVVLILELVAGgELFDFLAEK--ESLSEEEATEFLKQILDGVNYLHT--KNIAHFDLKPENIMLldkNVPI-P 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 293 AIKIVDFGSSCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV 367
Cdd:cd14105   150 RIKLIDFGLAHKIedGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV 226
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
156-371 8.89e-14

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 73.18  E-value: 8.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAY--DRVEQEWVAIKIIKNKKAFLNQAQiEVRLLELMnKHDTemkyyIVHLKRHFMFRN--HLCLVFEM 231
Cdd:cd07867    10 VGRGTYGHVYKAKrkDGKDEKEYALKQIEGTGISMSACR-EIALLREL-KHPN-----VIALQKVFLSHSdrKVWLLFDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYNLYDLLR-----NTNFRGVSL--NLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCN--PKRSAIKIVD---- 298
Cdd:cd07867    83 AEHDLWHIIKfhrasKANKKPMQLprSMVKSLLYQILDGIHYLHAN--WVLHRDLKPANILVMGegPERGRVKIADmgfa 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 299 --FGSSCQLGQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANE---------VDQMNKIVE 366
Cdd:cd07867   161 rlFNSPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFS 240

                  ....*
gi 1113820495 367 VLGIP 371
Cdd:cd07867   241 VMGFP 245
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
149-368 9.14e-14

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 72.98  E-value: 9.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEID---SLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAqiEVRLLELMNKHDTEMKYYIVHLKRHfmfrnHL 225
Cdd:cd14180     4 CYELDleePALGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQR--EVAALRLCQSHPNIVALHEVLHDQY-----HT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEML-SYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSA-IKIVDFGSSc 303
Cdd:cd14180    77 YLVMELLrGGELLDRIKKK--ARFSESEASQLMRSLVSAVSFMH--EAGVVHRDLKPENILYADESDGAvLKVIDFGFA- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 304 QLGQRIYQYIQSRF----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVL 368
Cdd:cd14180   152 RLRPQGSRPLQTPCftlqYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADIM 220
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
149-471 9.98e-14

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: 72.09  E-value: 9.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSL--IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMnkhdtEMKYY----IVHLKRHFMFR 222
Cdd:cd06648     6 RSDLDNFvkIGEGSTGIVCIATDKSTGRQVAVKKMDLRK----QQRRELLFNEVV-----IMRDYqhpnIVEMYSSYLVG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLSYN-LYDLLRNTNfrgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRsaIKIVDFGS 301
Cdd:cd06648    77 DELWVVMEFLEGGaLTDIVTHTR---MNEEQIATVCRAVLKALSFLHSQ--GVIHRDIKSDSILLTSDGR--VKLSDFGF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQLGQRIYQ---YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIvevlgippahildq 378
Cdd:cd06648   150 CAQVSKEVPRrksLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRI-------------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 379 apkarkffeklpdgtwnlkktkdgkREYKPPGTRKLHNILGVetggpggrragesghtvadylkFKDLILRMLDYDPKTR 458
Cdd:cd06648   216 -------------------------RDNEPPKLKNLHKVSPR----------------------LRSFLDRMLVRDPAQR 248
                         330
                  ....*....|...
gi 1113820495 459 IQPYYALQHSFFK 471
Cdd:cd06648   249 ATAAELLNHPFLA 261
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
157-354 1.07e-13

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 71.53  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 157 GKGSFGQVVKAYDRVEQEWVAIKIiknkkafLNQAQIEVRLLELMNkHDTEMKYYIVHLKRhfmfrNHLCLVFEMLSY-N 235
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKK-------LLKIEKEAEILSVLS-HRNIIQFYGAILEA-----PNYGIVTEYASYgS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 236 LYDLLRNTNFRGVSLNLTRKFAQQMCTALLFL-ATPELSIIHCDLKPENILLCNPkrSAIKIVDFGSSCQLGQRIYQYIQ 314
Cdd:cd14060    69 LFDYLNSNESEEMDMDQIMTWATDIAKGMHYLhMEAPVKVIHRDLKSRNVVIAAD--GVLKICDFGASRFHSHTTHMSLV 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1113820495 315 SRF-YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSG 354
Cdd:cd14060   147 GTFpWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKG 187
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
148-489 1.07e-13

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 72.07  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLiGKGSFGQVVKAYDRVEQEWVAIKIIKnkkAFLNQAQIEVRLLELmnkhDTEMK----YYIVHlkrhF---M 220
Cdd:cd06617     2 DLEVIEEL-GRGAYGVVDKMRHVPTGTIMAVKRIR---ATVNSQEQKRLLMDL----DISMRsvdcPYTVT----FygaL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNH---LCLvfEMLSYNLYDLLRNTNFRGVSL--NLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLcnPKRSAIK 295
Cdd:cd06617    70 FREGdvwICM--EVMDTSLDKFYKKVYDKGLTIpeDILGKIAVSIVKALEYLHS-KLSVIHRDVKPSNVLI--NRNGQVK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 296 IVDFGSSCQLGQRIYQYIQ--SRFYRSPEVLLG----MPYDLAIDMWSLGCILVEMHTGE-PLFSGANEVDQMNKIVEvl 368
Cdd:cd06617   145 LCDFGISGYLVDSVAKTIDagCKPYMAPERINPelnqKGYDVKSDVWSLGITMIELATGRfPYDSWKTPFQQLKQVVE-- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 369 GIPPahildqapkarkffeKLPDGTWNlkktkdgkreykppgtrklhnilgvetggpggrragesghtvadyLKFKDLIL 448
Cdd:cd06617   223 EPSP---------------QLPAEKFS---------------------------------------------PEFQDFVN 242
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1113820495 449 RMLDYDPKTRiqPYYA--LQHSFFKKTADEGTNTSNSVSTSPA 489
Cdd:cd06617   243 KCLKKNYKER--PNYPelLQHPFFELHLSKNTDVASFVSLILG 283
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
146-352 1.12e-13

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 71.93  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 146 WMDRYEID----SLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDtemkyYIVHLKRHFMF 221
Cdd:cd14113     1 WKDNFDSFysevAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTHELGVLQSL-QHP-----QLVGLLDTFET 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSYN-LYDLLRNTNfrgvslNLT----RKFAQQMCTALLFLATpeLSIIHCDLKPENILL-CNPKRSAIK 295
Cdd:cd14113    75 PTSYILVLEMADQGrLLDYVVRWG------NLTeekiRFYLREILEALQYLHN--CRIAHLDLKPENILVdQSLSKPTIK 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 296 IVDFGSSCQLGQR--IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14113   147 LADFGDAVQLNTTyyIHQLLGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPF 205
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
156-409 1.18e-13

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 72.43  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVV---KAYDRVEQEWVAIKIIKnkkaflnQAQIEVRllelmNKHDTEMKYYIVHLKRH-FMFRNHLCLVFEM 231
Cdd:cd05582     3 LGQGSFGKVFlvrKITGPDAGTLYAMKVLK-------KATLKVR-----DRVRTKMERDILADVNHpFIVKLHYAFQTEG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYNLYDLLRNTNFrgvslnLTRKFAQQMCT--------ALLFLATPEL---SIIHCDLKPENILLcnPKRSAIKIVDFG 300
Cdd:cd05582    71 KLYLILDFLRGGDL------FTRLSKEVMFTeedvkfylAELALALDHLhslGIIYRDLKPENILL--DEDGHIKLTDFG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 SSCQL---GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV-LGIPpaHIL 376
Cdd:cd05582   143 LSKESidhEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAkLGMP--QFL 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 377 DQAPKA--RKFFEKLP--------DGTWNLKK---------TKDGKREYKPP 409
Cdd:cd05582   221 SPEAQSllRALFKRNPanrlgagpDGVEEIKRhpffatidwNKLYRKEIKPP 272
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
155-347 1.23e-13

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 71.97  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKA-YDRVEQ---EWVAIKIIKNKKA-FLNQAQIEVRLLELMnKHDTEMKYYIVHLKRHfmfRNHLCLVF 229
Cdd:cd14205    11 QLGKGNFGSVEMCrYDPLQDntgEVVAVKKLQHSTEeHLRDFEREIEILKSL-QHDNIVKYKGVCYSAG---RRNLRLIM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSY-NLYDLLRNTNFRGVSLNLTrKFAQQMCTALLFLATPELsiIHCDLKPENILLCNPKRsaIKIVDFGSSCQLGQR 308
Cdd:cd14205    87 EYLPYgSLRDYLQKHKERIDHIKLL-QYTSQICKGMEYLGTKRY--IHRDLATRNILVENENR--VKIGDFGLTKVLPQD 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 309 iYQYIQSR-------FYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd14205   162 -KEYYKVKepgespiFWYAPESLTESKFSVASDVWSFGVVLYELFT 206
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
154-350 1.33e-13

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 72.03  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 154 SLIGKGSFGQVVKA-YDRVEQ---EWVAIKIIKNKKAFLNQAQIEvRLLELMNKHDTEmkyYIVHLK--RHFMFRNHLCL 227
Cdd:cd05038    10 KQLGEGHFGSVELCrYDPLGDntgEQVAVKSLQPSGEEQHMSDFK-REIEILRTLDHE---YIVKYKgvCESPGRRSLRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSY-NLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILLCNPKRsaIKIVDFGSSCQLG 306
Cdd:cd05038    86 IMEYLPSgSLRDYLQRHRDQ-IDLKRLLLFASQICKGMEYLGSQRY--IHRDLAARNILVESEDL--VKISDFGLAKVLP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 307 Q-RIYQYIQSR-----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHT-GEP 350
Cdd:cd05038   161 EdKEYYYVKEPgespiFWYAPECLRESRFSSASDVWSFGVTLYELFTyGDP 211
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
144-371 1.47e-13

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 72.40  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 144 EKWMDRYEIDSL-IGKGSFGQVVKAY--DRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEM-KYYIVHLKRHf 219
Cdd:cd07868    12 ERVEDLFEYEGCkVGRGTYGHVYKAKrkDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLqKVFLSHADRK- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 mfrnhLCLVFEMLSYNLYDLLR-----NTNFRGVSL--NLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCN--PK 290
Cdd:cd07868    91 -----VWLLFDYAEHDLWHIIKfhrasKANKKPVQLprGMVKSLLYQILDGIHYLHAN--WVLHRDLKPANILVMGegPE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 291 RSAIKIVD------FGSSCQLGQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLF---------SG 354
Cdd:cd07868   164 RGRVKIADmgfarlFNSPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFhcrqediktSN 243
                         250
                  ....*....|....*..
gi 1113820495 355 ANEVDQMNKIVEVLGIP 371
Cdd:cd07868   244 PYHHDQLDRIFNVMGFP 260
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
155-365 1.62e-13

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 72.25  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEV-----RLLELMNKHD--TEMKYYIVHLKRHFM---FRNH 224
Cdd:cd05590     2 VLGKGSFGKVMLARLKESGRLYAVKVLK-KDVILQDDDVECtmtekRILSLARNHPflTQLYCCFQTPDRLFFvmeFVNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYNLYDLLRntnfrgvslnlTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQ 304
Cdd:cd05590    81 GDLMFHIQKSRRFDEAR-----------ARFYAAEITSALMFLH--DKGIIYRDLKLDNVLL--DHEGHCKLADFGM-CK 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 305 LGQR----IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd05590   145 EGIFngktTSTFCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAIL 209
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
155-357 2.19e-13

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: 71.93  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK--------AFLNQAQIevrlLELMNKHdtemkyYIVHLKRHFMFRNHLC 226
Cdd:cd05632     9 VLGKGGFGEVCACQVRATGKMYACKRLEKKRikkrkgesMALNEKQI----LEKVNSQ------FVVNLAYAYETKDALC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEM-----LSYNLYdllrNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGS 301
Cdd:cd05632    79 LVLTImnggdLKFHIY----NMGNPGFEEERALFYAAEILCGLEDLH--RENTVYRDLKPENILLDD--YGHIRISDLGL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 302 SCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANE 357
Cdd:cd05632   151 AVKIpeGESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKE 208
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
155-345 2.41e-13

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 71.20  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAydRVEQEWVAIKI--IKNKKAFLNqaqiEVRLLELMN-KHDTEMKYYIVhLKRHFMFRNHLCLVFEM 231
Cdd:cd14053     2 IKARGRFGAVWKA--QYLNRLVAVKIfpLQEKQSWLT----EREIYSLPGmKHENILQFIGA-EKHGESLEAEYWLITEF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSY-NLYDLLRNtnfRGVSLNLTRKFAQQMCTALLFLAT--------PELSIIHCDLKPENILLCNPKRSAikIVDFGSS 302
Cdd:cd14053    75 HERgSLCDYLKG---NVISWNELCKIAESMARGLAYLHEdipatnggHKPSIAHRDFKSKNVLLKSDLTAC--IADFGLA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 303 C----------QLGQriyqyIQSRFYRSPEVLLG---MPYD--LAIDMWSLGCILVEM 345
Cdd:cd14053   150 LkfepgkscgdTHGQ-----VGTRRYMAPEVLEGainFTRDafLRIDMYAMGLVLWEL 202
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
148-364 2.59e-13

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 70.80  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkkAFLNQAQIEVRL-LELMNK-HDTEMkyyiVHLKRHFMFRNHL 225
Cdd:cd14191     2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFK---AYSAKEKENIRQeISIMNClHHPKL----VQCVDAFEEKANI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRNTNFRGVSLNLTrKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQ 304
Cdd:cd14191    75 VMVLEMVSGgELFERIIDEDFELTERECI-KYMRQISEGVEYIH--KQGIVHLDLKPENIMCVNKTGTKIKLIDFGLARR 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 305 L--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKI 364
Cdd:cd14191   152 LenAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANV 213
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
149-349 2.61e-13

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: 71.17  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAfLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMF--RNH 224
Cdd:cd13986     1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILchSKED-VKEAMREIENYRLFN-HP-----NILRLLDSQIVkeAGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY----NLYDLLRNTNFRGVSLNLTRKFA--QQMCTALLFLATPEL-SIIHCDLKPENILLcNPKRSAIkIV 297
Cdd:cd13986    74 KKEVYLLLPYykrgSLQDEIERRLVKGTFFPEDRILHifLGICRGLKAMHEPELvPYAHRDIKPGNVLL-SEDDEPI-LM 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 298 DFGSSCQL-----GQRIYQYIQ-------SRFYRSPE---VLLGMPYDLAIDMWSLGCILVEMHTGE 349
Cdd:cd13986   152 DLGSMNPArieieGRREALALQdwaaehcTMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGE 218
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
155-365 2.75e-13

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 71.50  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIK------IIKNKKafLNQAQIEVRLLELMNkHDtemkyYIVHLKRHFMFRNHLCLV 228
Cdd:cd05574     8 LLGKGDVGRVYLVRLKGTGKLFAMKvldkeeMIKRNK--VKRVLTEREILATLD-HP-----FLPTLYASFQTSTHLCFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEmlsY----NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnpKRSA-IKIVDFGSSC 303
Cdd:cd05574    80 MD---YcpggELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHL--LGFVYRDLKPENILL---HESGhIMLTDFDLSK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QLG----QRIYQYIQSRF----------------------------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPL 351
Cdd:cd05574   152 QSSvtppPVRKSLRKGSRrssvksieketfvaepsarsnsfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTP 231
                         250
                  ....*....|....
gi 1113820495 352 FSGANEVDQMNKIV 365
Cdd:cd05574   232 FKGSNRDETFSNIL 245
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
142-366 2.93e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 71.25  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 142 NGEKW---MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEmkyYIVHLKRH 218
Cdd:cd06618     6 DGKKYkadLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCP---YIVKCYGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLcnPKRSAIKIVD 298
Cdd:cd06618    83 FITDSDVFICMELMSTCLDKLLKRIQ-GPIPEDILGKMTVSIVKALHYLKE-KHGVIHRDVKPSNILL--DESGNVKLCD 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 299 FGSScqlGQRIYQYIQSR-----FYRSPEVLLGMP---YDLAIDMWSLGCILVEMHTGEPLFSGAN-EVDQMNKIVE 366
Cdd:cd06618   159 FGIS---GRLVDSKAKTRsagcaAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRNCKtEFEVLTKILN 232
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
148-367 3.17e-13

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: 70.76  E-value: 3.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI-------EVRLLELMNKHDtemkyyIVHLKRHFM 220
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVsreeierEVSILRQVLHPN------IITLHDVYE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNHLCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLC--NPKRSAIKIV 297
Cdd:cd14196    79 NRTDVVLILELVSGgELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLdkNIPIPHIKLI 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 298 DFGSSCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV 367
Cdd:cd14196   155 DFGLAHEIedGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV 226
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
142-361 3.43e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 73.62  E-value: 3.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  142 NGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQE---WVAIKIIKNKKAFLNQAQIEVRLL-ELMNKHdtemkyyIVHLKR 217
Cdd:PTZ00266     7 DGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEffcWKAISYRGLKEREKSQLVIEVNVMrELKHKN-------IVRYID 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  218 HFMFRNHLCLVFEMLSYNLYDLLRNTN-----FRGVSLNLTRKFAQQMCTALLFLATPE-----LSIIHCDLKPENILLC 287
Cdd:PTZ00266    80 RFLNKANQKLYILMEFCDAGDLSRNIQkcykmFGKIEEHAIVDITRQLLHALAYCHNLKdgpngERVLHRDLKPQNIFLS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  288 N---------------PKRSAIKIVDFGSSCQLG--QRIYQYIQSRFYRSPEVLL--GMPYDLAIDMWSLGCILVEMHTG 348
Cdd:PTZ00266   160 TgirhigkitaqannlNGRPIAKIGDFGLSKNIGieSMAHSCVGTPYYWSPELLLheTKSYDDKSDMWALGCIIYELCSG 239
                          250
                   ....*....|...
gi 1113820495  349 EPLFSGANEVDQM 361
Cdd:PTZ00266   240 KTPFHKANNFSQL 252
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
156-347 3.82e-13

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 70.16  E-value: 3.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQewVAIKIIK---NKKAFlnqaQIEVRLLELMNkHDTemkyyIVHLkrHFMFRNH--LCLVFE 230
Cdd:cd14058     1 VGRGSFGVVCKARWRNQI--VAVKIIEsesEKKAF----EVEVRQLSRVD-HPN-----IIKL--YGACSNQkpVCLVME 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSY-NLYDLLRNTNFRGV-SLNLTRKFAQQMCTALLFL--ATPElSIIHCDLKPENILLCNpKRSAIKIVDFGSSCQLG 306
Cdd:cd14058    67 YAEGgSLYNVLHGKEPKPIyTAAHAMSWALQCAKGVAYLhsMKPK-ALIHRDLKPPNLLLTN-GGTVLKICDFGTACDIS 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1113820495 307 QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd14058   145 THMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVIT 185
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
148-388 3.93e-13

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 70.86  E-value: 3.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQievrllelMNKHDTEMKYY----------IVHLKR 217
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKK--------ENYHKHACREYrihkeldhprIVKLYD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMF-RNHLCLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSA-IK 295
Cdd:cd14041    78 YFSLdTDSFCTVLEYCEGNDLDFYLKQH-KLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGeIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 296 IVDFGSSCQLGQRIYQYIQ----------SRFYRSPE--VLLGMPYDLA--IDMWSLGCILVEMHTGEPLF---SGANEV 358
Cdd:cd14041   157 ITDFGLSKIMDDDSYNSVDgmeltsqgagTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFYQCLYGRKPFghnQSQQDI 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1113820495 359 DQMNKIVEVLGI--PPAHILdqAPKARKFFEK 388
Cdd:cd14041   237 LQENTILKATEVqfPPKPVV--TPEAKAFIRR 266
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
148-388 4.07e-13

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 70.65  E-value: 4.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKkafLNQAQIEVRLLELMNKHDTeMKYYIVHLKRHFMFRNHLCL 227
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLE---LDESKFNQIIMELDILHKA-VSPYIVDFYGAFFIEGAVYM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLR--NTNFRGVSLNLTRKFAQQMCTALLFLATpELSIIHCDLKPENIlLCNPKrSAIKIVDFGSSCQL 305
Cdd:cd06622    77 CMEYMDAGSLDKLYagGVATEGIPEDVLRRITYAVVKGLKFLKE-EHNIIHRDVKPTNV-LVNGN-GQVKLCDFGVSGNL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQY-IQSRFYRSPEVL--LGMP----YDLAIDMWSLGCILVEMHTGE---PLFSGANEVDQMNKIVEvlGIPPAHI 375
Cdd:cd06622   154 VASLAKTnIGCQSYMAPERIksGGPNqnptYTVQSDVWSLGLSILEMALGRypyPPETYANIFAQLSAIVD--GDPPTLP 231
                         250
                  ....*....|...
gi 1113820495 376 LDQAPKARKFFEK 388
Cdd:cd06622   232 SGYSDDAQDFVAK 244
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
156-353 4.43e-13

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 70.47  E-value: 4.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnkkafLNQAQIEVRLLE----LMNKHDTEmkyYIVHLKRHFMFRNHLCLVFEM 231
Cdd:cd06642    12 IGKGSFGEVYKGIDNRTKEVVAIKIID-----LEEAEDEIEDIQqeitVLSQCDSP---YITRYYGSYLKGTKLWIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSY-NLYDLLRNTNFRGVSLnltRKFAQQMCTALLFLATPELsiIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQ--- 307
Cdd:cd06642    84 LGGgSALDLLKPGPLEETYI---ATILREILKGLDYLHSERK--IHRDIKAANVLL--SEQGDVKLADFGVAGQLTDtqi 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 308 RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFS 353
Cdd:cd06642   157 KRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNS 202
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
271-472 4.62e-13

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 70.54  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 271 ELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQLGQRIYQ-YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG- 348
Cdd:cd06615   118 KHKIMHRDVKPSNILVNS--RGEIKLCDFGVSGQLIDSMANsFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGr 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 349 -----------EPLFSGANEVDQMNKIVEvlgiPPAHILDQAPKARKFFEKLpdgtwnlkktkDGKREYKPPgtrKLhni 417
Cdd:cd06615   196 ypipppdakelEAMFGRPVSEGEAKESHR----PVSGHPPDSPRPMAIFELL-----------DYIVNEPPP---KL--- 254
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 418 lgvetggPGGRRAGEsghtvadylkFKDLILRMLDYDPKTRIQPYYALQHSFFKK 472
Cdd:cd06615   255 -------PSGAFSDE----------FQDFVDKCLKKNPKERADLKELTKHPFIKR 292
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
148-365 5.04e-13

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 69.95  E-value: 5.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDS--LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKkaflNQAQIEVRLLEL--MNKHDTEmkyYIVHLKRHFMFRN 223
Cdd:cd14190     2 STFSIHSkeVLGGGKFGKVHTCTEKRTGLKLAAKVINKQ----NSKDKEMVLLEIqvMNQLNHR---NLIQLYEAIETPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTNFRGVSLNlTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKIVDFGSS 302
Cdd:cd14190    75 EIVLFMEYVEGgELFERIVDEDYHLTEVD-AMVFVRQICEGIQFMH--QMRVLHLDLKPENILCVNRTGHQVKIIDFGLA 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 303 CQLGQRiyQYIQSRF----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd14190   152 RRYNPR--EKLKVNFgtpeFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVL 216
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
156-389 5.27e-13

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 70.40  E-value: 5.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMNKHDTEmKYYIVHLKRHFMFRNHLCLVFEMLSYN 235
Cdd:cd06659    29 IGEGSTGVVCIAREKHSGRQVAVKMMDLRK----QQRRELLFNEVVIMRDYQ-HPNVVEMYKSYLVGEELWVLMEYLQGG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 236 -LYDLLRNTNfrgvslnLTRKFAQQMCTALLFLA--TPELSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQLGQRIYQ- 311
Cdd:cd06659   104 aLTDIVSQTR-------LNEEQIATVCEAVLQALayLHSQGVIHRDIKSDSILLTLDGR--VKLSDFGFCAQISKDVPKr 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 312 --YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVlgiPPAHILDQ---APKARKFF 386
Cdd:cd06659   175 ksLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDS---PPPKLKNShkaSPVLRDFL 251

                  ...
gi 1113820495 387 EKL 389
Cdd:cd06659   252 ERM 254
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
145-357 5.29e-13

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 70.43  E-value: 5.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNH 224
Cdd:cd14177     1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSK---RDPSEEIEILMRYGQHPN-----IITLKDVYDDGRY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTNFrgvslnltrkFAQQMCTALLFLATPELSIIHC------DLKPENILLCNPKRSA--IK 295
Cdd:cd14177    73 VYLVTELMKGgELLDRILRQKF----------FSEREASAVLYTITKTVDYLHCqgvvhrDLKPSNILYMDDSANAdsIR 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 296 IVDFGSSCQL----GQRIYQYIQSRFYrSPEVLLGMPYDLAIDMWSLGCILVEMHTG-EPLFSGANE 357
Cdd:cd14177   143 ICDFGFAKQLrgenGLLLTPCYTANFV-APEVLMRQGYDAACDIWSLGVLLYTMLAGyTPFANGPND 208
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
147-372 6.69e-13

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 69.51  E-value: 6.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIiknkkafLNQAQIEVRLLELMNKHDTEMKYYIVH--LKRHFMFRNH 224
Cdd:cd14117     5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKV-------LFKSQIEKEGVEHQLRREIEIQSHLRHpnILRLYNYFHD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY----NLY-DLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd14117    78 RKRIYLILEYaprgELYkELQKHGRF---DEQRTATFMEELADALHYCH--EKKVIHRDIKPENLLM--GYKGELKIADF 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 300 GSSCQLGQ-RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV-LGIPP 372
Cdd:cd14117   151 GWSVHAPSlRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVdLKFPP 225
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
148-367 6.81e-13

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: 69.66  E-value: 6.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIevrllelmNKHDTEMKYYIVHLKRH--------- 218
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRGV--------SREDIEREVSILKEIQHpnvitlhev 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLC--NPKRSAIK 295
Cdd:cd14194    77 YENKTDVILILELVAGgELFDFLAEK--ESLTEEEATEFLKQILNGVYYLHS--LQIAHFDLKPENIMLLdrNVPKPRIK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 296 IVDFGSSCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV 367
Cdd:cd14194   153 IIDFGLAHKIdfGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAV 226
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
151-344 7.87e-13

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: 69.76  E-value: 7.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLiGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIeVRLLELMNKHDTEmkyYIVHLKRHFMfRNHLCLVFE 230
Cdd:cd06621     5 ELSSL-GEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQKQI-LRELEINKSCASP---YIVKYYGAFL-DEQDSSIGI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSY-------NLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSC 303
Cdd:cd06621    79 AMEYceggsldSIYKKVKKKGGR-IGEKVLGKIAESVLKGLSYLH--SRKIIHRDIKPSNILLT--RKGQVKLCDFGVSG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1113820495 304 QLGQRIYQ-YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVE 344
Cdd:cd06621   154 ELVNSLAGtFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLE 195
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
156-350 8.46e-13

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 69.33  E-value: 8.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnkkafLNQAQIEVRLLE----LMNKHDTE--MKYYIVHLKRhfmfrNHLCLVF 229
Cdd:cd06641    12 IGKGSFGEVFKGIDNRTQKVVAIKIID-----LEEAEDEIEDIQqeitVLSQCDSPyvTKYYGSYLKD-----TKLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSY-NLYDLLRNTNFRGVSLnltRKFAQQMCTALLFLATPELsiIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQ- 307
Cdd:cd06641    82 EYLGGgSALDLLEPGPLDETQI---ATILREILKGLDYLHSEKK--IHRDIKAANVLL--SEHGEVKLADFGVAGQLTDt 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 308 --RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd06641   155 qiKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEP 199
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
156-348 8.97e-13

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 69.52  E-value: 8.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIeVRLLELMNKHDTEmkyYIVHLKRHFMFRNHLCLVFEMLSYN 235
Cdd:cd06619     9 LGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQI-MSELEILYKCDSP---YIIGFYGAFFVENRISICTEFMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 236 LYDLlrntnFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQ-YIQ 314
Cdd:cd06619    85 SLDV-----YRKIPEHVLGRIAVAVVKGLTYLWS--LKILHRDVKPSNMLV--NTRGQVKLCDFGVSTQLVNSIAKtYVG 155
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1113820495 315 SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd06619   156 TNAYMAPERISGEQYGIHSDVWSLGISFMELALG 189
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
151-349 1.26e-12

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 68.92  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAYdrveqeW---VAIKIIKNKkaFLNQAQIEVRLLELMN----KHDTemkyyIVHLKRHFMFRN 223
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGR------WhgdVAIKLLNID--YLNEEQLEAFKEEVAAykntRHDN-----LVLFMGACMDPP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEML-SYNLYDLLRN--TNFrgvSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNPKrsaIKIVDFG 300
Cdd:cd14063    70 HLAIVTSLCkGRTLYSLIHErkEKF---DFNKTVQIAQQICQGMGYLHAKG--IIHKDLKSKNIFLENGR---VVITDFG 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 301 SSC-----QLGQRIYQYIQSR---FYRSPEVLLGM----------PYDLAIDMWSLGCILVEMHTGE 349
Cdd:cd14063   142 LFSlsgllQPGRREDTLVIPNgwlCYLAPEIIRALspdldfeeslPFTKASDVYAFGTVWYELLAGR 208
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
151-345 1.36e-12

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 69.07  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLiGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI---EVRLLELMNKHDtemkyyIVHLKRHFMFRNHLCL 227
Cdd:cd14049    10 EIARL-GKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKvlrEVKVLAGLQHPN------IVGYHTAWMEHVQLML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEM--LSYNLYDLLRNTNFRG------------VSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSa 293
Cdd:cd14049    83 YIQMqlCELSLWDWIVERNKRPceeefksapytpVDVDVTTKILQQLLEGVTYIHS--MGIVHRDLKPRNIFLHGSDIH- 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 294 IKIVDFGSSC--QLGQRIYQYIQSR-------------FYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd14049   160 VRIGDFGLACpdILQDGNDSTTMSRlnglthtsgvgtcLYAAPEQLEGSHYDFKSDMYSIGVILLEL 226
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
212-482 1.48e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 70.02  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 212 IVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPkr 291
Cdd:PHA03212  145 IIQLKGTFTYNKFTCLILPRYKTDLYCYLAAK--RNIAICDILAIERSVLRAIQYLH--ENRIIHRDIKAENIFINHP-- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 292 SAIKIVDFGSSCQ----LGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVD-------Q 360
Cdd:PHA03212  219 GDVCLGDFGAACFpvdiNANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFEKDGLDgdcdsdrQ 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 361 MNKIVEVLGIPPAhildqapkarkffeKLP-DGTWNLKKTKDG--KREYKPPGTRKLHNILgvetggpggrragesghtv 437
Cdd:PHA03212  299 IKLIIRRSGTHPN--------------EFPiDAQANLDEIYIGlaKKSSRKPGSRPLWTNL------------------- 345
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1113820495 438 adY---LKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTSN 482
Cdd:PHA03212  346 --YelpIDLEYLICKMLAFDAHHRPSAEALLDFAAFQDIPDPYPNPME 391
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
150-368 1.57e-12

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: 69.30  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEID---SLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkKAFLNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNHLC 226
Cdd:cd14179     6 YELDlkdKPLGEGSFSICRKCLHKKTNQEYAVKIVS--KRMEANTQREIAALKLCEGHPN-----IVKLHEVYHDQLHTF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNP-KRSAIKIVDFGSScQ 304
Cdd:cd14179    79 LVMELLKGgELLERIKKK--QHFSETEASHIMRKLVSAVSHMH--DVGVVHRDLKPENLLFTDEsDNSEIKIIDFGFA-R 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 305 LGQRIYQYIQSR----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVL 368
Cdd:cd14179   154 LKPPDNQPLKTPcftlHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEIM 221
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
145-372 1.74e-12

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: 68.18  E-value: 1.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KWMDryeiDSLIGKGSFGQVVKAYDRVEQEWVAIKiiknkkaflnqaQIEvrllelMNKHDTE------------MKYYI 212
Cdd:cd06629     2 KWVK----GELIGKGTYGRVYLAMNATTGEMLAVK------------QVE------LPKTSSDradsrqktvvdaLKSEI 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 213 VHLKRhfmfRNHL----CLVFE--MLSYNLY----------DLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPelSIIH 276
Cdd:cd06629    60 DTLKD----LDHPnivqYLGFEetEDYFSIFleyvpggsigSCLRK--YGKFEEDLVRFFTRQILDGLAYLHSK--GILH 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 277 CDLKPENILLcnPKRSAIKIVDFGSSCQlGQRIYQYIQ------SRFYRSPEVL--LGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd06629   132 RDLKADNILV--DLEGICKISDFGISKK-SDDIYGNNGatsmqgSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAG 208
                         250       260
                  ....*....|....*....|....
gi 1113820495 349 EPLFSGANEVDQMNKIVEVLGIPP 372
Cdd:cd06629   209 RRPWSDDEAIAAMFKLGNKRSAPP 232
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
154-365 1.83e-12

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 69.25  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 154 SLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQI-----EVRLLELMN--KHDtemkyYIVHLKRHFMFRNHLC 226
Cdd:cd05589     5 AVLGRGHFGKVLLAEYKPTGELFAIKALK-KGDIIARDEVeslmcEKRIFETVNsaRHP-----FLVNLFACFQTPEHVC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNlyDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQ-- 304
Cdd:cd05589    79 FVMEYAAGG--DLMMHIHEDVFSEPRAVFYAACVVLGLQFLH--EHKIVYRDLKLDNLLL--DTEGYVKIADFGL-CKeg 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 305 --LGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd05589   152 mgFGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIV 214
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
149-365 1.93e-12

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 67.85  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQ---AQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNhl 225
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRErkaAEQEAKLLSKL-KHPN-----IVSYKESFEGED-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY----NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFG- 300
Cdd:cd08223    73 GFLYIVMGFceggDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMH--ERNILHRDLKTQNIFLT--KSNIIKVGDLGi 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 -----SSCQLGQRIyqyIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANevdqMNKIV 365
Cdd:cd08223   149 arvleSSSDMATTL---IGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKD----MNSLV 211
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
155-345 1.96e-12

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 68.37  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKII-----KNKKAFlNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHLCLVF 229
Cdd:cd05608     8 VLGKGGFGEVSACQMRATGKLYACKKLnkkrlKKRKGY-EGAMVEKRILAKVHSR------FIVSLAYAFQTKTDLCLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EM-----LSYNLYDLlrNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQ 304
Cdd:cd05608    81 TImnggdLRYHIYNV--DEENPGFQEPRACFYTAQIISGLEHLH--QRRIIYRDLKPENVLLDD--DGNVRISDLGLAVE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1113820495 305 L--GQ-RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd05608   155 LkdGQtKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEM 198
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
148-471 2.13e-12

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 68.52  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEI-DSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNK------KAF-----LNQAQIEVRLLELMNKHDTEMKYYIVHL 215
Cdd:cd14174     1 DLYRLtDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNaghsrsRVFrevetLYQCQGNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 216 K-------RHFMFRNHLclvfemlsynlydllrntNFRGVSlnltrKFAQQMCTALLFLATPelSIIHCDLKPENILLCN 288
Cdd:cd14174    81 KlrggsilAHIQKRKHF------------------NEREAS-----RVVRDIASALDFLHTK--GIAHRDLKPENILCES 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 289 P-KRSAIKIVDF--GSSCQLGQ--------RIYQYIQSRFYRSPEVL-----LGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14174   136 PdKVSPVKICDFdlGSGVKLNSactpittpELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPF 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 353 SGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFeklPDGTWNlkktkdgkreykppgtrklhnilgvetggpggrrage 432
Cdd:cd14174   216 VGHCGTDCGWDRGEVCRVCQNKLFESIQEGKYEF---PDKDWS------------------------------------- 255
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1113820495 433 sgHTVADYlkfKDLILRMLDYDPKTRIQPYYALQHSFFK 471
Cdd:cd14174   256 --HISSEA---KDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
156-366 2.20e-12

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: 68.91  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK-NKKAFLNQAQ---IEVRLLELMnKHDTEMKYYIVHLKRHFMFrnhlcLVFEM 231
Cdd:cd06633    29 IGHGSFGAVYFATNSHTNEVVAIKKMSySGKQTNEKWQdiiKEVKFLQQL-KHPNTIEYKGCYLKDHTAW-----LVMEY 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYNLYDLLR--NTNFRGVSLNLTRKFAQQmctALLFLATPELsiIHCDLKPENILLCNPKRsaIKIVDFGSScQLGQRI 309
Cdd:cd06633   103 CLGSASDLLEvhKKPLQEVEIAAITHGALQ---GLAYLHSHNM--IHRDIKAGNILLTEPGQ--VKLADFGSA-SIASPA 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 310 YQYIQSRFYRSPEVLLGM---PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd06633   175 NSFVGTPYWMAPEVILAMdegQYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQ 234
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
156-372 2.45e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 67.72  E-value: 2.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDR---VEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDTEMKYYIvhlKRHFMFRNHLCLVFE-- 230
Cdd:cd14033     9 IGRGSFKTVYRGLDTettVEVAWCELQTRKLSKGERQRFSEEVEMLKGL-QHPNIVRFYD---SWKSTVRGHKCIILVte 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 -MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSaIKIVDFG-SSCQLGQR 308
Cdd:cd14033    85 lMTSGTLKTYLKR--FREMKLKLLQRWSRQILKGLHFLHSRCPPILHRDLKCDNIFITGPTGS-VKIGDLGlATLKRASF 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 309 IYQYIQSRFYRSPEvLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVeVLGIPP 372
Cdd:cd14033   162 AKSVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKV-TSGIKP 223
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
150-348 2.64e-12

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: 67.53  E-value: 2.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA---------FLNQAQIE--------VRLLELMnkhDTEMKYYI 212
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAkkdsyvtknLRREGRIQqmirhpniTQLLDIL---ETENSYYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 213 VHlkrhfmfrnHLCLVFEMLSyNLYDLLRntnfrgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRS 292
Cdd:cd14070    81 VM---------ELCPGGNLMH-RIYDKKR------LEEREARRYIRQLVSAVEHLH--RAGVVHRDLKIENLLL--DEND 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 293 AIKIVDFG-SSCQ----LGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd14070   141 NIKLIDFGlSNCAgilgYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTG 201
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
251-372 2.79e-12

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: 67.84  E-value: 2.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 251 NLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSaIKIVDFGSSCQLGQRIY-------QYIQSRFYRSPEV 323
Cdd:cd06630   103 NVIINYTLQILRGLAYLH--DNQIIHRDLKGANLLVDSTGQR-LRIADFGAAARLASKGTgagefqgQLLGTIAFMAPEV 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 324 LLGMPYDLAIDMWSLGCILVEMHTGEPLFsGANEVDQ----MNKIVEVLGIPP 372
Cdd:cd06630   180 LRGEQYGRSCDVWSVGCVIIEMATAKPPW-NAEKISNhlalIFKIASATTPPP 231
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
141-366 3.33e-12

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 68.47  E-value: 3.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 141 KNGEKWMDRYEIDSLiGKGSFGQVVKA-YDRVEQEWVAIKIIKNKKaFLNQAQI-----EVRLLELMNKHdtemkyYIVH 214
Cdd:PTZ00426   24 KNKMKYEDFNFIRTL-GTGSFGRVILAtYKNEDFPPVAIKRFEKSK-IIKQKQVdhvfsERKILNYINHP------FCVN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 215 LKRHFMFRNHLCLVFE-MLSYNLYDLLR-NTNFRGvslNLTRKFAQQMctALLFLATPELSIIHCDLKPENILLcnPKRS 292
Cdd:PTZ00426   96 LYGSFKDESYLYLVLEfVIGGEFFTFLRrNKRFPN---DVGCFYAAQI--VLIFEYLQSLNIVYRDLKPENLLL--DKDG 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 293 AIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:PTZ00426  169 FIKMTDFGFAKVVDTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILE 242
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
156-389 3.44e-12

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 67.29  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHLCLVFEMLSYN 235
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQ------YITLHDTYESPTSYILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 236 -LYDLLRNTNF---RGVSLnltrkFAQQMCTALLFLATpeLSIIHCDLKPENIL--LCNPKrSAIKIVDFGSSCQLG--Q 307
Cdd:cd14115    75 rLLDYLMNHDElmeEKVAF-----YIRDIMEALQYLHN--CRVAHLDIKPENLLidLRIPV-PRVKLIDLEDAVQISghR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 308 RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG-EPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFF 386
Cdd:cd14115   147 HVHHLLGNPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGvSPFLDESKEETCINVCRVDFSFPDEYFGDVSQAARDFI 226

                  ...
gi 1113820495 387 EKL 389
Cdd:cd14115   227 NVI 229
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
150-342 3.67e-12

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: 67.29  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnqaqieVRLLELMNKHDTEMKyyIVHLKRHfmfrNHLCLVF 229
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQK---------IKSLDMEEKIRREIQ--ILKLFRH----PHIIRLY 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLS----------Y----NLYDLLRNtnfRG-VSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAI 294
Cdd:cd14079    69 EVIEtptdifmvmeYvsggELFDYIVQ---KGrLSEDEARRFFQQIISGVEYCH--RHMVVHRDLKPENLLL--DSNMNV 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 295 KIVDFG------------SSCqlgqriyqyiQSRFYRSPEVLLGMPYdlA---IDMWSLGCIL 342
Cdd:cd14079   142 KIADFGlsnimrdgeflkTSC----------GSPNYAAPEVISGKLY--AgpeVDVWSCGVIL 192
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
159-349 3.84e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 67.19  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 159 GSFGQVVKAYDRVEQEWVAIKIIKNKkaflNQAQIEVRLLELM--NKHDTEMkYYIVHLKRHfmfrnHLcLVfemLSY-- 234
Cdd:PHA03390   27 GKFGKVSVLKHKPTQKLFVQKIIKAK----NFNAIEPMVHQLMkdNPNFIKL-YYSVTTLKG-----HV-LI---MDYik 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 --NLYDLLRNTNFrgVSLNLTRKFAQQMCTAL--LFLATpelsIIHCDLKPENILlCNPKRSAIKIVDFG-------SSC 303
Cdd:PHA03390   93 dgDLFDLLKKEGK--LSEAEVKKIIRQLVEALndLHKHN----IIHNDIKLENVL-YDRAKDRIYLCDYGlckiigtPSC 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 304 QLGQRIYqyiqsrFyrSPEVLLGMPYDLAIDMWSLGCILVEMHTGE 349
Cdd:PHA03390  166 YDGTLDY------F--SPEKIKGHNYDVSFDWWAVGVLTYELLTGK 203
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
155-373 4.38e-12

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 67.25  E-value: 4.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQewVAIKIIkNKKAFLNQAQIEVRLLELMNKHDTEMKYY---------IVHLKRHFMFR--- 222
Cdd:cd14000     1 LLGDGGFGSVYRASYKGEP--VAVKIF-NKHTSSNFANVPADTMLRHLRATDAMKNFrllrqeltvLSHLHHPSIVYllg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 ---NHLCLVFEMLSYNLYD-LLRNTNFRGVSLN--LTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCN-PKRSAI- 294
Cdd:cd14000    78 igiHPLMLVLELAPLGSLDhLLQQDSRSFASLGrtLQQRIALQVADGLRYLHSA--MIIYRDLKSHNVLVWTlYPNSAIi 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 295 -KIVDFG---SSCQLGQRIYQYIQSrfYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEvlG 369
Cdd:cd14000   156 iKIADYGisrQCCRMGAKGSEGTPG--FRAPEIARGnVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG--G 231

                  ....
gi 1113820495 370 IPPA 373
Cdd:cd14000   232 LRPP 235
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
156-356 5.24e-12

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: 66.51  E-value: 5.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKK--AFLN-QAQI--EVRLLELMN-KHdtemkyyIVHLkrHFMFRNH----L 225
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKlrRIPNgEANVkrEIQILRRLNhRN-------VIKL--VDVLYNEekqkL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQL 305
Cdd:cd14119    72 YMVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHS--QGIIHKDIKPGNLLLTTDGT--LKISDFGVAEAL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 306 -----GQRIYQYIQSRFYRSPEVLLGMPY--DLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd14119   148 dlfaeDDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMTTGKYPFEGDN 205
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
156-360 6.31e-12

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: 66.58  E-value: 6.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNK----KAFLNQAQIEVRLlelmNKHDTEMKYYIVhlkrhfMFRNHLCLVFEM 231
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPstklKDFLREYNISLEL----SVHPHIIKTYDV------AFETEDYYVFAQ 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 lSYNLY-DLLRN-TNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRI 309
Cdd:cd13987    71 -EYAPYgDLFSIiPPQVGLPEERVKRCAAQLASALDFMHS--KNLVHRDIKPENVLLFDKDCRRVKLCDFGLTRRVGSTV 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 310 YQYIQSRFYRSPEVLLGMPYDL-----AIDMWSLGCILVEMHTGEPLFSGANEVDQ 360
Cdd:cd13987   148 KRVSGTIPYTAPEVCEAKKNEGfvvdpSIDVWAFGVLLFCCLTGNFPWEKADSDDQ 203
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
150-354 6.41e-12

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: 66.66  E-value: 6.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRLLE--LMNKHDTEmkyYIVHLKRHFMFRNHLCL 227
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKI-NKQNLILRNQIQQVFVErdILTFAENP---FVVSMYCSFETKRHLCM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSY-NLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNpkRSAIKIVDFGSS---- 302
Cdd:cd05609    78 VMEYVEGgDCATLLKNIG--PLPVDMARMYFAETVLALEYLHS--YGIVHRDLKPDNLLITS--MGHIKLTDFGLSkigl 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 303 CQLGQRIYQYIQSR----F----------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSG 354
Cdd:cd05609   152 MSLTTNLYEGHIEKdtreFldkqvcgtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG 217
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
150-352 9.49e-12

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 66.03  E-value: 9.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF-------LNQAQIEVRLLELMNKHDTEMKyyIVHLKRHFMFR 222
Cdd:cd14101     2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQqwsklpgVNPVPNEVALLQSVGGGPGHRG--VIRLLDWFEIP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFE--MLSYNLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcNPKRSAIKIVDFG 300
Cdd:cd14101    80 EGFLLVLErpQHCQDLFDYI--TERGALDESLARRFFKQVVEAVQHCHSK--GVVHRDIKDENILV-DLRTGDIKLIDFG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 301 SSCQLGQRIY-QYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14101   155 SGATLKDSMYtDFDGTRVYSPPEWILYHQYHaLPATVWSLGILLYDMVCGDIPF 208
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
155-379 9.85e-12

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


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 66.26  E-value: 9.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIK------NKKAFLNQAQIEVRLLELMnKHDTEMKYYIVhlkrhfmFRNH---- 224
Cdd:cd06651    14 LLGQGAFGRVYLCYDVDTGRELAAKQVQfdpespETSKEVSALECEIQLLKNL-QHERIVQYYGC-------LRDRaekt 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFE-MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILlcNPKRSAIKIVDFGSS- 302
Cdd:cd06651    86 LTIFMEyMPGGSVKDQLKA--YGALTESVTRKYTRQILEGMSYLHSN--MIVHRDIKGANIL--RDSAGNVKLGDFGASk 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 303 -----CQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSganEVDQMNKIVEVLGIP-----P 372
Cdd:cd06651   160 rlqtiCMSGTGIRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQPtnpqlP 236

                  ....*..
gi 1113820495 373 AHILDQA 379
Cdd:cd06651   237 SHISEHA 243
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
156-353 1.08e-11

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: 65.93  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIK---------------IIKNKKaFLNQAqievrllelmnKHDTEMKYYIVHLKRHFM 220
Cdd:cd06607     9 IGHGSFGAVYYARNKRTSEVVAIKkmsysgkqstekwqdIIKEVK-FLRQL-----------RHPNTIEYKGCYLREHTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FrnhlcLVFEMLSYNLYDLLrNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPkrSAIKIVDFG 300
Cdd:cd06607    77 W-----LVMEYCLGSASDIV-EVHKKPLQEVEIAAICHGALQGLAYLHS--HNRIHRDVKAGNILLTEP--GTVKLADFG 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 301 SScQLGQRIYQYIQSRFYRSPEVLLGM---PYDLAIDMWSLGCILVEMhtGE---PLFS 353
Cdd:cd06607   147 SA-SLVCPANSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIEL--AErkpPLFN 202
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
148-352 1.15e-11

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: 65.78  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDS-LIGKGSFGQVVKAYDRVEQEWVAIKII-KNKKAflnQAQIEVRLLELMNKHdtemkyyIVHLKRHF--MFRN 223
Cdd:cd14172     3 DDYKLSKqVLGLGVNGKVLECFHRRTGQKCALKLLyDSPKA---RREVEHHWRASGGPH-------IVHILDVYenMHHG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQM---CTALLFLATpeLSIIHCDLKPENILLCNPKRSAI-KIVDF 299
Cdd:cd14172    73 KRCLLIIMECMEGGELFSRIQERGDQAFTEREASEIMrdiGTAIQYLHS--MNIAHRDVKPENLLYTSKEKDAVlKLTDF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 300 GSSCQLGQR--IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14172   151 GFAKETTVQnaLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPF 205
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
148-471 1.15e-11

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: 66.41  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK---------------NKKAFLNQAQIEVRLLELMNKHDTEMKYYI 212
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDvakftsspglstedlKREASICHMLKHPHIVELLETYSSDGMLYM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 213 VHlkrHFMFRNHLClvFEMLSynlydllRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNPKRS 292
Cdd:cd14094    83 VF---EFMDGADLC--FEIVK-------RADAGFVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 293 A-IKIVDFGSSCQLGQrIYQYIQSRF----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEvdqmnkivev 367
Cdd:cd14094   149 ApVKLGGFGVAIQLGE-SGLVAGGRVgtphFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE---------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 368 lgippahildqapkarKFFEKLPDGTWNLKktkdgkreykppgtrklhnilgvetgGPGGRRAGESGhtvadylkfKDLI 447
Cdd:cd14094   218 ----------------RLFEGIIKGKYKMN--------------------------PRQWSHISESA---------KDLV 246
                         330       340
                  ....*....|....*....|....
gi 1113820495 448 LRMLDYDPKTRIQPYYALQHSFFK 471
Cdd:cd14094   247 RRMLMLDPAERITVYEALNHPWIK 270
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
148-366 1.21e-11

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: 66.60  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQV----VKAYDRVeqewVAIKIIkNKKAFLNQAQI----EVRllELMNKHDtemKYYIVHLkrHF 219
Cdd:cd05597     1 DDFEILKVIGRGAFGEVavvkLKSTEKV----YAMKIL-NKWEMLKRAETacfrEER--DVLVNGD---RRWITKL--HY 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSYNLYDLLRNTNFRGVSL--NLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIV 297
Cdd:cd05597    69 AFQDENYLYLVMDYYCGGDLLTLLSKFEDRLpeEMARFYLAEMVLAIDSIHQ--LGYVHRDIKPDNVLL--DRNGHIRLA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 298 DFGSSCQLGQRiyQYIQSRF------YRSPEVLLGMP-----YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05597   145 DFGSCLKLRED--GTVQSSVavgtpdYISPEILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMN 222
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
148-354 1.32e-11

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 66.20  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEI-DSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA-----------FLNQAQIEVRLLELMNKHDTEMKYYivhl 215
Cdd:cd14173     1 DVYQLqEEVLGEGAYARVQTCINLITNKEYAVKIIEKRPGhsrsrvfreveMLYQCQGHRNVLELIEFFEEEDKFY---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 216 krhfmfrnhlcLVFEMLSYN--LYDLLRNTNFRGVSLNLTrkfAQQMCTALLFLATPelSIIHCDLKPENILLCNPKR-S 292
Cdd:cd14173    77 -----------LVFEKMRGGsiLSHIHRRRHFNELEASVV---VQDIASALDFLHNK--GIAHRDLKPENILCEHPNQvS 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 293 AIKIVDF--GSSCQLGQ--------RIYQYIQSRFYRSPEVLLGMP-----YDLAIDMWSLGCILVEMHTGEPLFSG 354
Cdd:cd14173   141 PVKICDFdlGSGIKLNSdcspistpELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVG 217
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
156-302 1.40e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 65.55  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNK--HDtemkyYIVHLKRHFMFRNHLCLVFE-ML 232
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERarHS-----YVLPLLGVCVERRSLGLVMEyME 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SYNLYDLLRnTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRsaIKIVDFGSS 302
Cdd:cd13978    76 NGSLKSLLE-REIQDVPWSLRFRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHFH--VKISDFGLS 142
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
149-344 1.42e-11

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: 65.91  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWV-AIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCL 227
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYAGAKDRLRRLEEVSILRELTLDGHDNIVQLIDSWEYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRNTNFRGVSLNLTR--KFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQL 305
Cdd:cd14052    81 QTELCENGSLDVFLSELGLLGRLDEFRvwKILVELSLGLRFIH--DHHFVHLDLKPANVLIT--FEGTLKIGDFGMATVW 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1113820495 306 G-QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVE 344
Cdd:cd14052   157 PlIRGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLE 196
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
148-476 1.48e-11

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 66.23  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII--KNKKAFLNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHL 225
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIhlEIKPAIRNQIIRELQVLHECNSP------YIVGFYGAFYSDGEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLATPElSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQL 305
Cdd:cd06650    79 SICMEHMDGGSLDQVLKKAGR-IPEQILGKVSIAVIKGLTYLREKH-KIMHRDVKPSNILVNS--RGEIKLCDFGVSGQL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQ-YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE-PLFSGANEVDQMNKIVEVLGIPPAHILDQAPKAR 383
Cdd:cd06650   155 IDSMANsFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRyPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGR 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 384 KFFEKLPDGtwnlkktkdgkreyKPPgtRKLHNILGVETGGPGGRRAgesghTVADYLKFKDLILRMLDYDPKTRIQPYY 463
Cdd:cd06650   235 PLSSYGMDS--------------RPP--MAIFELLDYIVNEPPPKLP-----SGVFSLEFQDFVNKCLIKNPAERADLKQ 293
                         330
                  ....*....|...
gi 1113820495 464 ALQHSFFKKTADE 476
Cdd:cd06650   294 LMVHAFIKRSDAE 306
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
148-367 1.59e-11

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: 65.41  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKafLNQAQIEVRLLELMNKHDT--EMKY-YIVHLKRHFMFRNH 224
Cdd:cd14195     5 DHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRR--LSSSRRGVSREEIEREVNIlrEIQHpNIITLHDIFENKTD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLC--NPKRSAIKIVDFGS 301
Cdd:cd14195    83 VVLILELVSGgELFDFLAEK--ESLTEEEATQFLKQILDGVHYLHSKR--IAHFDLKPENIMLLdkNVPNPRIKLIDFGI 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 302 SCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEV 367
Cdd:cd14195   159 AHKIeaGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAV 226
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
150-383 2.05e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 66.20  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF----LNQAQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHddedIDWVQTEKHVFEQASSNP-----FLVGLHSCFQTTSRL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLsyNLYDLLRNTNF-RGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQ 304
Cdd:cd05617    92 FLVIEYV--NGGDLMFHMQRqRKLPEEHARFYAAEICIALNFLH--ERGIIYRDLKLDNVLL--DADGHIKLTDYGM-CK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 LGQR----IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMN--------------KIVE 366
Cdd:cd05617   165 EGLGpgdtTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNtedylfqvilekpiRIPR 244
                         250       260
                  ....*....|....*....|.
gi 1113820495 367 VLGIPPAHI----LDQAPKAR 383
Cdd:cd05617   245 FLSVKASHVlkgfLNKDPKER 265
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
141-369 2.16e-11

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 65.81  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 141 KNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflNQAQIEVRLLELMNKHDTemkyyIVHLKRHFM 220
Cdd:cd14176    12 RNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEILLRYGQHPN-----IITLKDVYD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNHLCLVFEMLSY-NLYDLLRNTNFrgvslnltrkFAQQMCTALLFLATPELS------IIHCDLKPENILLC----NP 289
Cdd:cd14176    84 DGKYVYVVTELMKGgELLDKILRQKF----------FSEREASAVLFTITKTVEylhaqgVVHRDLKPSNILYVdesgNP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 290 KrsAIKIVDFGSSCQL----GQRIYQYIQSRFYrSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEvDQMNKIV 365
Cdd:cd14176   154 E--SIRICDFGFAKQLraenGLLMTPCYTANFV-APEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPD-DTPEEIL 229

                  ....
gi 1113820495 366 EVLG 369
Cdd:cd14176   230 ARIG 233
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
156-372 2.28e-11

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: 65.44  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMNKHDTEMKYyIVHLKRHFMFRNHLCLVFEMLSYN 235
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRK----QQRRELLFNEVVIMRDYHHEN-VVDMYNSYLVGDELWVVMEFLEGG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 236 -LYDLLRNTnfrgvslnltRKFAQQMCT-------ALLFLATPelSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQLGQ 307
Cdd:cd06658   105 aLTDIVTHT----------RMNEEQIATvclsvlrALSYLHNQ--GVIHRDIKSDSILLTSDGR--IKLSDFGFCAQVSK 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 308 RIYQ---YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLgiPP 372
Cdd:cd06658   171 EVPKrksLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNL--PP 236
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
156-350 3.02e-11

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: 64.65  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLlelmnKHDTEMKYY-------IVHLkrhFMFRNHLCLV 228
Cdd:cd13995    12 IPRGAFGKVYLAQDTKTKKRMACKLIPVEQFKPSDVEIQACF-----RHENIAELYgallweeTVHL---FMEAGEGGSV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSynlydllrntnfrgvSLNLTRKF-----AQQMCTALLFLATPElsIIHCDLKPENILLCNPKrsAIkIVDFGSSC 303
Cdd:cd13995    84 LEKLE---------------SCGPMREFeiiwvTKHVLKGLDFLHSKN--IIHHDIKPSNIVFMSTK--AV-LVDFGLSV 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QLGQRIYQYIQSR---FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEP 350
Cdd:cd13995   144 QMTEDVYVPKDLRgteIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSP 193
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
148-360 3.18e-11

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 65.08  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQievrllelMNKHDTEMKYYIVH----------LKR 217
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKK--------ENYHKHACREYRIHkeldhprivkLYD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 HFMF-RNHLCLVFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSA-IK 295
Cdd:cd14040    78 YFSLdTDTFCTVLEYCEGNDLDFYLKQH-KLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGeIK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 296 IVDFGSSCQLGQRIY---------QYIQSRFYRSPE--VLLGMPYDLA--IDMWSLGCILVEMHTGEPLFsGANEVDQ 360
Cdd:cd14040   157 ITDFGLSKIMDDDSYgvdgmdltsQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPF-GHNQSQQ 233
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
150-362 3.60e-11

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: 64.28  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIK---IIKNKKAFLNQAQI-EVRLLELMNkHDTEMKYYivhlkRHFMFRNHL 225
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKkvqIFEMMDAKARQDCVkEIDLLKQLN-HPNVIKYL-----DSFIEDNEL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLR--NTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCnpKRSAIKIVDFGss 302
Cdd:cd08228    78 NIVLELADAgDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRR--VMHRDIKPANVFIT--ATGVVKLGDLG-- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 303 cqLGQ-------RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGanevDQMN 362
Cdd:cd08228   152 --LGRffsskttAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG----DKMN 212
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
155-354 4.41e-11

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 63.95  E-value: 4.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQewVAIKIIK-----NKKAFLNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNHLCLVF 229
Cdd:cd14061     1 VIGVGGFGKVYRGIWRGEE--VAVKAARqdpdeDISVTLENVRQEARLFWML-RHPN-----IIALRGVCLQPPNLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMlsYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLA-TPELSIIHCDLKPENILLCNP------KRSAIKIVDFGss 302
Cdd:cd14061    73 EY--ARGGALNRVLAGRKIPPHVLVDWAIQIARGMNYLHnEAPVPIIHRDLKSSNILILEAienedlENKTLKITDFG-- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 303 cqLGQRIYQYIQ-----SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSG 354
Cdd:cd14061   149 --LAREWHKTTRmsaagTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
156-366 4.51e-11

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: 64.69  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQI--EVRLLELMnKHDTEMKYYIVHLKRHFMFrnhlcLVFEM 231
Cdd:cd06635    33 IGHGSFGAVYFARDVRTSEVVAIKKMSysGKQSNEKWQDIikEVKFLQRI-KHPNSIEYKGCYLREHTAW-----LVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYNLYDLLR--NTNFRGVSLNLTRKFAQQmctALLFLATPELsiIHCDLKPENILLCNPKRsaIKIVDFGSScQLGQRI 309
Cdd:cd06635   107 CLGSASDLLEvhKKPLQEIEIAAITHGALQ---GLAYLHSHNM--IHRDIKAGNILLTEPGQ--VKLADFGSA-SIASPA 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 310 YQYIQSRFYRSPEVLLGM---PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd06635   179 NSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQ 238
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
149-352 4.63e-11

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: 63.97  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSL-----IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAflNQAQI---EVRLLELMnKHDTEMKYYIVHLKrhfm 220
Cdd:cd06624     4 EYEYDESgervvLGKGTFGVVYAARDLSTQVRIAIKEIPERDS--REVQPlheEIALHSRL-SHKNIVQYLGSVSE---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 frNHLCLVF--EMLSYNLYDLLRNT------NfrgvsLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcNPKRS 292
Cdd:cd06624    77 --DGFFKIFmeQVPGGSLSALLRSKwgplkdN-----ENTIGYYTKQILEGLKYLH--DNKIVHRDIKGDNVLV-NTYSG 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 293 AIKIVDFGSSCQLGqRIYQYIQSrF-----YRSPEVLLGMP--YDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd06624   147 VVKISDFGTSKRLA-GINPCTET-FtgtlqYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPF 211
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
149-373 4.72e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 65.25  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQV--VKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMNkHDTemkyyIVHLKRHFMFRNHLC 226
Cdd:PHA03207   93 QYNILSSLTPGSEGEVfvCTKHGDEQRKKVIVKAVTGGK----TPGREIDILKTIS-HRA-----IINLIHAYRWKSTVC 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNLYDLLRNTNfrGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSAIKivDFGSSCQLG 306
Cdd:PHA03207  163 MVMPKYKCDLFTYVDRSG--PLPLEQAITIQRRLLEALAYLH--GRGIIHRDVKTENIFLDEPENAVLG--DFGAACKLD 236
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 307 QRI-----YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE-PLFSGANEVD--QMNKIVEVLGIPPA 373
Cdd:PHA03207  237 AHPdtpqcYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNvTLFGKQVKSSssQLRSIIRCMQVHPL 311
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
148-472 6.95e-11

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 63.89  E-value: 6.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNHLCL 227
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSK---RDPSEEIEILLRYGQHPN-----IITLKDVYDDGKHVYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFE-MLSYNLYDLLRNTNFrgvslnltrkFAQQMCTALLFLATPELS------IIHCDLKPENILLC----NPKrsAIKI 296
Cdd:cd14175    73 VTElMRGGELLDKILRQKF----------FSEREASSVLHTICKTVEylhsqgVVHRDLKPSNILYVdesgNPE--SLRI 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 297 VDFGSSCQL----GQRIYQYIQSRFYrSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEvDQMNKIVEVLGipp 372
Cdd:cd14175   141 CDFGFAKQLraenGLLMTPCYTANFV-APEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPS-DTPEEILTRIG--- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 373 ahildqapkARKFfeKLPDGTWNlkktkdgkreykppgtrklhnilgvetggpggrragesghTVADYLkfKDLILRMLD 452
Cdd:cd14175   216 ---------SGKF--TLSGGNWN----------------------------------------TVSDAA--KDLVSKMLH 242
                         330       340
                  ....*....|....*....|
gi 1113820495 453 YDPKTRIQPYYALQHSFFKK 472
Cdd:cd14175   243 VDPHQRLTAKQVLQHPWITQ 262
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
147-347 7.43e-11

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 63.52  E-value: 7.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAY------DRVEQEwVAIKI------IKNKKAFLNQAQIevrllelMNKHDTemkYYIVH 214
Cdd:cd05032     5 REKITLIRELGQGSFGMVYEGLakgvvkGEPETR-VAIKTvnenasMRERIEFLNEASV-------MKEFNC---HHVVR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 215 LKRHFMFRNHLCLVFEMLSY-NLYDLLR-------NTNFRGV-SLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENIL 285
Cdd:cd05032    74 LLGVVSTGQPTLVVMELMAKgDLKSYLRsrrpeaeNNPGLGPpTLQKFIQMAAEIADGMAYLA--AKKFVHRDLAARNCM 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 286 LcNPKRSaIKIVDFGsscqLGQRIYQyiqSRFYR------------SPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05032   152 V-AEDLT-VKIGDFG----MTRDIYE---TDYYRkggkgllpvrwmAPESLKDGVFTTKSDVWSFGVVLWEMAT 216
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
147-367 7.98e-11

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 64.31  E-value: 7.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI----EVRLLELMNKHDTEmkyYIVHLKRHFMFR 222
Cdd:cd05633     4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlalnERIMLSLVSTGDCP---FIVCMTYAFHTP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLsyNLYDLLRNTNFRGV-SLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGS 301
Cdd:cd05633    81 DKLCFILDLM--NGGDLHYHLSQHGVfSEKEMRFYATEIILGLEHMHNR--FVVYRDLKPANILL--DEHGHVRISDLGL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 302 SCQLGQRI-YQYIQSRFYRSPEVLL-GMPYDLAIDMWSLGCILVEMHTGEPLF-----SGANEVDQMNKIVEV 367
Cdd:cd05633   155 ACDFSKKKpHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTVNV 227
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
156-356 8.14e-11

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


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 63.41  E-value: 8.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNHLCLVFEMLSY- 234
Cdd:cd06647    15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPN-----IVNYLDSYLVGDELWVVMEYLAGg 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYDLLRNTNF-RGVSLNLTRKFAQqmctALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLG---QRIY 310
Cdd:cd06647    90 SLTDVVTETCMdEGQIAAVCRECLQ----ALEFLHSNQ--VIHRDIKSDNILL--GMDGSVKLTDFGFCAQITpeqSKRS 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 311 QYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd06647   162 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 207
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
150-365 9.09e-11

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: 64.65  E-value: 9.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQV----VKAYDRVeqewVAIKIIkNKKAFLNQAQI----EVRllELMNKHDTEmkyYIVHLKRHFMF 221
Cdd:cd05623    74 FEILKVIGRGAFGEVavvkLKNADKV----FAMKIL-NKWEMLKRAETacfrEER--DVLVNGDSQ---WITTLHYAFQD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEM-LSYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLflATPELSIIHCDLKPENILLcnPKRSAIKIVDFG 300
Cdd:cd05623   144 DNNLYLVMDYyVGGDLLTLLSKFEDR-LPEDMARFYLAEMVLAID--SVHQLHYVHRDIKPDNILM--DMNGHIRLADFG 218
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 301 SSCQLGQRiyQYIQSRF------YRSPEVLLGMP-----YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd05623   219 SCLKLMED--GTVQSSVavgtpdYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
271-416 1.01e-10

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: 63.18  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 271 ELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQL----GQRIYQYIQSRFYRSPEVLLGMP--YDLAIDMWSLGCILVE 344
Cdd:cd05583   117 KLGIIYRDIKLENILL--DSEGHVVLTDFGLSKEFlpgeNDRAYSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYE 194
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 345 MHTGEPLFSGANEVDQMNKIVE-VLGIPPAHILDQAPKARKFFEKLpdgtwnLKKTKDGKREYKPPGTRKLHN 416
Cdd:cd05583   195 LLTGASPFTVDGERNSQSEISKrILKSHPPIPKTFSAEAKDFILKL------LEKDPKKRLGAGPRGAHEIKE 261
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
149-348 1.07e-10

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 62.86  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVrllelMNkHDTEMKYYIVHLKRHFMFRNHLCLV 228
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREI-----IN-HRSLRHPNIIRFKEVVLTPTHLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSY-NLYDllRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSAIKIVDFG--SSCQL 305
Cdd:cd14662    75 MEYAAGgELFE--RICNAGRFSEDEARYFFQQLISGVSYCHS--MQICHRDLKLENTLLDGSPAPRLKICDFGysKSSVL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1113820495 306 GQRIYQYIQSRFYRSPEVLLGMPYDLAI-DMWSLGCILVEMHTG 348
Cdd:cd14662   151 HSQPKSTVGTPAYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVG 194
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
144-362 1.12e-10

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 63.03  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 144 EKWMDRYEI--DSLIGKGSFGQVVKAYDR-VEQEWVAIKIIKNKKAFLNQAQI--EVRLLELmnkhdTEMKYYIVHLKRH 218
Cdd:cd14197     3 EPFQERYSLspGRELGRGKFAVVRKCVEKdSGKEFAAKFMRKRRKGQDCRMEIihEIAVLEL-----AQANPWVINLHEV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLS----YNLYDLLRNTNFRGVSLnltRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKR-SA 293
Cdd:cd14197    78 YETASEMILVLEYAAggeiFNQCVADREEAFKEKDV---KRLMKQILEGVSFLHNN--NVVHLDLKPQNILLTSESPlGD 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 294 IKIVDFGSSCQL--GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANE------VDQMN 362
Cdd:cd14197   153 IKIVDFGLSRILknSEELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKqetflnISQMN 229
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
156-349 1.17e-10

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 62.51  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQewVAIKIIKNKKaflnqaQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHLCLVFEMLSY- 234
Cdd:cd14059     1 LGSGAQGAVFLGKFRGEE--VAVKKVRDEK------ETDIKHLRKLNHPN------IIKFKGVCTQAPCYCILMEYCPYg 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNpkRSAIKIVDFGSSCQLGQRIYQ--Y 312
Cdd:cd14059    67 QLYEVLRAG--REITPSLLVDWSKQIASGMNYLHLHK--IIHRDLKSPNVLVTY--NDVLKISDFGTSKELSEKSTKmsF 140
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1113820495 313 IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE 349
Cdd:cd14059   141 AGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGE 177
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
148-354 1.65e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 64.43  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK----NKKAFL----NQAQIEVRLlelmnKH-------DT---EMK 209
Cdd:NF033483    7 GRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVLRpdlaRDPEFVarfrREAQSAASL-----SHpnivsvyDVgedGGI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 210 YYIVhlkrhfMfrnhlclvfEmlsY----NLYDLLRNtnfRGVsLNLTR--KFAQQMCTALlflatpELS----IIHCDL 279
Cdd:NF033483   82 PYIV------M---------E---YvdgrTLKDYIRE---HGP-LSPEEavEIMIQILSAL------EHAhrngIVHRDI 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 280 KPENILLcnPKRSAIKIVDFG--------SSCQ----LGqriyqyiqSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:NF033483  134 KPQNILI--TKDGRVKVTDFGiaralsstTMTQtnsvLG--------TVHYLSPEQARGGTVDARSDIYSLGIVLYEMLT 203

                  ....*..
gi 1113820495 348 GEPLFSG 354
Cdd:NF033483  204 GRPPFDG 210
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
147-352 2.07e-10

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: 62.48  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEID--SLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMNKHDTEMKYYIVH-----LKRHF 219
Cdd:cd14171     3 LEEYEVNwtQKLGTGISGPVRVCVKKSTGERFALKILLDRP----KARTEVRLHMMCSGHPNIVQIYDVYansvqFPGES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLS-YNLYDllRNTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKRSA-IKIV 297
Cdd:cd14171    79 SPRARLLIVMELMEgGELFD--RISQHRHFTEKQAAQYTKQIALAVQHCHS--LNIAHRDLKPENLLLKDNSEDApIKLC 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 298 DFGSScQLGQRIYQYIQ-SRFYRSPEVL---------------LGMPY--DLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14171   155 DFGFA-KVDQGDLMTPQfTPYYVAPQVLeaqrrhrkersgiptSPTPYtyDKSCDMWSLGVIIYIMLCGYPPF 226
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
148-357 2.22e-10

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 62.34  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNHLCL 227
Cdd:cd14178     3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSK---RDPSEEIEILLRYGQHPN-----IITLKDVYDDGKFVYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFE-MLSYNLYD-LLRNTNFRgvslnlTRKFAQQMCT---ALLFLATPelSIIHCDLKPENILLC----NPKrsAIKIVD 298
Cdd:cd14178    75 VMElMRGGELLDrILRQKCFS------EREASAVLCTitkTVEYLHSQ--GVVHRDLKPSNILYMdesgNPE--SIRICD 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 299 FGSSCQL----GQRIYQYIQSRFYrSPEVLLGMPYDLAIDMWSLGCILVEMHTG-EPLFSGANE 357
Cdd:cd14178   145 FGFAKQLraenGLLMTPCYTANFV-APEVLKRQGYDAACDIWSLGILLYTMLAGfTPFANGPDD 207
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
156-348 2.84e-10

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 61.90  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQ--IEVRLLELMNkHDTEMKYYIVHLKRHFMFRNHLCLVfeMLS 233
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERwcLEIQIMKRLN-HPNVVAARDVPEGLQKLAPNDLPLL--AME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRN-----TNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCN-PKRSAIKIVDFGSSCQL-- 305
Cdd:cd14038    79 YCQGGDLRKylnqfENCCGLREGAILTLLSDISSALRYLH--ENRIIHRDLKPENIVLQQgEQRLIHKIIDLGYAKELdq 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1113820495 306 GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd14038   157 GSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITG 199
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
155-362 3.21e-10

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 62.44  E-value: 3.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIK----NKKAFLNQAQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05588     2 VIGRGSYAKVLMVELKKTKRIYAMKVIKkelvNDDEDIDWVQTEKHVFETASNHP-----FLVGLHSCFQTESRLFFVIE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSYN--LYDLLRNtnfRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQLGQR 308
Cdd:cd05588    77 FVNGGdlMFHMQRQ---RRLPEEHARFYSAEISLALNFLH--EKGIIYRDLKLDNVLL--DSEGHIKLTDYGM-CKEGLR 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 309 IYQyIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFS--GANEVDQMN 362
Cdd:cd05588   149 PGD-TTSTFcgtpnYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDivGSSDNPDQN 208
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
140-356 3.28e-10

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: 62.05  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 140 VKNGEKWMDRYEidsLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMNKHDTEmKYYIVHLKRHF 219
Cdd:cd06655    14 IGDPKKKYTRYE---KIGQGASGTVFTAIDVATGQEVAIKQINLQK----QPKKELIINEILVMKELK-NPNIVNFLDSF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MFRNHLCLVFEMLSY-NLYDLLRNTNFRGVSLnltRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVD 298
Cdd:cd06655    86 LVGDELFVVMEYLAGgSLTDVVTETCMDEAQI---AAVCRECLQALEFLHANQ--VIHRDIKSDNVLL--GMDGSVKLTD 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 299 FGSSCQLG---QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd06655   159 FGFCAQITpeqSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 219
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
148-389 4.16e-10

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 60.99  E-value: 4.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEI-DSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIevrllelMNKHDtemkyyivHLKrhfMFRNHLC 226
Cdd:cd14109     3 ELYEIgEEDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMREVDI-------HNSLD--------HPN---IVQMHDA 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNLYDLLrNTNFRGVSLNLTRK-----------FAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKrsaIK 295
Cdd:cd14109    65 YDDEKLAVTVIDNL-ASTIELVRDNLLPGkdyyterqvavFVRQLLLALKHMH--DLGIAHLDLRPEDILLQDDK---LK 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 296 IVDFGSSCQLGQ-RIYQYIQ-SRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE----VLG 369
Cdd:cd14109   139 LADFGQSRRLLRgKLTTLIYgSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSgkwsFDS 218
                         250       260
                  ....*....|....*....|
gi 1113820495 370 IPPAHILDQapkARKFFEKL 389
Cdd:cd14109   219 SPLGNISDD---ARDFIKKL 235
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
156-353 7.04e-10

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 61.43  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKN----KKAFLNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHLCLVFE- 230
Cdd:cd05610    12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKadmiNKNMVHQVQAERDALALSKSP------FIVHLYYSLQSANNVYLVMEy 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSYNLYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFG---------- 300
Cdd:cd05610    86 LIGGDVKSLLHIYGY--FDEEMAVKYISEVALALDYLH--RHGIIHRDLKPDNMLISN--EGHIKLTDFGlskvtlnrel 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 --------SSCQLGQRIYQYIQSRF--------------------------------------YRSPEVLLGMPYDLAID 334
Cdd:cd05610   160 nmmdilttPSMAKPKNDYSRTPGQVlslisslgfntptpyrtpksvrrgaarvegerilgtpdYLAPELLLGKPHGPAVD 239
                         250
                  ....*....|....*....
gi 1113820495 335 MWSLGCILVEMHTGEPLFS 353
Cdd:cd05610   240 WWALGVCLFEFLTGIPPFN 258
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
155-361 7.46e-10

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 60.35  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQewVAIKIIKNKKAF--LNQaqievRLLELMNKHDTEMKYYIVHLKRHFMfrnhlcLVFEML 232
Cdd:cd14068     1 LLGDGGFGSVYRAVYRGED--VAVKIFNKHTSFrlLRQ-----ELVVLSHLHHPSLVALLAAGTAPRM------LVMELA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRSA---IKIVDFGSS---CQLG 306
Cdd:cd14068    68 PKGSLDALLQQDNASLTRTLQHRIALHVADGLRYLHSA--MIIYRDLKPHNVLLFTLYPNCaiiAKIADYGIAqycCRMG 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 307 QRIYQyiQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHT-GEPLFSG---ANEVDQM 361
Cdd:cd14068   146 IKTSE--GTPGFRAPEVARGnVIYNQQADVYSFGLLLYDILTcGERIVEGlkfPNEFDEL 203
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
145-389 7.76e-10

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


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 60.66  E-value: 7.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLLELMNkHDTEMKYYIVHLKR----- 217
Cdd:cd14048     3 RFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRlpNNELAREKVLREVRALAKLD-HPGIVRYFNAWLERppegw 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 -HFMFRNHLCLVFEMLSY-NLYDLL-RNTNFRGVSLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILLCnpKRSAI 294
Cdd:cd14048    82 qEKMDEVYLYIQMQLCRKeNLKDWMnRRCTMESRELFVCLNIFKQIASAVEYLHSKGL--IHRDLKPSNVFFS--LDDVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 295 KIVDFGSSCQLGQ---------------RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMhtgepLFSGANEVD 359
Cdd:cd14048   158 KVGDFGLVTAMDQgepeqtvltpmpayaKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFEL-----IYSFSTQME 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1113820495 360 QMNKIVEV--LGIPPahILDQA-PKARKFFEKL 389
Cdd:cd14048   233 RIRTLTDVrkLKFPA--LFTNKyPEERDMVQQM 263
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
150-358 7.99e-10

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: 60.09  E-value: 7.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAF---------LNQAQIEVRLLELMNKHDTEmkyYIVHLKRHFM 220
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILvdtwvrdrkLGTVPLEIHILDTLNKRSHP---NIVKLLDFFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNHLCLVFEM--LSYNLYDLL-RNTNfrgVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIV 297
Cdd:cd14004    79 DDEFYYLVMEKhgSGMDLFDFIeRKPN---MDEKEAKYIFRQVADAVKHLHDQG--IVHRDIKDENVIL--DGNGTIKLI 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 298 DFGSSCQLGQ-RIYQYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGANEV 358
Cdd:cd14004   152 DFGSAAYIKSgPFDTFVGTIDYAAPEVLRGNPYGgKEQDIWALGVLLYTLVFKENPFYNIEEI 214
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
149-379 8.60e-10

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: 60.03  E-value: 8.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK-AFLNQAQIEVRLLELmnkHDTEMKYYIVHLKRHFMFRNHLCL 227
Cdd:cd14188     2 RYCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRvSKPHQREKIDKEIEL---HRILHHKHVVQFYHYFEDKENIYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSY-NLYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQL- 305
Cdd:cd14188    79 LLEYCSRrSMAHILKARKV--LTEPEVRYYLRQIVSGLKYLHEQE--ILHRDLKLGNFFI--NENMELKVGDFGLAARLe 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 306 --GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQA 379
Cdd:cd14188   153 plEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPA 228
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
156-389 9.14e-10

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 60.42  E-value: 9.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKaflnQAQIEVRLLELMNKHDTEMKYyIVHLKRHFMFRNHLCLVFEMLSYN 235
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRK----QQRRELLFNEVVIMRDYQHEN-VVEMYNSYLVGDELWVVMEFLEGG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 236 -LYDLLRNTNfrgvslnLTRKFAQQMCTALL--FLATPELSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQLG---QRI 309
Cdd:cd06657   103 aLTDIVTHTR-------MNEEQIAAVCLAVLkaLSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGFCAQVSkevPRR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 310 YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKL 389
Cdd:cd06657   174 KSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLDRL 253
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
156-366 9.55e-10

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: 60.81  E-value: 9.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQ----IEVRLLELMnKHDTEMKYYIVHLKRHFMFrnhlcLVFEM 231
Cdd:cd06634    23 IGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWqdiiKEVKFLQKL-RHPNTIEYRGCYLREHTAW-----LVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYNLYDLLR--NTNFRGVSLNLTRKFAQQmctALLFLATPELsiIHCDLKPENILLCNPkrSAIKIVDFGSSCQLGQrI 309
Cdd:cd06634    97 CLGSASDLLEvhKKPLQEVEIAAITHGALQ---GLAYLHSHNM--IHRDVKAGNILLTEP--GLVKLGDFGSASIMAP-A 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 310 YQYIQSRFYRSPEVLLGM---PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd06634   169 NSFVGTPYWMAPEVILAMdegQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQ 228
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
152-347 1.03e-09

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 60.36  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 152 IDSLIGKGSFGQVVKAY-----DRVEQEWVAIKIIKNkkaflNQAQIEVR-------LLELMNkHDTEMKYY-------- 211
Cdd:cd05045     4 LGKTLGEGEFGKVVKATafrlkGRAGYTTVAVKMLKE-----NASSSELRdllsefnLLKQVN-HPHVIKLYgacsqdgp 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 212 ---IVHLKRHFMFRNHLCLVFEM-LSYNLYDLLRNTNF------RGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKP 281
Cdd:cd05045    78 lllIVEYAKYGSLRSFLRESRKVgPSYLGSDGNRNSSYldnpdeRALTMGDLISFAWQISRGMQYLA--EMKLVHRDLAA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 282 ENILLCNPKRsaIKIVDFGsscqLGQRIYQ---YI---QSRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05045   156 RNVLVAEGRK--MKISDFG----LSRDVYEedsYVkrsKGRIpvkWMAIESLFDHIYTTQSDVWSFGVLLWEIVT 224
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
154-347 1.04e-09

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 60.29  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 154 SLIGKGSFGQV-VKAYDRVEQ---EWVAIKIIKNKKA-FLNQAQIEVRLLELMNkHDTEMKYYIVHLKRHfmfRNHLCLV 228
Cdd:cd05081    10 SQLGKGNFGSVeLCRYDPLGDntgALVAVKQLQHSGPdQQRDFQREIQILKALH-SDFIVKYRGVSYGPG---RRSLRLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEML-SYNLYDLL-RNTNFRGVSLNLTrkFAQQMCTALLFLATPELsiIHCDLKPENILLcnPKRSAIKIVDFGSSCQLG 306
Cdd:cd05081    86 MEYLpSGCLRDFLqRHRARLDASRLLL--YSSQICKGMEYLGSRRC--VHRDLAARNILV--ESEAHVKIADFGLAKLLP 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1113820495 307 Q-RIYQYIQSR-----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05081   160 LdKDYYVVREPgqspiFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
150-348 1.17e-09

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: 59.66  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA------FLNQaqiEVRLLELMNKHDTEMKYYIVH-LKRhfmfr 222
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLdqktqrLLSR---EISSMEKLHHPNIIRLYEVVEtLSK----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 nhLCLVFEMLSY-NLYDLLRNtnfRGVSLNLTRK--FAQqMCTALLFLAtpELSIIHCDLKPENILLCNPKRsaIKIVDF 299
Cdd:cd14075    76 --LHLVMEYASGgELYTKIST---EGKLSESEAKplFAQ-IVSAVKHMH--ENNIIHRDLKAENVFYASNNC--VKVGDF 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 300 GSSCQL--GQRIYQYIQSRFYRSPEVL-----LGMPydlaIDMWSLGCILVEMHTG 348
Cdd:cd14075   146 GFSTHAkrGETLNTFCGSPPYAAPELFkdehyIGIY----VDIWALGVLLYFMVTG 197
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
156-348 1.17e-09

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 60.15  E-value: 1.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIK--------IIKNKKAFLNQAQIEVRLlelmnKHDTEMKYYIVHLKRHFMFRNHL-C 226
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqelspSDKNRERWCLEVQIMKKL-----NHPNVVSARDVPPELEKLSPNDLpL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLL-RNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCN-PKRSAIKIVDFGSSC 303
Cdd:cd13989    76 LAMEYCSGgDLRKVLnQPENCCGLKESEVRTLLSDISSAISYLH--ENRIIHRDLKPENIVLQQgGGRVIYKLIDLGYAK 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QLGQriyQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd13989   154 ELDQ---GSLCTSFvgtlqYLAPELFESKKYTCTVDYWSFGTLAFECITG 200
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
156-364 1.24e-09

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 59.66  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAydrveqEW---------VAIKIIKNKKafLNQAQI------EVRLLELMNkHDTEMKYYIVHLKRHFM 220
Cdd:cd05040     3 LGDGSFGVVRRG------EWttpsgkviqVAVKCLKSDV--LSQPNAmddflkEVNAMHSLD-HPNLIRLYGVVLSSPLM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 frnhlcLVFEMLSY-NLYDLLRNtnfRGVSLNLTR--KFAQQMCTALLFLATPELsiIHCDLKPENILLCNPKRsaIKIV 297
Cdd:cd05040    74 ------MVTELAPLgSLLDRLRK---DQGHFLISTlcDYAVQIANGMAYLESKRF--IHRDLAARNILLASKDK--VKIG 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 298 DFGSSCQLGQRiYQYIQSRFYR-------SPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGANEVDQMNKI 364
Cdd:cd05040   141 DFGLMRALPQN-EDHYVMQEHRkvpfawcAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKI 214
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
140-352 1.32e-09

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 60.47  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 140 VKNGEKWMDRYE-----------------IDSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKkaflnqaqievrlLELMN 202
Cdd:cd05596     1 NKNIENFLNRYEkpvneitklrmnaedfdVIKVIGRGAFGEVQLVRHKSTKKVYAMKLL-SK-------------FEMIK 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 203 KHDT----EMKYYIVH------LKRHFMFRN--HLCLVFE-MLSYNLYDLLRNTNFrgvslnlTRKFAQQMC--TALLFL 267
Cdd:cd05596    67 RSDSaffwEERDIMAHansewiVQLHYAFQDdkYLYMVMDyMPGGDLVNLMSNYDV-------PEKWARFYTaeVVLALD 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 268 ATPELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQ----RIYQYIQSRFYRSPEVLLGMP----YDLAIDMWSLG 339
Cdd:cd05596   140 AIHSMGFVHRDVKPDNMLL--DASGHLKLADFGTCMKMDKdglvRSDTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVG 217
                         250
                  ....*....|...
gi 1113820495 340 CILVEMHTGEPLF 352
Cdd:cd05596   218 VFLYEMLVGDTPF 230
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
156-347 1.38e-09

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 59.58  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYdRVEQEWVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVHLKRhfmfrNHLCLVFEM 231
Cdd:cd05112    12 IGSGQFGLVHLGY-WLNKDKVAIKTIRegamSEEDFIEEAEVMMKL-----SHPKLVQLYGVCLEQ-----APICLVFEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYN-LYDLLRNTnfRGvslnltrKFAQQ--------MCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSS 302
Cdd:cd05112    81 MEHGcLSDYLRTQ--RG-------LFSAEtllgmcldVCEGMAYLE--EASVIHRDLAARNCLV--GENQVVKVSDFGMT 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 303 cqlgqRIY---QYIQS---RF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05112   148 -----RFVlddQYTSStgtKFpvkWSSPEVFSFSRYSSKSDVWSFGVLMWEVFS 196
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
156-356 1.38e-09

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: 60.12  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNHLCLVFEMLSY- 234
Cdd:cd06656    27 IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPN-----IVNYLDSYLVGDELWVVMEYLAGg 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYDLLRNTNF-RGVSLNLTRKFAQqmctALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLG---QRIY 310
Cdd:cd06656   102 SLTDVVTETCMdEGQIAAVCRECLQ----ALDFLHSNQ--VIHRDIKSDNILL--GMDGSVKLTDFGFCAQITpeqSKRS 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 311 QYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd06656   174 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNEN 219
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
151-373 1.42e-09

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 59.71  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAYDR---VEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDTEMKYYIVhLKRHFMFRNHLCL 227
Cdd:cd14032     4 KFDIELGRGSFKTVYKGLDTetwVEVAWCELQDRKLTKVERQRFKEEAEMLKGL-QHPNIVRFYDF-WESCAKGKRCIVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFE-MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSaIKIVDFG-SSCQL 305
Cdd:cd14032    82 VTElMTSGTLKTYLKR--FKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGPTGS-VKIGDLGlATLKR 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 306 GQRIYQYIQSRFYRSPEvLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVeVLGIPPA 373
Cdd:cd14032   159 ASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKV-TCGIKPA 224
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
156-356 2.00e-09

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: 59.35  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNHLCLVFEMLSY- 234
Cdd:cd06654    28 IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPN-----IVNYLDSYLVGDELWVVMEYLAGg 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYDLLRNTNF-RGVSLNLTRKFAQqmctALLFLATPElsIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLG---QRIY 310
Cdd:cd06654   103 SLTDVVTETCMdEGQIAAVCRECLQ----ALEFLHSNQ--VIHRDIKSDNILL--GMDGSVKLTDFGFCAQITpeqSKRS 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 311 QYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGAN 356
Cdd:cd06654   175 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNEN 220
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
154-345 2.04e-09

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 58.90  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 154 SLIGKGSFGQVVKAYDRVEQewVAIKIIKN----KKAFLNQAQIEVRLlelmnKHDTemkyyIVHLKRHFMFRNHLCLVF 229
Cdd:cd05039    12 ELIGKGEFGDVMLGDYRGQK--VAVKCLKDdstaAQAFLAEASVMTTL-----RHPN-----LVQLLGVVLEGNGLYIVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 E-MLSYNLYDLLRNtnfRGVSLNLTR---KFAQQMCTALLFLAtpELSIIHCDLKPENILLcNPKRSAiKIVDFG--SSC 303
Cdd:cd05039    80 EyMAKGSLVDYLRS---RGRAVITRKdqlGFALDVCEGMEYLE--SKKFVHRDLAARNVLV-SEDNVA-KVSDFGlaKEA 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 304 QLGQRIyqyiqSRF---YRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd05039   153 SSNQDG-----GKLpikWTAPEALREKKFSTKSDVWSFGILLWEI 192
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
155-354 2.15e-09

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 58.90  E-value: 2.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQewVAIKIIK-----NKKAFLNQAQIEVRLLELMnKHDTemkyyIVHLKRHFMFRNHLCLVF 229
Cdd:cd14146     1 IIGVGGFGKVYRATWKGQE--VAVKAARqdpdeDIKATAESVRQEAKLFSML-RHPN-----IIKLEGVCLEEPNLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EM-----LSYNLYDLLRNTNFRG---VSLNLTRKFAQQMCTALLFLATPEL-SIIHCDLKPENILLCNPK------RSAI 294
Cdd:cd14146    73 EFarggtLNRALAAANAAPGPRRarrIPPHILVNWAVQIARGMLYLHEEAVvPILHRDLKSSNILLLEKIehddicNKTL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 295 KIVDFGSSCQLGQRIYQYIQSRF-YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSG 354
Cdd:cd14146   153 KITDFGLAREWHRTTKMSAAGTYaWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
pknD PRK13184
serine/threonine-protein kinase PknD;
147-347 2.33e-09

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 60.94  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKN--------KKAFLNQAQIEVRLLelmnkH-----------DTE 207
Cdd:PRK13184    1 MQRYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREdlsenpllKKRFLREAKIAADLI-----HpgivpvysicsDGD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 208 MKYYIVHLKRHFMFRNHLCLVFEMlsynlyDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLc 287
Cdd:PRK13184   76 PVYYTMPYIEGYTLKSLLKSVWQK------ESLSKELAEKTSVGAFLSIFHKICATIEYVHSK--GVLHRDLKPDNILL- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 288 nPKRSAIKIVDFGS--SCQLGQ--------RIYQYIQSRF-----------YRSPEVLLGMPYDLAIDMWSLGCILVEMH 346
Cdd:PRK13184  147 -GLFGEVVILDWGAaiFKKLEEedlldidvDERNICYSSMtipgkivgtpdYMAPERLLGVPASESTDIYALGVILYQML 225

                  .
gi 1113820495 347 T 347
Cdd:PRK13184  226 T 226
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
143-394 2.56e-09

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: 59.27  E-value: 2.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 143 GEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI----EVRLLELMNkHDTEMKYYIvhlkrH 218
Cdd:cd08229    19 GYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARAdcikEIDLLKQLN-HPNVIKYYA-----S 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEML-SYNLYDLLRN--TNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCnpKRSAIK 295
Cdd:cd08229    93 FIEDNELNIVLELAdAGDLSRMIKHfkKQKRLIPEKTVWKYFVQLCSALEHMHSRR--VMHRDIKPANVFIT--ATGVVK 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 296 IVDFGSSCQLGQRI---YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGanevDQMN-----KIVEV 367
Cdd:cd08229   169 LGDLGLGRFFSSKTtaaHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG----DKMNlyslcKKIEQ 244
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1113820495 368 LGIPPAHILDQAPKARKFF--------EKLPDGTW 394
Cdd:cd08229   245 CDYPPLPSDHYSEELRQLVnmcinpdpEKRPDITY 279
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
151-373 2.57e-09

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 58.96  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAYDR---VEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDTEMKYYIvhlKRHFMFRNHLCL 227
Cdd:cd14031    13 KFDIELGRGAFKTVYKGLDTetwVEVAWCELQDRKLTKAEQQRFKEEAEMLKGL-QHPNIVRFYD---SWESVLKGKKCI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFE---MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSaIKIVDFGSSCQ 304
Cdd:cd14031    89 VLVtelMTSGTLKTYLKR--FKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGS-VKIGDLGLATL 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 LGQRIYQ-YIQSRFYRSPEvLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVeVLGIPPA 373
Cdd:cd14031   166 MRTSFAKsVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKV-TSGIKPA 233
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
156-345 2.66e-09

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 58.66  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNkkaFLNQAQIeVRLLELMNK--HDTEMKYYIVHLKRhfmfrNHLCLVFEMLS 233
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKR---FDEQRSF-LKEVKLMRRlsHPNILRFIGVCVKD-----NKLNFITEYVN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 Y-NLYDLLRNTNfrgVSLNLTRK--FAQQMCTALLFLATpeLSIIHCDLKPENILL--CNPKRSAIkIVDFGSSCQLG-- 306
Cdd:cd14065    72 GgTLEELLKSMD---EQLPWSQRvsLAKDIASGMAYLHS--KNIIHRDLNSKNCLVreANRGRNAV-VADFGLAREMPde 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 307 -------QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd14065   146 ktkkpdrKKRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEI 191
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
151-342 2.70e-09

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: 58.83  E-value: 2.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAYDRVEQEWVAIK--IIKNKKAfLNQAQIEVRLLELMNKHDTEMKYYIVHLKRhfmFRNHLCLV 228
Cdd:cd14037     6 TIEKYLAEGGFAHVYLVKTSNGGNRAALKrvYVNDEHD-LNVCKREIEIMKRLSGHKNIVGYIDSSANR---SGNGVYEV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSY----NLYDLLrNTNFR-GVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLcNPKRSaIKIVDFGSSC 303
Cdd:cd14037    82 LLLMEYckggGVIDLM-NQRLQtGLTESEILKIFCDVCEAVAAMHYLKPPLIHRDLKVENVLI-SDSGN-YKLCDFGSAT 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 304 -------------QLGQRIYQYIQSRfYRSPEVL---LGMPYDLAIDMWSLGCIL 342
Cdd:cd14037   159 tkilppqtkqgvtYVEEDIKKYTTLQ-YRAPEMIdlyRGKPITEKSDIWALGCLL 212
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
148-365 2.87e-09

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 60.02  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-------KNKKAFLNQaqiEVRLLELMNKHdtemkyYIVHLKRHFM 220
Cdd:cd05622    73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLskfemikRSDSAFFWE---ERDIMAFANSP------WVVQLFYAFQ 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRNHLCLVFE-MLSYNLYDLLRNTNfrgVSLNLTRKFAQQMCTALlfLATPELSIIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd05622   144 DDRYLYMVMEyMPGGDLVNLMSNYD---VPEKWARFYTAEVVLAL--DAIHSMGFIHRDVKPDNMLL--DKSGHLKLADF 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 300 GSSCQLGQ----RIYQYIQSRFYRSPEVLLGMP----YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd05622   217 GTCMKMNKegmvRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 290
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
150-353 2.97e-09

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: 58.39  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII----KNKKAFLNQAQIEVRLlelmnKHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIpykpEDKQLVLREYQVLRRL-----SHP-----RIAQLHSAYLSPRHL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYN--LYDLLRNTNFRGVSLnltRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPkrSAIKIVDFGSSC 303
Cdd:cd14110    75 VLIEELCSGPelLYNLAERNSYSEAEV---TDYLWQILSAVDYLHSR--RILHLDLRSENMIITEK--NLLKIVDLGNAQ 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 304 QLGQ-------RIYQYIQSrfyRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFS 353
Cdd:cd14110   148 PFNQgkvlmtdKKGDYVET---MAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVS 201
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
148-348 3.10e-09

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 59.29  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII--KNKKAFLNQAQIEVRLLELMNKHdtemkyYIVHLKRHFMFRNHL 225
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIhlEIKPAIRNQIIRELQVLHECNSP------YIVGFYGAFYSDGEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFE-MLSYNLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPElSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQ 304
Cdd:cd06649    79 SICMEhMDGGSLDQVLKEA--KRIPEEILGKVSIAVLRGLAYLREKH-QIMHRDVKPSNILVNS--RGEIKLCDFGVSGQ 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 305 LGQRIYQ-YIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd06649   154 LIDSMANsFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIG 198
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
152-354 3.21e-09

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


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 58.50  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 152 IDSLIGKGSFGQVVKAYDRveQEWVAIKIIKNK-----KAFLNQAQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHLC 226
Cdd:cd14147     7 LEEVIGIGGFGKVYRGSWR--GELVAVKAARQDpdediSVTAESVRQEARLFAMLAHPN------IIALKAVCLEEPNLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNlyDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPEL-SIIHCDLKPENILLCNP------KRSAIKIVDF 299
Cdd:cd14147    79 LVMEYAAGG--PLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALvPVIHRDLKSNNILLLQPienddmEHKTLKITDF 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 300 GSSCQLGQRIYQYIQSRF-YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSG 354
Cdd:cd14147   157 GLAREWHKTTQMSAAGTYaWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRG 212
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
156-389 3.23e-09

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 58.39  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAydrveqEW-----VAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVhlkrhfMFRNHLC 226
Cdd:cd14203     3 LGQGCFGEVWMG------TWngttkVAIKTLKpgtmSPEAFLEEAQIMKKL-----RHDKLVQLYAV------VSEEPIY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQL 305
Cdd:cd14203    66 IVTEFMSKgSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIE--RMNYIHRDLRAANILVGD--NLVCKIADFGLARLI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 GQRIYQYIQ-SRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGAN------EVDQMNKIVEVLGIPPA- 373
Cdd:cd14203   142 EDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNnrevleQVERGYRMPCPPGCPESl 221
                         250       260
                  ....*....|....*....|.
gi 1113820495 374 -----HILDQAPKARKFFEKL 389
Cdd:cd14203   222 helmcQCWRKDPEERPTFEYL 242
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
149-363 3.28e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 59.88  E-value: 3.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNK---KAFLNQAQIEVRLLelMNkhdteMKYY-IVHLKRHFMFRN- 223
Cdd:PTZ00283   33 KYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEgmsEADKNRAQAEVCCL--LN-----CDFFsIVKCHEDFAKKDp 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 ----HLCLVFEMLSY-NLYDLLRNTNFRGVSlnlTRKFAQQMcTALLF----LATPEL---SIIHCDLKPENILLCNpkR 291
Cdd:PTZ00283  106 rnpeNVLMIALVLDYaNAGDLRQEIKSRAKT---NRTFREHE-AGLLFiqvlLAVHHVhskHMIHRDIKSANILLCS--N 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 292 SAIKIVDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNK 363
Cdd:PTZ00283  180 GLVKLGDFGFSKMYAATVSDDVGRTFcgtpyYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHK 256
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
274-366 3.39e-09

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 58.30  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 274 IIHCDLKPENILLCNpkRSAIKIVDFGSSCQLG----QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE 349
Cdd:cd14111   120 VLHLDIKPDNIMVTN--LNAIKIVDFGSAQSFNplslRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGR 197
                          90
                  ....*....|....*..
gi 1113820495 350 PLFSGANEVDQMNKIVE 366
Cdd:cd14111   198 SPFEDQDPQETEAKILV 214
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
150-347 4.18e-09

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: 58.09  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIK----NKKAFLNQAQiEVRLLELMNKHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRsrfrGEKDRKRKLE-EVERHEKLGEHP-----NCVRFIKAWEEKGIL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNfrgvSLNLTR--KFAQQMCTALLFLATPELsiIHCDLKPENILLcnPKRSAIKIVDFGSSC 303
Cdd:cd14050    77 YIQTELCDTSLQQYCEETH----SLPESEvwNILLDLLKGLKHLHDHGL--IHLDIKPANIFL--SKDGVCKLGDFGLVV 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1113820495 304 QLGQRIYQYIQ---SRfYRSPEVLLGMpYDLAIDMWSLGCILVEMHT 347
Cdd:cd14050   149 ELDKEDIHDAQegdPR-YMAPELLQGS-FTKAADIFSLGITILELAC 193
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
150-345 5.54e-09

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 57.69  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNK-------KAFLNQaqiEVRLLELMNKHDTEMKYYIVHLKRhfmfr 222
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpeefiQRFLPR---ELQIVERLDHKNIIHVYEMLESAD----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLS-YNLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnpKRSAIKIVDFGS 301
Cdd:cd14163    74 GKIYLVMELAEdGDVFDCV--LHGGPLPEHRAKALFRQLVEAIRYCHG--CGVAHRDLKCENALL---QGFTLKLTDFGF 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1113820495 302 SCQL---GQRIYQ-YIQSRFYRSPEVLLGMPYDLAI-DMWSLGCILVEM 345
Cdd:cd14163   147 AKQLpkgGRELSQtFCGSTAYAAPEVLQGVPHDSRKgDIWSMGVVLYVM 195
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
225-400 6.64e-09

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: 57.67  E-value: 6.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYNLYDLLRNTNFRGVSL-----NLTRKFAQQMCTALLFLATPelSIIHCDLKPENIL---LCNPKRSAIKI 296
Cdd:cd14067    83 LCFALELAPLGSLNTVLEENHKGSSFmplghMLTFKIAYQIAAGLAYLHKK--NIIFCDLKSDNILvwsLDVQEHINIKL 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 297 VDFGSSCQ-LGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEvlGIPPahI 375
Cdd:cd14067   161 SDYGISRQsFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSK--GIRP--V 236
                         170       180
                  ....*....|....*....|....*..
gi 1113820495 376 LDQaPKARKFF--EKLPDGTWNLKKTK 400
Cdd:cd14067   237 LGQ-PEEVQFFrlQALMMECWDTKPEK 262
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
150-389 7.41e-09

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 58.14  E-value: 7.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI----EVRLLELMNKHDTEmkyYIVHLKRHFMFRNHL 225
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlalnERIMLSLVSTGDCP---FIVCMSYAFHTPDKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLsyNLYDLLRNTNFRGV-SLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ 304
Cdd:cd14223    79 SFILDLM--NGGDLHYHLSQHGVfSEAEMRFYAAEIILGLEHMHSR--FVVYRDLKPANILL--DEFGHVRISDLGLACD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 LGQRI-YQYIQSRFYRSPEVLL-GMPYDLAIDMWSLGCILVEMHTGEPLF-----SGANEVDQMNKIVEVlGIPPAHild 377
Cdd:cd14223   153 FSKKKpHASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFrqhktKDKHEIDRMTLTMAV-ELPDSF--- 228
                         250
                  ....*....|..
gi 1113820495 378 qAPKARKFFEKL 389
Cdd:cd14223   229 -SPELRSLLEGL 239
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
150-366 7.66e-09

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: 58.47  E-value: 7.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKII-------KNKKAFLNQAQievrllELMNKHDTEmkyYIVHLKRHFMFR 222
Cdd:cd05621    54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLskfemikRSDSAFFWEER------DIMAFANSP---WVVQLFCAFQDD 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFE-MLSYNLYDLLRNTNfrgVSLNLTRKFAQQMCTALlfLATPELSIIHCDLKPENILLcnPKRSAIKIVDFGS 301
Cdd:cd05621   125 KYLYMVMEyMPGGDLVNLMSNYD---VPEKWAKFYTAEVVLAL--DAIHSMGLIHRDVKPDNMLL--DKYGHLKLADFGT 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 302 SCQLGQ----RIYQYIQSRFYRSPEVLLGMP----YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05621   198 CMKMDEtgmvHCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMD 270
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
155-367 7.80e-09

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 57.45  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI----EVRLLELMNKHDTEMkyYIVHLKRHFMFRNHLCLVFE 230
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETlalnERIMLSLVSTGGDCP--FIVCMTYAFQTPDKLCFILD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLsyNLYDLLRNTNFRGV-SLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLGQRI 309
Cdd:cd05606    79 LM--NGGDLHYHLSQHGVfSEAEMRFYAAEVILGLEHMH--NRFIVYRDLKPANILLD--EHGHVRISDLGLACDFSKKK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 310 -YQYIQSRFYRSPEVLL-GMPYDLAIDMWSLGCILVEMHTGEPLFSGAN-----EVDQMNKIVEV 367
Cdd:cd05606   153 pHASVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKtkdkhEIDRMTLTMNV 217
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
156-341 7.82e-09

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 57.28  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKA--YDRVEqewVAIKIIKnkKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFrnhlcLVFEMLS 233
Cdd:cd13982     9 LGYGSEGTIVFRgtFDGRP---VAVKRLL--PEFFDFADREVQLLRESDEHPNVIRYFCTEKDRQFLY-----IALELCA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRNTNFRGVSLNLTR---KFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSA---IKIVDFGSSCQLGQ 307
Cdd:cd13982    79 ASLQDLVESPRESKLFLRPGLepvRLLRQIASGLAHLH--SLNIVHRDLKPQNILISTPNAHGnvrAMISDFGLCKKLDV 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1113820495 308 RIYQYIQSRF------YRSPEVLLGMPYD---LAIDMWSLGCI 341
Cdd:cd13982   157 GRSSFSRRSGvagtsgWIAPEMLSGSTKRrqtRAVDIFSLGCV 199
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
149-342 7.98e-09

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: 57.52  E-value: 7.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI-EVRLLELMNKHDTEMKYYIV---------HLKRH 218
Cdd:cd14036     1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIqEINFMKKLSGHPNIVQFCSAasigkeesdQGQAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLClvfemlSYNLYDLLRNTNFRG-VSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRsaIKIV 297
Cdd:cd14036    81 YLLLTELC------KGQLVDFVKKVEAPGpFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLIGNQGQ--IKLC 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 298 DFGSSCQL----------GQR--IYQYIQ---SRFYRSPEVL---LGMPYDLAIDMWSLGCIL 342
Cdd:cd14036   153 DFGSATTEahypdyswsaQKRslVEDEITrntTPMYRTPEMIdlySNYPIGEKQDIWALGCIL 215
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
149-329 9.22e-09

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 57.38  E-value: 9.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKI--IKNKKAflnQAQIEVRLLELMNK---------HDTEMKYYIvhlkr 217
Cdd:cd14125     1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLesVKTKHP---QLLYESKLYKILQGgvgipnvrwYGVEGDYNV----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 218 hfmfrnhlcLVFEMLSYNLYDLLrntNF--RGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKR-SAI 294
Cdd:cd14125    73 ---------MVMDLLGPSLEDLF---NFcsRKFSLKTVLMLADQMISRIEYVHSK--NFIHRDIKPDNFLMGLGKKgNLV 138
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1113820495 295 KIVDFGsscqLGQRiyqyiqsrfYRSPEVLLGMPY 329
Cdd:cd14125   139 YIIDFG----LAKK---------YRDPRTHQHIPY 160
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
155-371 9.66e-09

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 56.92  E-value: 9.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQewVAIKII-----KNKKAFLNQAQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHLCLVF 229
Cdd:cd14148     1 IIGVGGFGKVYKGLWRGEE--VAVKAArqdpdEDIAVTAENVRQEARLFWMLQHPN------IIALRGVCLNPPHLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNlyDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPE-LSIIHCDLKPENILLCNPKRS------AIKIVDFGSS 302
Cdd:cd14148    73 EYARGG--ALNRALAGKKVPPHVLVNWAVQIARGMNYLHNEAiVPIIHRDLKSSNILILEPIENddlsgkTLKITDFGLA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 303 CQLGQRIYQYIQSRF-YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFsgaNEVD--------QMNKIveVLGIP 371
Cdd:cd14148   151 REWHKTTKMSAAGTYaWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY---REIDalavaygvAMNKL--TLPIP 223
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
155-345 1.38e-08

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 56.68  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAydRVEQEWVAIKI--IKNKKAFLNQAQIevrLLELMNKHDTEMKYyIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd13998     2 VIGKGRFGEVWKA--SLKNEPVAVKIfsSRDKQSWFREKEI---YRTPMLKHENILQF-IAADERDTALRTELWLVTAFH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SY-NLYDLLRNTNFRGVSLnltRKFAQQMCTALLFLAT-------PELSIIHCDLKPENILLCNPKRSAikIVDFGSSCQ 304
Cdd:cd13998    76 PNgSL*DYLSLHTIDWVSL---CRLALSVARGLAHLHSeipgctqGKPAIAHRDLKSKNILVKNDGTCC--IADFGLAVR 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 305 LGQRIYQ-------YIQSRFYRSPEVLLG------MPYDLAIDMWSLGCILVEM 345
Cdd:cd13998   151 LSPSTGEednanngQVGTKRYMAPEVLEGainlrdFESFKRVDIYAMGLVLWEM 204
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
156-389 1.47e-08

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 57.33  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLE--LMNKHDTEmkyYIVHLKRHFMFRNHLCLVFE--- 230
Cdd:cd05626     9 LGIGAFGEVCLACKVDTHALYAMKTLR-KKDVLNRNQVAHVKAErdILAEADNE---WVVKLYYSFQDKDNLYFVMDyip 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 ---MLSYnlydLLRNTNFRGVslnLTRKFAQQMCTALLflATPELSIIHCDLKPENILLcnPKRSAIKIVDFG------- 300
Cdd:cd05626    85 ggdMMSL----LIRMEVFPEV---LARFYIAELTLAIE--SVHKMGFIHRDIKPDNILI--DLDGHIKLTDFGlctgfrw 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 ---------------------------SSCQLGQRI----------------YQYIQSRFYRSPEVLLGMPYDLAIDMWS 337
Cdd:cd05626   154 thnskyyqkgshirqdsmepsdlwddvSNCRCGDRLktleqratkqhqrclaHSLVGTPNYIAPEVLLRKGYTQLCDWWS 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 338 LGCILVEMHTGEPLFSGANEVDQMNKIV---EVLGIPPAHILdqAPKARKFFEKL 389
Cdd:cd05626   234 VGVILFEMLVGQPPFLAPTPTETQLKVInweNTLHIPPQVKL--SPEAVDLITKL 286
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
224-358 1.67e-08

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: 56.21  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLS-YNLYDLLrntnFRGVSLNLT--RKFAQQMCTALLFLATpeLSIIHCDLKPENILL-CNPKRSAIKIVDF 299
Cdd:cd14012    78 KVYLLTEYAPgGSLSELL----DSVGSVPLDtaRRWTLQLLEALEYLHR--NGVVHKSLHAGNVLLdRDAGTGIVKLTDY 151
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 300 GSS----CQLGQRIYQYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPL---FSGANEV 358
Cdd:cd14012   152 SLGktllDMCSRGSLDEFKQTYWLPPELAQGsKSPTRKTDVWDLGLLFLQMLFGLDVlekYTSPNPV 218
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
150-302 1.87e-08

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 56.60  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYD---RVEQEWVAIKIikNKKAFLNQAQIEVRLLELMNKHDTE---MKYYIVHLkrhfmFRN 223
Cdd:cd13981     2 YVISKELGEGGYASVYLAKDddeQSDGSLVALKV--EKPPSIWEFYICDQLHSRLKNSRLResiSGAHSAHL-----FQD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY----NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNPKRS------- 292
Cdd:cd13981    75 ESILVMDYSSQgtllDVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVG--IIHGDIKPDNFLLRLEICAdwpgege 152
                         170
                  ....*....|....*.
gi 1113820495 293 ------AIKIVDFGSS 302
Cdd:cd13981   153 ngwlskGLKLIDFGRS 168
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
147-389 1.89e-08

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: 56.35  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIdSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnkkafLNQAQIEVRLLELMN-KHDTEMKYYIVHLKRHFMF---- 221
Cdd:cd14047     6 QDFKEI-ELIGSGGFGQVFKAKHRIDGKTYAIKRVK-----LNNEKAEREVKALAKlDHPNIVRYNGCWDGFDYDPetss 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 ----RNHL-CLVFEML---SYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILLCNPKRsa 293
Cdd:cd14047    80 snssRSKTkCLFIQMEfceKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKL--IHRDLKPSNIFLVDTGK-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 IKIVDFGSSCQL---GQRIYQYiQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMhtgeplFSGANEVDQMNKIVEVL-- 368
Cdd:cd14047   156 VKIGDFGLVTSLkndGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFEL------LHVCDSAFEKSKFWTDLrn 228
                         250       260
                  ....*....|....*....|.
gi 1113820495 369 GIPPAHILDQAPKARKFFEKL 389
Cdd:cd14047   229 GILPDIFDKRYKIEKTIIKKM 249
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
254-385 1.94e-08

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: 56.29  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 254 RKFAQQMCTALLFLAtpELSIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRS---------PEVL 324
Cdd:cd06631   106 CRYTKQILEGVAYLH--NNNVIHRDIKGNNIMLM--PNGVIKLIDFGCAKRLCINLSSGSQSQLLKSmrgtpywmaPEVI 181
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 325 LGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKF 385
Cdd:cd06631   182 NETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLPDKFSPEARDF 242
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
156-348 2.18e-08

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: 56.08  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKI------IKNKKAFLNQAQIEVRLlelmnKHDTEMKYYIVHLKRHFMFRNHLCLVF 229
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKScrlelsVKNKDRWCHEIQIMKKL-----NHPNVVKACDVPEEMNFLVNDVPLLAM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSY-NLYDLL-RNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL--CNPKrSAIKIVDFGSSCQL 305
Cdd:cd14039    76 EYCSGgDLRKLLnKPENCCGLKESQVLSLLSDIGSGIQYLH--ENKIIHRDLKPENIVLqeINGK-IVHKIIDLGYAKDL 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 306 --GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd14039   153 dqGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAG 197
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
193-381 2.23e-08

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 56.18  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 193 IEVRLLELMNKHDTEMKYYIV-----HLK--RHFMF----------RNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRK 255
Cdd:cd14011    29 FEKKQLEEYSKRDREQILELLkrgvkQLTrlRHPRIltvqhpleesRESLAFATEPVFASLANVLGERDNMPSPPPELQD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 256 FA----------QQMCTALLFLATpELSIIHCDLKPENILLcNpKRSAIKIVDFGSSCQLGQRIYQYIQSRFYR------ 319
Cdd:cd14011   109 YKlydveikyglLQISEALSFLHN-DVKLVHGNICPESVVI-N-SNGEWKLAGFDFCISSEQATDQFPYFREYDpnlppl 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 320 --------SPEVLLGMPYDLAIDMWSLGCILVEMH-TGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPK 381
Cdd:cd14011   186 aqpnlnylAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSYKKNSNQLRQLSLSLLEKVPE 256
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
152-395 2.38e-08

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 55.82  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 152 IDSLIGKGSFGQVVKAYdrVEQEWVAIKIIKNK-----KAFLNQAQIEVRLLELMnKHDTEMKYYIVHLKRhfmfrNHLC 226
Cdd:cd14145    10 LEEIIGIGGFGKVYRAI--WIGDEVAVKAARHDpdediSQTIENVRQEAKLFAML-KHPNIIALRGVCLKE-----PNLC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNlyDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPEL-SIIHCDLKPENILLC------NPKRSAIKIVDF 299
Cdd:cd14145    82 LVMEFARGG--PLNRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIvPVIHRDLKSSNILILekvengDLSNKILKITDF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 GSSCQLGQRIYQYIQSRF-YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVD-----QMNKivevLGIPpa 373
Cdd:cd14145   160 GLAREWHRTTKMSAAGTYaWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAvaygvAMNK----LSLP-- 233
                         250       260
                  ....*....|....*....|..
gi 1113820495 374 hILDQAPKArkfFEKLPDGTWN 395
Cdd:cd14145   234 -IPSTCPEP---FARLMEDCWN 251
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
156-365 3.22e-08

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: 56.04  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRLLELMNKHDTEMKY--YIVHLKRHFMFRNHLCLVFEMLS 233
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVL-SKKVIVAKKEVAHTIGERNILVRTALDEspFIVGLKFSFQTPTDLYLVTDYMS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YN--LYDLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFG-SSCQLGQRIY 310
Cdd:cd05586    80 GGelFWHLQKEGRF---SEDRAKFYIAELVLALEHLH--KNDIVYRDLKPENILL--DANGHIALCDFGlSKADLTDNKT 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 311 --QYIQSRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTG-EPLFsgANEVDQMNKIV 365
Cdd:cd05586   153 tnTFCGTTEYLAPEVLLDeKGYTKMVDFWSLGVLVFEMCCGwSPFY--AEDTQQMYRNI 209
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
148-352 3.29e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 55.81  E-value: 3.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEI-DSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNkkafLNQAQIEVRLLELMNKHDTEMKYYIVHLKrhfMFRNHLC 226
Cdd:cd14170     1 DDYKVtSQVLGLGINGKVLQIFNKRTQEKFALKMLQD----CPKARREVELHWRASQCPHIVRIVDVYEN---LYAGRKC 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCT---ALLFLATpeLSIIHCDLKPENILLCNPKRSAI-KIVDFG-- 300
Cdd:cd14170    74 LLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSigeAIQYLHS--INIAHRDVKPENLLYTSKRPNAIlKLTDFGfa 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 301 ----SSCQLGQRIYqyiqSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14170   152 kettSHNSLTTPCY----TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPF 203
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
156-384 3.56e-08

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 55.41  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAydrveqEW---VAIKIIKNKKAFLNQAQIEVRLLELMNKhdteMKYYIVHLKRHFMFRNHLCLVFEML 232
Cdd:cd14150     8 IGTGSFGTVFRG------KWhgdVAVKILKVTEPTPEQLQAFKNEMQVLRK----TRHVNILLFMGFMTRPNFAIITQWC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 S-YNLYDLLR--NTNFRGVSL-NLTRKFAQQMCtallFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFG-----SSC 303
Cdd:cd14150    78 EgSSLYRHLHvtETRFDTMQLiDVARQTAQGMD----YLHAK--NIIHRDLKSNNIFL--HEGLTVKIGDFGlatvkTRW 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 QLGQRIYQYIQSRFYRSPEVLLGM---PYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPP--AHILDQ 378
Cdd:cd14150   150 SGSQQVEQPSGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYLSPdlSKLSSN 229

                  ....*.
gi 1113820495 379 APKARK 384
Cdd:cd14150   230 CPKAMK 235
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
148-372 3.97e-08

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 55.79  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRLLE--LMNKHDTEmkyYIVHLKRHFMFRNHL 225
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTL-RKKDVLKRNQVAHVKAErdILAEADNE---WVVKLYYSFQDKENL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEmlsynlY----DLLrntnfrgvSLnLTRK--FAQ---QMCTALLFLATP---ELSIIHCDLKPENILLcnPKRSA 293
Cdd:cd05598    77 YFVMD------YipggDLM--------SL-LIKKgiFEEdlaRFYIAELVCAIEsvhKMGFIHRDIKPDNILI--DRDGH 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 294 IKIVDFGsSCQlGQRIYQyiQSRFYR-----------SPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMN 362
Cdd:cd05598   140 IKLTDFG-LCT-GFRWTH--DSKYYLahslvgtpnyiAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQL 215
                         250
                  ....*....|...
gi 1113820495 363 KIV---EVLGIPP 372
Cdd:cd05598   216 KVInwrTTLKIPH 228
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
148-352 4.02e-08

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 55.03  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK--IIKNKKAFLNQAQIEVRLLELMNKHDtemkyyIVHLKRHFMFRNHL 225
Cdd:cd14088     1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkfLKRDGRKVRKAAKNEINILKMVKHPN------ILQLVDVFETRKEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLS-YNLYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNP-KRSAIKIVDFGSSC 303
Cdd:cd14088    75 FIFLELATgREVFDWILDQGY--YSERDTSNVIRQVLEAVAYLHS--LKIVHRNLKLENLVYYNRlKNSKIVISDFHLAK 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1113820495 304 QLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14088   151 LENGLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPF 199
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
151-349 4.22e-08

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 55.01  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVkaYDRVEQEwVAIKIIKNKKAflNQAQIEVRLLELMNKHDTEMKYYIVHLKRhFMFRNHLCLVFE 230
Cdd:cd14153     3 EIGELIGKGRFGQVY--HGRWHGE-VAIRLIDIERD--NEEQLKAFKREVMAYRQTRHENVVLFMGA-CMSPPHLAIITS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLS-YNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKrsaIKIVDFG-----SSCQ 304
Cdd:cd14153    77 LCKgRTLYSVVRDAKVV-LDVNKTRQIAQEIVKGMGYLHAK--GILHKDLKSKNVFYDNGK---VVITDFGlftisGVLQ 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 305 LGQRIYQY-IQSRF--YRSPEVLL---------GMPYDLAIDMWSLGCILVEMHTGE 349
Cdd:cd14153   151 AGRREDKLrIQSGWlcHLAPEIIRqlspeteedKLPFSKHSDVFAFGTIWYELHARE 207
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
156-459 4.40e-08

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


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 55.06  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRLLELMNKHDTEMK------YY--IVHLKR--HFMF---- 221
Cdd:cd14118     2 IGKGSYGIVKLAYNEEDNTLYAMKIL-SKKKLLKQAGFFRRPPPRRKPGALGKPldpldrVYreIAILKKldHPNVvklv 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 -------RNHLCLVFEMLsyNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNPKRsaI 294
Cdd:cd14118    81 evlddpnEDNLYMVFELV--DKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQK--IIHRDIKPSNLLLGDDGH--V 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 295 KIVDFGSSCQL---GQRIYQYIQSRFYRSPEVLLGMPYDL---AIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV-EV 367
Cdd:cd14118   155 KIADFGVSNEFegdDALLSSTAGTPAFMAPEALSESRKKFsgkALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKtDP 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 368 LGIPPAHILDqapkarkffEKLpdgtwnlkktkdgkreykppgtrklhnilgvetggpggrragesghtvadylkfKDLI 447
Cdd:cd14118   235 VVFPDDPVVS---------EQL------------------------------------------------------KDLI 251
                         330
                  ....*....|..
gi 1113820495 448 LRMLDYDPKTRI 459
Cdd:cd14118   252 LRMLDKNPSERI 263
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
156-407 4.44e-08

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 55.82  E-value: 4.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRL-LELMNKHDTEmkyYIVHLKRHFMFRNHLCLVFEMLSY 234
Cdd:cd05625     9 LGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAeRDILAEADNE---WVVRLYYSFQDKDNLYFVMDYIPG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NlyDLLRNTNFRGV-SLNLTRKFAQQMCTALLflATPELSIIHCDLKPENILLcnPKRSAIKIVDFG------------- 300
Cdd:cd05625    86 G--DMMSLLIRMGVfPEDLARFYIAELTCAVE--SVHKMGFIHRDIKPDNILI--DRDGHIKLTDFGlctgfrwthdsky 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 ---------------------SSCQLGQRI----------------YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILV 343
Cdd:cd05625   160 yqsgdhlrqdsmdfsnewgdpENCRCGDRLkplerraarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILF 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 344 EMHTGEPLFSGANEVDQMNKIVE---VLGIPPAHILdqAPKARKFFEKLPDGTWNlKKTKDGKREYK 407
Cdd:cd05625   240 EMLVGQPPFLAQTPLETQMKVINwqtSLHIPPQAKL--SPEASDLIIKLCRGPED-RLGKNGADEIK 303
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
151-373 5.10e-08

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 55.06  E-value: 5.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAYDR---VEQEWVAIKIIKNKKAFLNQAQIEVRLLELMnKHDTEMKYYIvHLKRHFMFRNHLCL 227
Cdd:cd14030    28 KFDIEIGRGSFKTVYKGLDTettVEVAWCELQDRKLSKSERQRFKEEAGMLKGL-QHPNIVRFYD-SWESTVKGKKCIVL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFE-MLSYNLYDLLRNtnFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSaIKIVDFG-SSCQL 305
Cdd:cd14030   106 VTElMTSGTLKTYLKR--FKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPTGS-VKIGDLGlATLKR 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 306 GQRIYQYIQSRFYRSPEvLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVeVLGIPPA 373
Cdd:cd14030   183 ASFAKSVIGTPEFMAPE-MYEEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRRV-TSGVKPA 248
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
150-366 5.47e-08

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 55.42  E-value: 5.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVV----KAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDtemkyYIVHLKRHFMFRNHL 225
Cdd:cd05618    22 FDLLRVIGRGSYAKVLlvrlKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHP-----FLVGLHSCFQTESRL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLsyNLYDLLRNTNF-RGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSsCQ 304
Cdd:cd05618    97 FFVIEYV--NGGDLMFHMQRqRKLPEEHARFYSAEISLALNYLH--ERGIIYRDLKLDNVLL--DSEGHIKLTDYGM-CK 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 305 LGQR----IYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd05618   170 EGLRpgdtTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTE 235
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
225-347 5.57e-08

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 55.10  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSYNLYDLLRNTNFRGVS---LNLTRKFAQQMCTALLFLATpELSIIHCDLKPENILLCNPKRSaIKIVDFGS 301
Cdd:cd14001    81 LCLAMEYGGKSLNDLIEERYEAGLGpfpAATILKVALSIARALEYLHN-EKKILHGDIKSGNVLIKGDFES-VKLCDFGV 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 302 SCQLGQRIY-------QYIQSRFYRSPEVLL-GMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd14001   159 SLPLTENLEvdsdpkaQYVGTEPWKAKEALEeGGVITDKADIFAYGLVLWEMMT 212
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
140-377 6.14e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 55.86  E-value: 6.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 140 VKNGEKWMDRYEIDSLIGKGSFGQV----VKAYDRVEQ---------------EWVAIKIIKNKKAFLNQAQIEVRLLEL 200
Cdd:PHA03210  140 LKHDDEFLAHFRVIDDLPAGAFGKIficaLRASTEEAEarrgvnstnqgkpkcERLIAKRVKAGSRAAIQLENEILALGR 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 201 MNkHDTEMKyyivhLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVS---LNLTRKFAQQMCTALLFLATPELsiIHC 277
Cdd:PHA03210  220 LN-HENILK-----IEEILRSEANTYMITQKYDFDLYSFMYDEAFDWKDrplLKQTRAIMKQLLCAVEYIHDKKL--IHR 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 278 DLKPENILL-CNPKrsaIKIVDFGSSCQLGQ----RIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGE--P 350
Cdd:PHA03210  292 DIKLENIFLnCDGK---IVLGDFGTAMPFEKereaFDYGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDfcP 368
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1113820495 351 LF-SGANEVDQMNKIVEVLGI-------PPAHILD 377
Cdd:PHA03210  369 IGdGGGKPGKQLLKIIDSLSVcdeefpdPPCKLFD 403
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
152-384 7.83e-08

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 54.65  E-value: 7.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 152 IDSLIGKGSFGQVVKAydrveqEW---VAIKIIKNKKAFLNQAQIEVRLLELMNKhdteMKYYIVHLKRHFMFRNHLCLV 228
Cdd:cd14149    16 LSTRIGSGSFGTVYKG------KWhgdVAVKILKVVDPTPEQFQAFRNEVAVLRK----TRHVNILLFMGYMTKDNLAIV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEM-----LSYNLYdlLRNTNFRGVSL-NLTRKFAQQMCtallFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFG-- 300
Cdd:cd14149    86 TQWcegssLYKHLH--VQETKFQMFQLiDIARQTAQGMD----YLHAK--NIIHRDMKSNNIFL--HEGLTVKIGDFGla 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 301 ---SSCQLGQRIYQYIQSRFYRSPEVLL---GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPP-- 372
Cdd:cd14149   156 tvkSRWSGSQQVEQPTGSILWMAPEVIRmqdNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPdl 235
                         250
                  ....*....|..
gi 1113820495 373 AHILDQAPKARK 384
Cdd:cd14149   236 SKLYKNCPKAMK 247
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
150-358 8.57e-08

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 54.21  E-value: 8.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKA-----FLNQAQIEVRLLeLMNKHDTEMKYyIVHLKRHFMFRNH 224
Cdd:cd14100     2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVsewgeLPNGTRVPMEIV-LLKKVGSGFRG-VIRLLDWFERPDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEM--LSYNLYDLLrnTNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcNPKRSAIKIVDFGSS 302
Cdd:cd14100    80 FVLVLERpePVQDLFDFI--TERGALPEELARSFFRQVLEAVRHCHN--CGVLHRDIKDENILI-DLNTGELKLIDFGSG 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 303 CQLGQRIY-QYIQSRFYRSPEVLLGMPYD-LAIDMWSLGCILVEMHTGEPLFSGANEV 358
Cdd:cd14100   155 ALLKDTVYtDFDGTRVYSPPEWIRFHRYHgRSAAVWSLGILLYDMVCGDIPFEHDEEI 212
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
147-352 9.57e-08

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: 54.17  E-value: 9.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLELmNKHDTEMKYYIVHLKRHFMFRNHLC 226
Cdd:cd14187     6 RRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVP-KSLLLKPHQKEKMSMEI-AIHRSLAHQHVVGFHGFFEDNDFVY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPElsIIHCDLKPENILLCNPKRsaIKIVDFGSSCQL 305
Cdd:cd14187    84 VVLELCRRrSLLELHKRR--KALTEPEARYYLRQIILGCQYLHRNR--VIHRDLKLGNLFLNDDME--VKIGDFGLATKV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1113820495 306 ---GQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14187   158 eydGERKKTLCGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPF 207
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
148-389 9.84e-08

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: 54.30  E-value: 9.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAydrveqEW-----VAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVhlkrh 218
Cdd:cd05070     9 ESLQLIKRLGNGQFGEVWMG------TWngntkVAIKTLKpgtmSPESFLEEAQIMKKL-----KHDKLVQLYAV----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 fMFRNHLCLVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKrsAIKIV 297
Cdd:cd05070    73 -VSEEPIYIVTEYMSKgSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIE--RMNYIHRDLRSANILVGNGL--ICKIA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 298 DFGSSCQLGQRIYQYIQ-SRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGANEVDQMNKIVEVLGIP- 371
Cdd:cd05070   148 DFGLARLIEDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGYRMPc 227
                         250       260
                  ....*....|....*....|....*....
gi 1113820495 372 PA-----------HILDQAPKARKFFEKL 389
Cdd:cd05070   228 PQdcpislhelmiHCWKKDPEERPTFEYL 256
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
147-372 1.13e-07

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 54.68  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRL-LELMNKHDTEmkyYIVHLKRHFMFRNHL 225
Cdd:cd05627     1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAeRDILVEADGA---WVVKMFYSFQDKRNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEML-SYNLYDLLRNTNfrGVSLNLTRKFAQQmcTALLFLATPELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ 304
Cdd:cd05627    78 YLIMEFLpGGDMMTLLMKKD--TLSEEATQFYIAE--TVLAIDAIHQLGFIHRDIKPDNLLL--DAKGHVKLSDFGLCTG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 LG--------------------------------------QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMH 346
Cdd:cd05627   152 LKkahrtefyrnlthnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEML 231
                         250       260
                  ....*....|....*....|....*....
gi 1113820495 347 TGEPLFSGANEVDQMNKIV---EVLGIPP 372
Cdd:cd05627   232 IGYPPFCSETPQETYRKVMnwkETLVFPP 260
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
150-372 1.28e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 54.50  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIiKNKKAFLnqaqIEVRLLELMNkHDTEMKyyivhLKRHFMFRNHLCLVF 229
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKI-GQKGTTL----IEAMLLQNVN-HPSVIR-----MKDTLVSGAITCMVL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNLYDLLRNtNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSScqlgqrI 309
Cdd:PHA03209  137 PHYSSDLYTYLTK-RSRPLPIDQALIIEKQILEGLRYLH--AQRIIHRDVKTENIFI--NDVDQVCIGDLGAA------Q 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 310 YQYIQSRFY--------RSPEVLLGMPYDLAIDMWSLGCILVEM----HT---------GEPLFSGANevdQMNKIVEVL 368
Cdd:PHA03209  206 FPVVAPAFLglagtvetNAPEVLARDKYNSKADIWSAGIVLFEMlaypSTifedppstpEEYVKSCHS---HLLKIISTL 282

                  ....
gi 1113820495 369 GIPP 372
Cdd:PHA03209  283 KVHP 286
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
147-389 1.30e-07

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 53.45  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSLIGKGSFGQVVKAYDRVEQewVAIKIIKNK---KAFLNQAQIEVRLlelmnKHDTEMKYYIVHLKRhfmfRN 223
Cdd:cd05082     5 MKELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCIKNDataQAFLAEASVMTQL-----RHSNLVQLLGVIVEE----KG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFE-MLSYNLYDLLRNtnfRGVSL---NLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd05082    74 GLYIVTEyMAKGSLVDYLRS---RGRSVlggDCLLKFSLDVCEAMEYLEGN--NFVHRDLAARNVLV--SEDNVAKVSDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 300 G-----SSCQLGQRIyqyiqSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHT-GE------PLFSGANEVDQMNKIVEV 367
Cdd:cd05082   147 GltkeaSSTQDTGKL-----PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRvpypriPLKDVVPRVEKGYKMDAP 221
                         250       260
                  ....*....|....*....|....*...
gi 1113820495 368 LGIPPA--HILDQA----PKARKFFEKL 389
Cdd:cd05082   222 DGCPPAvyDVMKNCwhldAAMRPSFLQL 249
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
150-389 1.45e-07

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 54.15  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVV---KAYDRVEQEWVAIKIIKnKKAFLNQAQI------EVRLLELMNKHDtemkyYIVHLkrHFM 220
Cdd:cd05614     2 FELLKVLGTGAYGKVFlvrKVSGHDANKLYAMKVLR-KAALVQKAKTvehtrtERNVLEHVRQSP-----FLVTL--HYA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FRN----HLCLVF----EMLSYnlydLLRNTNFrgvSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRS 292
Cdd:cd05614    74 FQTdaklHLILDYvsggELFTH----LYQRDHF---SEDEVRFYSGEIILALEHLH--KLGIVYRDIKLENILL--DSEG 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 293 AIKIVDFGSSCQL----GQRIYQYIQSRFYRSPEVLLGMP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE- 366
Cdd:cd05614   143 HVVLTDFGLSKEFlteeKERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEVSRr 222
                         250       260
                  ....*....|....*....|...
gi 1113820495 367 VLGIPPAHILDQAPKARKFFEKL 389
Cdd:cd05614   223 ILKCDPPFPSFIGPVARDLLQKL 245
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
149-345 1.92e-07

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 53.71  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK-----------------------------IIKNKKAFLNQAQIEVRLLE 199
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKkircnapenvelalrefwalssiqrqhpnVIQLEECVLQRDGLAQRMSH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 200 LMNKHDTEMKYYIVHLK--RHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPElsIIHC 277
Cdd:cd13977    81 GSSKSDLYLLLVETSLKgeRCFDPRSACYLWFVMEFCDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQ--IVHR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 278 DLKPENILLCNPKRSAI-KIVDFGSS--CQ-LGQRIYQYIQ-----------SRFYRSPEVLLGMpYDLAIDMWSLGCIL 342
Cdd:cd13977   159 DLKPDNILISHKRGEPIlKVADFGLSkvCSgSGLNPEEPANvnkhflssacgSDFYMAPEVWEGH-YTAKADIFALGIII 237

                  ...
gi 1113820495 343 VEM 345
Cdd:cd13977   238 WAM 240
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
271-398 2.25e-07

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: 53.08  E-value: 2.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 271 ELSIIHCDLKPENILLcnPKRSAIKIVDFGSS----CQLGQRIYQYIQSRFYRSPEVLLG--MPYDLAIDMWSLGCILVE 344
Cdd:cd05613   123 KLGIIYRDIKLENILL--DSSGHVVLTDFGLSkeflLDENERAYSFCGTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYE 200
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 345 MHTGEPLFSGANEVDQMNKIVE-VLGIPPAHILDQAPKARKFFEKL------------PDGTWNLKK 398
Cdd:cd05613   201 LLTGASPFTVDGEKNSQAEISRrILKSEPPYPQEMSALAKDIIQRLlmkdpkkrlgcgPNGADEIKK 267
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
226-357 2.31e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 54.13  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLrNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRsaIKIVDFGSSCQL 305
Cdd:PHA03211  236 CLVLPKYRSDLYTYL-GARLRPLGLAQVTAVARQLLSAIDYIHGE--GIIHRDIKTENVLVNGPED--ICLGDFGAACFA 310
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 306 -GQRiyqyiQSRFY---------RSPEVLLGMPYDLAIDMWSLGCILVE--MHTGEpLFSGANE 357
Cdd:PHA03211  311 rGSW-----STPFHygiagtvdtNAPEVLAGDPYTPSVDIWSAGLVIFEaaVHTAS-LFSASRG 368
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
156-348 2.40e-07

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 52.84  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEwVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVHLKRhfmfrNHLCLVFEM 231
Cdd:cd05059    12 LGSGQFGVVHLGKWRGKID-VAIKMIKegsmSEDDFIEEAKVMMKL-----SHPKLVQLYGVCTKQ-----RPIFIVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYN-LYDLLRNTNFRGVSLNLTrKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSScqlgqRIY 310
Cdd:cd05059    81 MANGcLLNYLRERRGKFQTEQLL-EMCKDVCEAMEYLE--SNGFIHRDLAARNCLV--GEQNVVKVSDFGLA-----RYV 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1113820495 311 ---QYIQS---RF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd05059   151 lddEYTSSvgtKFpvkWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSE 197
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
144-347 2.41e-07

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 53.26  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 144 EKW---MDRYEIDSLIGKGSFGQVVKAY-------DRVEQewVAIKIIKnKKAFLNQAQIEVRLLELMNkhdtemkyyiv 213
Cdd:cd05055    28 LKWefpRNNLSFGKTLGAGAFGKVVEATayglsksDAVMK--VAVKMLK-PTAHSSEREALMSELKIMS----------- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 214 HLKRHFMFRNHL--C-------LVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPEN 283
Cdd:cd05055    94 HLGNHENIVNLLgaCtiggpilVITEYCCYgDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASK--NCIHRDLAARN 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 284 ILLCNPKrsAIKIVDFGsscqLGQRIYQ---YI---QSRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05055   172 VLLTHGK--IVKICDFG----LARDIMNdsnYVvkgNARLpvkWMAPESIFNCVYTFESDVWSYGILLWEIFS 238
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
149-357 2.52e-07

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 52.91  E-value: 2.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDslIGKGSFGQVVKAY------DRvEQEWVAIKIIKNKKAFLNQAQIEvRLLELMNKHDTEmkyYIVHLKRHFMFR 222
Cdd:cd05050     8 EYVRD--IGQGAFGRVFQARapgllpYE-PFTMVAVKMLKEEASADMQADFQ-REAALMAEFDHP---NIVKLLGVCAVG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFEMLSY-NLYDLLRNTNFRGVS------------------LNLTRKF--AQQMCTALLFLAtpELSIIHCDLKP 281
Cdd:cd05050    81 KPMCLLFEYMAYgDLNEFLRHRSPRAQCslshstssarkcglnplpLSCTEQLciAKQVAAGMAYLS--ERKFVHRDLAT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 282 ENILLcnPKRSAIKIVDFGsscqLGQRIYqyiQSRFYRS------------PEVLLGMPYDLAIDMWSLGCILVEMHTG- 348
Cdd:cd05050   159 RNCLV--GENMVVKIADFG----LSRNIY---SADYYKAsendaipirwmpPESIFYNRYTTESDVWAYGVVLWEIFSYg 229
                         250
                  ....*....|
gi 1113820495 349 -EPLFSGANE 357
Cdd:cd05050   230 mQPYYGMAHE 239
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
149-329 3.20e-07

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 52.50  E-value: 3.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiIKNKKAFLNQAQIEVRLLELMNK-HDTEMKYYIVHLKRHFMfrnhlcL 227
Cdd:cd14127     1 HYKVGKKIGEGSFGVIFEGTNLLNGQQVAIK-FEPRKSDAPQLRDEYRTYKLLAGcPGIPNVYYFGQEGLHNI------L 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLSYNLYDLLRNTNfRGVSLNLTRKFAQQMCTalLFLATPELSIIHCDLKPENILLCNPKRSA---IKIVDFGsscq 304
Cdd:cd14127    74 VIDLLGPSLEDLFDLCG-RKFSVKTVVMVAKQMLT--RVQTIHEKNLIYRDIKPDNFLIGRPGTKNanvIHVVDFG---- 146
                         170       180
                  ....*....|....*....|....*
gi 1113820495 305 lgqriyqyiQSRFYRSPEVLLGMPY 329
Cdd:cd14127   147 ---------MAKQYRDPKTKQHIPY 162
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
155-385 3.21e-07

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: 52.24  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRVEQEWVAIKIIKNKK-AFLNQAQIEVRLLELmnkHDTEMKYYIVHLKRHFMFRNHLCLVFEMLS 233
Cdd:cd14189     8 LLGKGGFARCYEMTDLATNKTYAVKVIPHSRvAKPHQREKIVNEIEL---HRDLHHKHVVKFSHHFEDAENIYIFLELCS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNlyDLLRNTNFRGVSLN-LTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLG---QRI 309
Cdd:cd14189    85 RK--SLAHIWKARHTLLEpEVRYYLKQIISGLKYLHLK--GILHRDLKLGNFFI--NENMELKVGDFGLAARLEppeQRK 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1113820495 310 YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHIldqAPKARKF 385
Cdd:cd14189   159 KTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASL---SLPARHL 231
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
156-361 3.24e-07

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


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 52.40  E-value: 3.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYdrveqeW---VAIKIIKNK-------KAFLNqaqiEVRLLElMNKHDTemkyyiVHLKRHFMFRNHL 225
Cdd:cd14062     1 IGSGSFGTVYKGR------WhgdVAVKKLNVTdptpsqlQAFKN----EVAVLR-KTRHVN------ILLFMGYMTKPQL 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLS-YNLYDLLR--NTNFRGVSL-NLTRKFAQQMCtallFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFG- 300
Cdd:cd14062    64 AIVTQWCEgSSLYKHLHvlETKFEMLQLiDIARQTAQGMD----YLHAK--NIIHRDLKSNNIFL--HEDLTVKIGDFGl 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 301 -------SSCQLGQriyQYIQSRFYRSPEVLL---GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQM 361
Cdd:cd14062   136 atvktrwSGSQQFE---QPTGSILWMAPEVIRmqdENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQI 203
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
151-358 3.56e-07

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 52.28  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKAydrveqEW---VAIKIIKNKKAflNQAQIEVRLLELMNKHDTEMKYYIVHLKRhFMFRNHLCL 227
Cdd:cd14152     3 ELGELIGQGRWGKVHRG------RWhgeVAIRLLEIDGN--NQDHLKLFKKEVMNYRQTRHENVVLFMGA-CMHPPHLAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEMLS-YNLYDLLRNTNFrGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKrsaIKIVDFG-----S 301
Cdd:cd14152    74 ITSFCKgRTLYSFVRDPKT-SLDINKTRQIAQEIIKGMGYLHAK--GIVHKDLKSKNVFYDNGK---VVITDFGlfgisG 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 302 SCQLGQRIYQYIQSR---FYRSPEVLLGM---------PYDLAIDMWSLGCILVEMHTGE-PLFSGANEV 358
Cdd:cd14152   148 VVQEGRRENELKLPHdwlCYLAPEIVREMtpgkdedclPFSKAADVYAFGTIWYELQARDwPLKNQPAEA 217
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
149-300 4.19e-07

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. TTBK1 has been linked to Alzheimer's disease (AD) while TTBK2 is associated with spinocerebellar ataxia type 11 (SCA11). Both AD and SCA11 patients show the presence of neurofibrillary tangles in the brain. The Drosophila TTBK homolog, Asator, is an essential protein that localizes to the mitotic spindle during mitosis and may be involved in regulating microtubule dynamics and function. The TTBK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 51.87  E-value: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIK---------IIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVhlkrhf 219
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKvesksqpkqVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIV------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 220 MfrnhlclvfEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILL-CNP-KRSAIKIV 297
Cdd:cd14017    75 M---------TLLGPNLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIH--EVGFLHRDVKPSNFAIgRGPsDERTVYIL 143

                  ...
gi 1113820495 298 DFG 300
Cdd:cd14017   144 DFG 146
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
156-345 5.23e-07

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 51.75  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKkafLNQAQIeVRLLELMNK--HDTEMKYYIVHLKRhfmfrNHLCLVFEMLS 233
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKND---VDQHKI-VREISLLQKlsHPNIVRYLGICVKD-----EKLHPILEYVS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YN-LYDLLRNTNfrgVSLNLTRK--FAQQMCTALLFLATPelSIIHCDLKPENILL-CNPK-RSAIkIVDFGSSCQLG-- 306
Cdd:cd14156    72 GGcLEELLAREE---LPLSWREKveLACDISRGMVYLHSK--NIYHRDLNSKNCLIrVTPRgREAV-VTDFGLAREVGem 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1113820495 307 -----QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd14156   146 pandpERKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEI 189
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
148-347 6.32e-07

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 51.64  E-value: 6.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEID-------SLIGKGSFGQVVkaydrvEQEW-----VAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYY 211
Cdd:cd05068     1 DQWEIDrkslkllRKLGSGQFGEVW------EGLWnnttpVAVKTLKpgtmDPEDFLREAQIMKKL-----RHPKLIQLY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 212 IVHLKRHFMFrnhlcLVFEMLSY-NLYDLLRNtnfRGVSLNLTR--KFAQQMCTALLFLATPelSIIHCDLKPENILLCN 288
Cdd:cd05068    70 AVCTLEEPIY-----IITELMKHgSLLEYLQG---KGRSLQLPQliDMAAQVASGMAYLESQ--NYIHRDLAARNVLVGE 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 289 pkRSAIKIVDFGSSCQLGQR-IYQ-YIQSRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05068   140 --NNICKVADFGLARVIKVEdEYEaREGAKFpikWTAPEAANYNRFSIKSDVWSFGILLTEIVT 201
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
148-350 1.11e-06

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 50.88  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKA------YDRVEQEWVAIKIIK---NKKAFLNQAQiEVRLLELMNKHDTEMK--------- 209
Cdd:cd05053    12 DRLTLGKPLGEGAFGQVVKAeavgldNKPNEVVTVAVKMLKddaTEKDLSDLVS-EMEMMKMIGKHKNIINllgactqdg 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 210 --YYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTnfrgvSLNLTRK----FAQQMCTALLFLATPElsIIHCDLKPEN 283
Cdd:cd05053    91 plYVVVEYASKGNLREFLRARRPPGEEASPDDPRVP-----EEQLTQKdlvsFAYQVARGMEYLASKK--CIHRDLAARN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 284 ILLCnpKRSAIKIVDFGSScqlgqRIYQYIQsrFYR------------SPEVLLGMPYDLAIDMWSLGCILVEMHT--GE 349
Cdd:cd05053   164 VLVT--EDNVMKIADFGLA-----RDIHHID--YYRkttngrlpvkwmAPEALFDRVYTHQSDVWSFGVLLWEIFTlgGS 234

                  .
gi 1113820495 350 P 350
Cdd:cd05053   235 P 235
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
150-348 1.39e-06

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: 50.56  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQV------VKAYDRVEQEwVAIKIIKNKKafLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRN 223
Cdd:cd14076     3 YILGRTLGEGEFGKVklgwplPKANHRSGVQ-VAIKLIRRDT--QQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEMLSY-NLYDLLRNTnfRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSS 302
Cdd:cd14076    80 YIGIVLEFVSGgELFDYILAR--RRLKDSVACRLFAQLISGVAYLHKK--GVVHRDLKLENLLL--DKNRNLVITDFGFA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 303 CQLGQRIYQYIQ----SRFYRSPE-VLLGMPYD-LAIDMWSLGCILVEMHTG 348
Cdd:cd14076   154 NTFDHFNGDLMStscgSPCYAAPElVVSDSMYAgRKADIWSCGVILYAMLAG 205
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
152-347 1.44e-06

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 50.46  E-value: 1.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 152 IDSLIGKGSFGQV-VKAYDRVEQewVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVhlkrhfMFRNHLC 226
Cdd:cd05069    16 LDVKLGQGCFGEVwMGTWNGTTK--VAIKTLKpgtmMPEAFLQEAQIMKKL-----RHDKLVPLYAV------VSEEPIY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQL 305
Cdd:cd05069    83 IVTEFMGKgSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIE--RMNYIHRDLRAANILVGD--NLVCKIADFGLARLI 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 306 GQRIYQYIQ-SRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05069   159 EDNEYTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELVT 204
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
258-365 1.94e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 51.17  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 258 QQMCTALLF----LATPEL---SIIHCDLKPENILLCnpKRSAIKIVDFGSSCQLGQRIYQYIQSRF-----YRSPEVLL 325
Cdd:PTZ00267  167 QEYEVGLLFyqivLALDEVhsrKMMHRDLKSANIFLM--PTGIIKLGDFGFSKQYSDSVSLDVASSFcgtpyYLAPELWE 244
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1113820495 326 GMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:PTZ00267  245 RKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVL 284
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
156-364 2.09e-06

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 50.04  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRV---EQEWVAIKIIK------NKKAFLNQAQIEVRLlelmnKHDtemkyYIVHL----KRHFMfr 222
Cdd:cd05060     3 LGHGNFGSVRKGVYLMksgKEVEVAVKTLKqehekaGKKEFLREASVMAQL-----DHP-----CIVRLigvcKGEPL-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 nhlCLVFEML---SYNLYdLLRNTNFRGVSLNLtrkFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDF 299
Cdd:cd05060    71 ---MLVMELAplgPLLKY-LKKRREIPVSDLKE---LAHQVAMGMAYLE--SKHFVHRDLAARNVLLVN--RHQAKISDF 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 300 GSSCQL--GQRIYQYIQS-----RFYrSPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGANEVDQMNKI 364
Cdd:cd05060   140 GMSRALgaGSDYYRATTAgrwplKWY-APECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAML 211
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
149-348 2.14e-06

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


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 49.81  E-value: 2.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKiIKNKKAFLNQAQIEVRLLELMNKHDTemkyyIVHLKRHFMFRNHLCLV 228
Cdd:cd14128     1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVK-LESQKARHPQLLYESKLYKILQGGVG-----IPHIRWYGQEKDYNVLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSYNLYDLLrntNF--RGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILL-----CNpkrsAIKIVDFGS 301
Cdd:cd14128    75 MDLLGPSLEDLF---NFcsRRFTMKTVLMLADQMIGRIEYVHNK--NFIHRDIKPDNFLMgigrhCN----KLFLIDFGL 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 302 SCQL-GQRIYQYIQSR---------FYRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd14128   146 AKKYrDSRTRQHIPYRedknltgtaRYASINAHLGIEQSRRDDMESLGYVLMYFNRG 202
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
156-347 2.16e-06

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 49.93  E-value: 2.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQV-VKAYDRVEQ---EWVAIKIIK--NKKAFLNQAQIEVRLLELMnKHDTEMKYYIVHLKRHfmfRNHLCLVF 229
Cdd:cd05079    12 LGEGHFGKVeLCRYDPEGDntgEQVAVKSLKpeSGGNHIADLKKEIEILRNL-YHENIVKYKGICTEDG---GNGIKLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EML-SYNLYDLL-RNTNfrGVSLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILLCNPKRsaIKIVDFG--SSCQL 305
Cdd:cd05079    88 EFLpSGSLKEYLpRNKN--KINLKQQLKYAVQICKGMDYLGSRQY--VHRDLAARNVLVESEHQ--VKIGDFGltKAIET 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1113820495 306 GQRIYQYIQSR----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05079   162 DKEYYTVKDDLdspvFWYAPECLIQSKFYIASDVWSFGVTLYELLT 207
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
148-364 2.30e-06

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: 49.73  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKA-YDRVEQEW--VAIKIIKN------KKAFLNQAQIE--------VRLLELMnkhdTEMKY 210
Cdd:cd05056     6 EDITLGRCIGEGQFGDVYQGvYMSPENEKiaVAVKTCKNctspsvREKFLQEAYIMrqfdhphiVKLIGVI----TENPV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 211 YIVhlkrhfMfrnHLCLVFEMLSYnlydLLRNTNfrgvSLNLTR--KFAQQMCTALLFLATpeLSIIHCDLKPENILLCN 288
Cdd:cd05056    82 WIV------M---ELAPLGELRSY----LQVNKY----SLDLASliLYAYQLSTALAYLES--KRFVHRDIAARNVLVSS 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 289 PKrsAIKIVDFGSSCQLGQRIYqYIQSRF-----YRSPEVLLGMPYDLAIDMWSLG-CILVEMHTGEPLFSGANEVDQMN 362
Cdd:cd05056   143 PD--CVKLGDFGLSRYMEDESY-YKASKGklpikWMAPESINFRRFTSASDVWMFGvCMWEILMLGVKPFQGVKNNDVIG 219

                  ..
gi 1113820495 363 KI 364
Cdd:cd05056   220 RI 221
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
148-365 3.63e-06

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 49.85  E-value: 3.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRL-LELMNKHDTEmkyYIVHLKRHFMFRNHLC 226
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAeRDVLAESDSP---WVVSLYYSFQDAQYLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEML-SYNLYDLLrnTNFRGVSLNLTRKFAQQMCTALLflATPELSIIHCDLKPENILLcnPKRSAIKIVDFGSSC-- 303
Cdd:cd05629    78 LIMEFLpGGDLMTML--IKYDTFSEDVTRFYMAECVLAIE--AVHKLGFIHRDIKPDNILI--DRGGHIKLSDFGLSTgf 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 304 ----------QLGQ------------------------------------RI--YQYIQSRFYRSPEVLLGMPYDLAIDM 335
Cdd:cd05629   152 hkqhdsayyqKLLQgksnknridnrnsvavdsinltmsskdqiatwkknrRLmaYSTVGTPDYIAPEIFLQQGYGQECDW 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 1113820495 336 WSLGCILVEMHTGEPLFSGANEVDQMNKIV 365
Cdd:cd05629   232 WSLGAIMFECLIGWPPFCSENSHETYRKII 261
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
156-348 4.07e-06

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 48.98  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIK------NKKAFLNQAQIevrllelmnkhdteMKYY----IVHLKRHFMFRNHL 225
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVKTCRetlppdLKRKFLQEARI--------------LKQYdhpnIVKLIGVCVQKQPI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFE-MLSYNLYDLLRNTNFRgvslnLTRKFAQQMC----TALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFG 300
Cdd:cd05041    69 MIVMElVPGGSLLTFLRKKGAR-----LTVKQLLQMCldaaAGMEYLESK--NCIHRDLAARNCLV--GENNVLKISDFG 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1113820495 301 SSCQLGQRIYQyIQSRF------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd05041   140 MSREEEDGEYT-VSDGLkqipikWTAPEALNYGRYTSESDVWSFGILLWEIFSL 192
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
150-372 4.16e-06

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 49.65  E-value: 4.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKnKKAFLNQAQI-EVRL-LELMNKHDTemkYYIVHLKRHFMFRNHLCL 227
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKKDTGHVYAMKILR-KADMLEKEQVgHIRAeRDILVEADS---LWVVKMFYSFQDKLNLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 228 VFEML-SYNLYDLLRNTNfrgvslNLTRKFAQQMC--TALLFLATPELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ 304
Cdd:cd05628    79 IMEFLpGGDMMTLLMKKD------TLTEEETQFYIaeTVLAIDSIHQLGFIHRDIKPDNLLL--DSKGHVKLSDFGLCTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 305 LG--------------------------------------QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMH 346
Cdd:cd05628   151 LKkahrtefyrnlnhslpsdftfqnmnskrkaetwkrnrrQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEML 230
                         250       260
                  ....*....|....*....|....*....
gi 1113820495 347 TGEPLFSGANEVDQMNKIV---EVLGIPP 372
Cdd:cd05628   231 IGYPPFCSETPQETYKKVMnwkETLIFPP 259
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
156-364 5.95e-06

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 48.50  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEwVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVHLKRHFMFrnhlcLVFE- 230
Cdd:cd05072    15 LGAGQFGEVWMGYYNNSTK-VAVKTLKpgtmSVQAFLEEANLMKTL-----QHDKLVRLYAVVTKEEPIY-----IITEy 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIY 310
Cdd:cd05072    84 MAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERK--NYIHRDLRAANVLV--SESLMCKIADFGLARVIEDNEY 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 311 QYIQ-SRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGANEVDQMNKI 364
Cdd:cd05072   160 TAREgAKFpikWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSAL 218
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
150-353 6.42e-06

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: 48.40  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 150 YEIDSLIGKGSFGQVVKAYDRvEQEWVaIKIIKNKKAFLNQAQIEVRLLELMNK-----HDTEMKYYIVHLKRHFMFRNH 224
Cdd:cd13980     2 YLYDKSLGSTRFLKVARARHD-EGLVV-VKVFVKPDPALPLRSYKQRLEEIRDRllelpNVLPFQKVIETDKAAYLIRQY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LclvfemlSYNLYDLLRNTNFrgvsLNLT-RKF-AQQMCTALLFLAtpELSIIHCDLKPENILLCnpkrSA--IKIVDFG 300
Cdd:cd13980    80 V-------KYNLYDRISTRPF----LNLIeKKWiAFQLLHALNQCH--KRGVCHGDIKTENVLVT----SWnwVYLTDFA 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 301 SS--CQL---------------GQRIYqYIQ-SRFYrSPEVLLGMPYDL------AIDMWSLGCILVEMHT-GEPLFS 353
Cdd:cd13980   143 SFkpTYLpednpadfsyffdtsRRRTC-YIApERFV-DALTLDAESERRdgeltpAMDIFSLGCVIAELFTeGRPLFD 218
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
147-347 9.52e-06

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 47.95  E-value: 9.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 147 MDRYEIDSL--IGKGSFGqVVKAYDRVEQEWVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVHLKRHFM 220
Cdd:cd05113     1 IDPKDLTFLkeLGTGQFG-VVKYGKWRGQYDVAIKMIKegsmSEDEFIEEAKVMMNL-----SHEKLVQLYGVCTKQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 221 FrnhlcLVFEMLSYN-LYDLLRNTNFRGVSLNLTrKFAQQMCTALLFLATPELsiIHCDLKPENILLcnPKRSAIKIVDF 299
Cdd:cd05113    75 F-----IITEYMANGcLLNYLREMRKRFQTQQLL-EMCKDVCEAMEYLESKQF--LHRDLAARNCLV--NDQGVVKVSDF 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 300 G-SSCQLGQRIYQYIQSRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05113   145 GlSRYVLDDEYTSSVGSKFpvrWSPPEVLMYSKFSSKSDVWAFGVLMWEVYS 196
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
156-347 1.26e-05

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 47.76  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKA-YDRVEQewVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVhlkrhfMFRNHLCLVFE 230
Cdd:cd05071    17 LGQGCFGEVWMGtWNGTTR--VAIKTLKpgtmSPEAFLQEAQVMKKL-----RHEKLVQLYAV------VSEEPIYIVTE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQLGQRI 309
Cdd:cd05071    84 YMSKgSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVE--RMNYVHRDLRAANILVGE--NLVCKVADFGLARLIEDNE 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1113820495 310 YQYIQ-SRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05071   160 YTARQgAKFpikWTAPEAALYGRFTIKSDVWSFGILLTELTT 201
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
156-347 1.32e-05

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 47.56  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAyDRVEQEwVAIKIIK---NKKAFLNQAQIevrLLELMNKHDTEMKYYIVHlkrhfmfrNHLCLVFEML 232
Cdd:cd05083    14 IGEGEFGAVLQG-EYMGQK-VAVKNIKcdvTAQAFLEETAV---MTKLQHKNLVRLLGVILH--------NGLYIVMELM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 233 SY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILLcnPKRSAIKIVDFG-SSCQLGQRIY 310
Cdd:cd05083    81 SKgNLVNFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKL--VHRDLAARNILV--SEDGVAKISDFGlAKVGSMGVDN 156
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1113820495 311 QYIQSRfYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05083   157 SRLPVK-WTAPEALKNKKFSSKSDVWSYGVLLWEVFS 192
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
259-348 1.59e-05

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 47.12  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 259 QMCTALLFLATPElsIIHCDLKPENILLCNPKRSAIkIVDFGSSCQL---GQRIYQYIQSRF-----YRSPEVLLGMPYD 330
Cdd:cd13991   106 QALEGLEYLHSRK--ILHGDVKADNVLLSSDGSDAF-LCDFGHAECLdpdGLGKSLFTGDYIpgtetHMAPEVVLGKPCD 182
                          90
                  ....*....|....*...
gi 1113820495 331 LAIDMWSLGCILVEMHTG 348
Cdd:cd13991   183 AKVDVWSSCCMMLHMLNG 200
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
156-347 1.66e-05

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 47.27  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKA-----YDRVEQEWVAIKIIKNKKAFLNQA-QIEVRLLELMnKHDTEMKYYIVHLKRhfmfrNHLCLVF 229
Cdd:cd05092    13 LGEGAFGKVFLAechnlLPEQDKMLVAVKALKEATESARQDfQREAELLTVL-QHQHIVRFYGVCTEG-----EPLIMVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSY-NLYDLLRN--------TNFRGVS---LNLTR--KFAQQMCTALLFLATpeLSIIHCDLKPENILLCNpkRSAIK 295
Cdd:cd05092    87 EYMRHgDLNRFLRShgpdakilDGGEGQApgqLTLGQmlQIASQIASGMVYLAS--LHFVHRDLATRNCLVGQ--GLVVK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 296 IVDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05092   163 IGDFGMSRDIYSTDYYRVGGRTmlpirWMPPESILYRKFTTESDIWSFGVVLWEIFT 219
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
148-355 1.83e-05

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 47.14  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKAYDRVEQ--EWVAIKIIKnkkaFLNQAQIEVRLLELMNKHDTEMkyyIVHLKRHFMFRNHL 225
Cdd:cd14112     3 GRFSFGSEIFRGRFSVIVKAVDSTTEtdAHCAVKIFE----VSDEASEAVREFESLRTLQHEN---VQRLIAAFKPSNFA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSYNLYDLLRNTNF---RGVSLNLTrkfaqQMCTALLFLATPelSIIHCDLKPENILLCNPKRSAIKIVDFGSS 302
Cdd:cd14112    76 YLVMEKLQEDVFTRFSSNDYyseEQVATTVR-----QILDALHYLHFK--GIAHLDVQPDNIMFQSVRSWQVKLVDFGRA 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 303 CQLGQRIYQYIQ-SRFYRSPEVLLG-MPYDLAIDMWSLGCILVEMHTGEPLFSGA 355
Cdd:cd14112   149 QKVSKLGKVPVDgDTDWASPEFHNPeTPITVQSDIWGLGVLTFCLLSGFHPFTSE 203
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
156-365 2.07e-05

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 47.10  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIkNKKAFLNQAQIEVRLLELMNK--HDTEMKYYIVHLKrhfMFRNHLCLVFEMLS 233
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVF-NNLSFMRPLDVQMREFEVLKKlnHKNIVKLFAIEEE---LTTRHKVLVMELCP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 Y-NLYDLLRN-TNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENIL--LCNPKRSAIKIVDFGSSCQLGQ-- 307
Cdd:cd13988    77 CgSLYTVLEEpSNAYGLPESEFLIVLRDVVAGMNHLR--ENGIVHRDIKPGNIMrvIGEDGQSVYKLTDFGAARELEDde 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 308 ---RIY---QYIQSRFYRSPeVL---LGMPYDLAIDMWSLGCILVEMHTG----EPLFSGANEVDQMNKIV 365
Cdd:cd13988   155 qfvSLYgteEYLHPDMYERA-VLrkdHQKKYGATVDLWSIGVTFYHAATGslpfRPFEGPRRNKEVMYKII 224
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
146-345 2.51e-05

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 46.92  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 146 WMDrYEIDSLIGKGSFGQVVKAYDRVEQEWV--AIKIIKNKKAFLNQAQI--EVRLLELMNKHDTemkyyIVHLKRHFMF 221
Cdd:cd05089     1 WED-IKFEDVIGEGNFGQVIKAMIKKDGLKMnaAIKMLKEFASENDHRDFagELEVLCKLGHHPN-----IINLLGACEN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 222 RNHLCLVFEMLSY-NLYDLLRNTNF----------RGVSLNLTR----KFAQQMCTALLFLAtpELSIIHCDLKPENILL 286
Cdd:cd05089    75 RGYLYIAIEYAPYgNLLDFLRKSRVletdpafakeHGTASTLTSqqllQFASDVAKGMQYLS--EKQFIHRDLAARNVLV 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 287 cnPKRSAIKIVDFGSScqLGQRIyqYIQSRFYRSP------EVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd05089   153 --GENLVSKIADFGLS--RGEEV--YVKKTMGRLPvrwmaiESLNYSVYTTKSDVWSFGVLLWEI 211
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
156-345 3.40e-05

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: 46.66  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAyDRVEQEWVAIK---IIKNKKAFlnqAQIEV----RLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLV 228
Cdd:cd14013     3 LGEGGFGTVYKG-SLLQKDPGGEKrrvVLKKAKEY---GEVEIwmneRVRRACPSSCAEFVGAFLDTTSKKFTKPSLWLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSYN-LYDLLRNTNF----------------RGV--SLNLTRKFAQQMCTALLFL-ATpelSIIHCDLKPENILLCN 288
Cdd:cd14013    79 WKYEGDAtLADLMQGKEFpynlepiifgrvlippRGPkrENVIIKSIMRQILVALRKLhST---GIVHRDVKPQNIIVSE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 289 PKRSaIKIVDFGSSCQLgqRI-YQYIQSRF-----YRSPEVL------------------------LGMPyDLaIDMWSL 338
Cdd:cd14013   156 GDGQ-FKIIDLGAAADL--RIgINYIPKEFlldprYAPPEQYimstqtpsappapvaaalspvlwqMNLP-DR-FDMYSA 230

                  ....*..
gi 1113820495 339 GCILVEM 345
Cdd:cd14013   231 GVILLQM 237
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
145-347 4.70e-05

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 45.94  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 145 KW---MDRYEIDSLIGKGSFGQVVKA----YDRVEQ-EWVAIKIIKNkkaflNQAQIEVRllELMnkhdTEMKYYIvHLK 216
Cdd:cd05054     1 KWefpRDRLKLGKPLGRGAFGKVIQAsafgIDKSATcRTVAVKMLKE-----GATASEHK--ALM----TELKILI-HIG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 217 RHFMFRNHL--C--------LVFEMLSY-NLYDLLRNT--NFRGVSLNLTRK----------------------FAQQMC 261
Cdd:cd05054    69 HHLNVVNLLgaCtkpggplmVIVEFCKFgNLSNYLRSKreEFVPYRDKGARDveeeedddelykepltledlicYSFQVA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 262 TALLFLATPElsIIHCDLKPENILLCNpkRSAIKIVDFGsscqLGQRIYQ---YIQSRFYR------SPEVLLGMPYDLA 332
Cdd:cd05054   149 RGMEFLASRK--CIHRDLAARNILLSE--NNVVKICDFG----LARDIYKdpdYVRKGDARlplkwmAPESIFDKVYTTQ 220
                         250
                  ....*....|....*
gi 1113820495 333 IDMWSLGCILVEMHT 347
Cdd:cd05054   221 SDVWSFGVLLWEIFS 235
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
155-345 5.42e-05

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 45.80  E-value: 5.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAydRVEQEW----VAIKIIK------NKKAFLNQAQIEVRLLELMNkhdtemkyyIVHLKRHFMFRNH 224
Cdd:cd05047     2 VIGEGNFGQVLKA--RIKKDGlrmdAAIKRMKeyaskdDHRDFAGELEVLCKLGHHPN---------IINLLGACEHRGY 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFEMLSY-NLYDLLRNTNF----------RGVSLNLTRK----FAQQMCTALLFLATPELsiIHCDLKPENILLCNp 289
Cdd:cd05047    71 LYLAIEYAPHgNLLDFLRKSRVletdpafaiaNSTASTLSSQqllhFAADVARGMDYLSQKQF--IHRDLAARNILVGE- 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113820495 290 kRSAIKIVDFGSScqLGQRIyqYIQSRFYRSP------EVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd05047   148 -NYVAKIADFGLS--RGQEV--YVKKTMGRLPvrwmaiESLNYSVYTTNSDVWSYGVLLWEI 204
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
158-345 5.62e-05

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 45.79  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 158 KGSFGQVVKAydRVEQEWVAIKI--IKNKKAFlnQAQIEVRLLELMnKHDTEMKYyIVHLKRHFMFRNHLCLVFEMLSY- 234
Cdd:cd14140     5 RGRFGCVWKA--QLMNEYVAVKIfpIQDKQSW--QSEREIFSTPGM-KHENLLQF-IAAEKRGSNLEMELWLITAFHDKg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 235 NLYDLLRNTnfrGVSLNLTRKFAQQMCTALLFL---------ATPELSIIHCDLKPENILLCNpKRSAIkIVDFGSSCQL 305
Cdd:cd14140    79 SLTDYLKGN---IVSWNELCHIAETMARGLSYLhedvprckgEGHKPAIAHRDFKSKNVLLKN-DLTAV-LADFGLAVRF 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 306 ----------GQriyqyIQSRFYRSPEVLLG---MPYD--LAIDMWSLGCILVEM 345
Cdd:cd14140   154 epgkppgdthGQ-----VGTRRYMAPEVLEGainFQRDsfLRIDMYAMGLVLWEL 203
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
156-347 6.19e-05

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 45.66  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQV-VKAYDRVEQ---EWVAIKIIKNKKAFLNQA--QIEVRLLELMNkHDTEMKYYIVHLKRHfmfRNHLCLVF 229
Cdd:cd05080    12 LGEGHFGKVsLYCYDPTNDgtgEMVAVKALKADCGPQHRSgwKQEIDILKTLY-HENIVKYKGCCSEQG---GKSLQLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSY-NLYDLLRNTNfrgVSLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILLCNPKrsAIKIVDFGSSCQL--G 306
Cdd:cd05080    88 EYVPLgSLRDYLPKHS---IGLAQLLLFAQQICEGMAYLHSQHY--IHRDLAARNVLLDNDR--LVKIGDFGLAKAVpeG 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 307 QRIYQYIQSR----FYRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05080   161 HEYYRVREDGdspvFWYAPECLKEYKFYYASDVWSFGVTLYELLT 205
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
274-349 6.55e-05

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 45.47  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 274 IIHCDLKPENILLcNPKRSAIKIVDFGSSCQL---GQRIYQYIQSRFYRSPEVLLGMPY-DLAIDMWSLGCILVEMHTGE 349
Cdd:cd13974   153 IVHRDLKLGNMVL-NKRTRKITITNFCLGKHLvseDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQ 231
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
148-363 6.58e-05

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 45.78  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 148 DRYEIDSLIGKGSFGQVVKA------YDR-VEQEWVAIKIIKNKKAFLNQAQI--EVRLLELMNKHDTemkyyIVHLKRH 218
Cdd:cd05101    24 DKLTLGKPLGEGCFGQVVMAeavgidKDKpKEAVTVAVKMLKDDATEKDLSDLvsEMEMMKMIGKHKN-----IINLLGA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 219 FMFRNHLCLVFEMLSY-NLYDLLRNTNFRGV--SLNLTRKFAQQM-------CT-----ALLFLATPElsIIHCDLKPEN 283
Cdd:cd05101    99 CTQDGPLYVIVEYASKgNLREYLRARRPPGMeySYDINRVPEEQMtfkdlvsCTyqlarGMEYLASQK--CIHRDLAARN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 284 ILLCnpKRSAIKIVDFGSSCQLGQRIY--QYIQSRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT--GEP------ 350
Cdd:cd05101   177 VLVT--ENNVMKIADFGLARDINNIDYykKTTNGRLpvkWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlgGSPypgipv 254
                         250
                  ....*....|....*
gi 1113820495 351 --LFSGANEVDQMNK 363
Cdd:cd05101   255 eeLFKLLKEGHRMDK 269
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
273-384 7.89e-05

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 45.05  E-value: 7.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 273 SIIHCDLKPENILLcnPKRSAIKIVDFG-----SSCQLGQRIYQYIQSRFYRSPEVLL---GMPYDLAIDMWSLGCILVE 344
Cdd:cd14151   124 SIIHRDLKSNNIFL--HEDLTVKIGDFGlatvkSRWSGSHQFEQLSGSILWMAPEVIRmqdKNPYSFQSDVYAFGIVLYE 201
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1113820495 345 MHTGEPLFSGANEVDQMNKIVEVLGIPP--AHILDQAPKARK 384
Cdd:cd14151   202 LMTGQLPYSNINNRDQIIFMVGRGYLSPdlSKVRSNCPKAMK 243
STKc_Bub1_vert cd14028
Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint ...
152-288 8.66e-05

Catalytic domain of the Serine/Threonine kinase, Vertebrate Spindle assembly checkpoint protein Bub1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Bub1 (Budding uninhibited by benzimidazoles 1) contains an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding, a GLEBS motif for Bub3/kinetochore binding, and a C-terminal kinase domain. It is involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Bub1 contributes to the inhibition of APC/C by phosphorylating its crucial cofactor, Cdc20, rendering it unable to activate APC/C. In addition, Bub1 facilitates the localization to kinetochores of other SAC and motor proteins including Mad1, Mad2, BubR1, and Plk1. It acts as the master organizer of the functional inner centromere. Bub1 also play roles in protecting sister chromatid cohesion and normal metaphase congression. The Bub1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270930 [Multi-domain]  Cd Length: 290  Bit Score: 45.23  E-value: 8.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 152 IDSLIGKGSFGQVVKA-----YDRVEQEWVAIKIIK--NKKAFLNQAQIEVRLlelmnkhDTEMKYYIVHLKRHFMFRNH 224
Cdd:cd14028     4 VDHLLGEGAFAQVYQAtqldlNDAKSNQKFVLKVQKpaNPWEFYIGTQLMERL-------KPSMRHLFIKFYSAHLFQNG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 225 LCLVFEMLSY----NLYDLLRNTNFRGVSLNLTRKFAqqMCTALLFLATPELSIIHCDLKPENILLCN 288
Cdd:cd14028    77 SVLVGELYNYgtllNAINLYKKLPEKVMPQPLVIYFA--MRILYMVEQLHDCEIIHGDIKPDNFILGE 142
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
156-356 9.13e-05

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: 44.73  E-value: 9.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAY--DRVEqewVAIKIIKNKKAF-LNQAQIEVRLLE-LMNKHDTEMkYYIVHLKRHFMFRNHLclvfeM 231
Cdd:cd05148    14 LGSGYFGEVWEGLwkNRVR---VAIKILKSDDLLkQQDFQKEVQALKrLRHKHLISL-FAVCSVGEPVYIITEL-----M 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQ 311
Cdd:cd05148    85 EKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLE--EQNSIHRDLAARNILV--GEDLVCKVADFGLARLIKEDVYL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1113820495 312 YIQSRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT-GEPLFSGAN 356
Cdd:cd05148   161 SSDKKIpykWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMN 209
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
156-345 1.03e-04

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: 44.95  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKII-----KNKKAFLNQAQIeVRLLElmnkHDTEMKYYIVHLKRhfmfrNHLCLVFE 230
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKELirfdeETQRTFLKEVKV-MRCLE----HPNVLKFIGVLYKD-----KRLNFITE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 ML-SYNLYDLLRNTNFRgVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNPKrsAIKIVDFG--------- 300
Cdd:cd14221    71 YIkGGTLRGIIKSMDSH-YPWSQRVSFAKDIASGMAYLHS--MNIIHRDLNSHNCLVRENK--SVVVADFGlarlmvdek 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 301 SSCQLGQRI--------YQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd14221   146 TQPEGLRSLkkpdrkkrYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEI 198
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
156-345 1.26e-04

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 44.39  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIikNKKAfLNQAQIeVRLLELMNK--HDTEMKYY--IVHlkrhfmfRNHLCLVFEM 231
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKM--NTLS-SNRANM-LREVQLMNRlsHPNILRFMgvCVH-------QGQLHALTEY 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSY-NLYDLLRNTNFrgVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKRSAIKIV-DFGsscqLGQRI 309
Cdd:cd14155    70 INGgNLEQLLDSNEP--LSWTVRVKLALDIARGLSYLHSK--GIFHRDLTSKNCLIKRDENGYTAVVgDFG----LAEKI 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1113820495 310 YQY---------IQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd14155   142 PDYsdgkeklavVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEI 186
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
176-347 1.30e-04

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 44.60  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 176 VAIKIIK---NKKA---FLNQAQIEVRLlelmnkHDTEmkyyIVHLKRHFMFRNHLCLVFE-MLSYNLYDLLRN------ 242
Cdd:cd05095    49 VAVKMLRadaNKNArndFLKEIKIMSRL------KDPN----IIRLLAVCITDDPLCMITEyMENGDLNQFLSRqqpegq 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 243 ----TNFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQYIQSRF- 317
Cdd:cd05095   119 lalpSNALTVSYSDLRFMAAQIASGMKYLSS--LNFVHRDLATRNCLV--GKNYTIKIADFGMSRNLYSGDYYRIQGRAv 194
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1113820495 318 ----YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05095   195 lpirWMSWESILLGKFTTASDVWAFGVTLWETLT 228
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
155-344 1.33e-04

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 44.23  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 155 LIGKGSFGQVVKAYDRvEQEWVAIKIIKN------KKAFLNQAQIevrllelMNKHDTEmkyYIVHLKRHFMFRNHLCLV 228
Cdd:cd05085     3 LLGKGNFGEVYKGTLK-DKTPVAVKTCKEdlpqelKIKFLSEARI-------LKQYDHP---NIVKLIGVCTQRQPIYIV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSYNlyDLLRNTNFRGVSLNLTR--KFAQQMCTALLFLATPelSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLG 306
Cdd:cd05085    72 MELVPGG--DFLSFLRKKKDELKTKQlvKFSLDAAAGMAYLESK--NCIHRDLAARNCLV--GENNALKISDFGMSRQED 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1113820495 307 QRIY-----QYIQSRfYRSPEVLLGMPYDLAIDMWSLGCILVE 344
Cdd:cd05085   146 DGVYsssglKQIPIK-WTAPEALNYGRYSSESDVWSFGILLWE 187
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
252-378 1.48e-04

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


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 44.07  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 252 LTRKFAQQMCTALLflATPELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDL 331
Cdd:cd05576   114 CIQRWAAEMVVALD--ALHREGIVCRDLNPNNILL--NDRGHIQLTYFSRWSEVEDSCDSDAIENMYCAPEVGGISEETE 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 332 AIDMWSLGCILVEMHTGEPLF----SGANEVDQMNkIVEVLGIPPAHILDQ 378
Cdd:cd05576   190 ACDWWSLGALLFELLTGKALVechpAGINTHTTLN-IPEWVSEEARSLLQQ 239
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
256-350 1.49e-04

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 45.00  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 256 FAQQMCTALLFLATPelSIIHCDLKPENILLCNPKrsAIKIVDFGSSCQLgQRIYQYIQ--SRF----YRSPEVLLGMPY 329
Cdd:cd05107   244 FSYQVANGMEFLASK--NCVHRDLAARNVLICEGK--LVKICDFGLARDI-MRDSNYISkgSTFlplkWMAPESIFNNLY 318
                          90       100
                  ....*....|....*....|...
gi 1113820495 330 DLAIDMWSLGCILVEMHT--GEP 350
Cdd:cd05107   319 TTLSDVWSFGILLWEIFTlgGTP 341
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
263-368 1.58e-04

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 43.16  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495  263 ALLFLATPELSIIHCDLKPENILLCNPKRsaikIVDFGSSCQLGQRiyQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCIL 342
Cdd:smart00750  21 AVCLQCLGALRELHRQAKSGNILLTWDGL----LKLDGSVAFKTPE--QSRPDPYFMAPEVIQGQSYTEKADIYSLGITL 94
                           90       100
                   ....*....|....*....|....*.
gi 1113820495  343 VEMHTGEPlfsGANEVDQMNKIVEVL 368
Cdd:smart00750  95 YEALDYEL---PYNEERELSAILEIL 117
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
151-347 1.69e-04

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 44.25  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 151 EIDSLIGKGSFGQVVKA-YDRVEQewVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVhlkrhfMFRNHL 225
Cdd:cd05073    14 KLEKKLGAGQFGEVWMAtYNKHTK--VAVKTMKpgsmSVEAFLAEANVMKTL-----QHDKLVKLHAV------VTKEPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 226 CLVFEMLSY-NLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQ 304
Cdd:cd05073    81 YIITEFMAKgSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIE--QRNYIHRDLRAANILV--SASLVCKIADFGLARV 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1113820495 305 LGQRIYQYIQ-SRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05073   157 IEDNEYTAREgAKFpikWTAPEAINFGSFTIKSDVWSFGILLMEIVT 203
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
156-347 3.20e-04

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 43.34  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEwVAIKIIK----NKKAFLNQAQIEVRLlelmnKHDTEMKYYIVhlkrhfMFRNHLCLVFE- 230
Cdd:cd05067    15 LGAGQFGEVWMGYYNGHTK-VAIKSLKqgsmSPDAFLAEANLMKQL-----QHQRLVRLYAV------VTQEPIYIITEy 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 231 MLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIY 310
Cdd:cd05067    83 MENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIE--ERNYIHRDLRAANILV--SDTLSCKIADFGLARLIEDNEY 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1113820495 311 QYIQ-SRF---YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05067   159 TAREgAKFpikWTAPEAINYGTFTIKSDVWSFGILLTEIVT 199
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
238-345 3.55e-04

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha 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: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 43.47  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 238 DLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPelSIIHCDLKPENILLCNPKrsAIKIVDFGsscqLGQRIYQ---YIQ 314
Cdd:cd05105   224 NLLSDDGSEGLTTLDLLSFTYQVARGMEFLASK--NCVHRDLAARNVLLAQGK--IVKICDFG----LARDIMHdsnYVS 295
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1113820495 315 --SRF----YRSPEVLLGMPYDLAIDMWSLGCILVEM 345
Cdd:cd05105   296 kgSTFlpvkWMAPESIFDNLYTTLSDVWSYGILLWEI 332
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
156-300 3.65e-04

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 41.27  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQI-EVR-LLELMNKHDTEMKYYIVHLKRHFMFrnhlcLVFEMLS 233
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNEEGEDLEsEMDiLRRLKGLELNIPKVLVTEDVDGPNI-----LLMELVK 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 234 -YNLYDLLRNTNFRGVSlnlTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAIKIVDFG 300
Cdd:cd13968    76 gGTLIAYTQEEELDEKD---VESIMYQLAECMRLLH--SFHLIHRDLNNDNILL--SEDGNVKLIDFG 136
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
244-347 5.04e-04

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 42.66  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 244 NFRGVSLNLTRKFAQQMCTALLFLATpeLSIIHCDLKPENILLCNpkRSAIKIVDFGSSCQLGQRIYQYIQS------RF 317
Cdd:cd05097   122 NIPSVSIANLLYMAVQIASGMKYLAS--LNFVHRDLATRNCLVGN--HYTIKIADFGMSRNLYSGDYYRIQGravlpiRW 197
                          90       100       110
                  ....*....|....*....|....*....|
gi 1113820495 318 YRSPEVLLGmPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05097   198 MAWESILLG-KFTTASDVWAFGVTLWEMFT 226
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
257-345 5.13e-04

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


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 43.00  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 257 AQQMCTALLFLATpeLSIIHCDLKPENILLcnPKRSAIKIVDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGMPYDL 331
Cdd:cd05096   144 ALQIASGMKYLSS--LNFVHRDLATRNCLV--GENLTIKIADFGMSRNLYAGDYYRIQGRAvlpirWMAWECILMGKFTT 219
                          90
                  ....*....|....
gi 1113820495 332 AIDMWSLGCILVEM 345
Cdd:cd05096   220 ASDVWAFGVTLWEI 233
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
146-352 7.26e-04

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 42.10  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 146 WMDRYEID--SLIGKGSFGQVVKAYdrVEQEWVAIKiiknKKAFLNQAQIEvrllELMNKHDTEMKYY-------IVHLK 216
Cdd:cd14158    11 FDERPISVggNKLGEGGFGVVFKGY--INDKNVAVK----KLAAMVDISTE----DLTKQFEQEIQVMakcqhenLVELL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 217 RHFMFRNHLCLVFE-MLSYNLYDLLRNTNFR-GVSLNLTRKFAQQMCTALLFLAtpELSIIHCDLKPENILLcnPKRSAI 294
Cdd:cd14158    81 GYSCDGPQLCLVYTyMPNGSLLDRLACLNDTpPLSWHMRCKIAQGTANGINYLH--ENNHIHRDIKSANILL--DETFVP 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113820495 295 KIVDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGmPYDLAIDMWSLGCILVEMHTGEPLF 352
Cdd:cd14158   157 KISDFGLARASEKFSQTIMTERIvgttaYMAPEALRG-EITPKSDIFSFGVVLLEIITGLPPV 218
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
149-366 8.49e-04

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Genetic variations in TTBK1 are linked to Alzheimer's disease (AD). Hyperphosphorylated tau is a major component of paired helical filaments that accumulate in the brain of AD patients. Studies in transgenic mice show that TTBK1 is involved in the phosphorylation-dependent pathogenic aggregation of tau. The TTBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 41.94  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 149 RYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKI--IKNKKAFLnqaQIEVRLLELMNKHDTEMKYYIVHLKRHFMFrnhlc 226
Cdd:cd14130     1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVesAQQPKQVL---KMEVAVLKKLQGKDHVCRFIGCGRNEKFNY----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 227 LVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALlfLATPELSIIHCDLKPENILLCNPKRSAIK--IVDFGSSCQ 304
Cdd:cd14130    73 VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESI--EAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLARQ 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 305 LG---------QRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVE 366
Cdd:cd14130   151 YTnttgevrppRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKE 221
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
230-313 9.58e-04

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690 [Multi-domain]  Cd Length: 158  Bit Score: 40.36  E-value: 9.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 230 EMLSYNLYDLLRNTNFRGVSLNLTR----KFAQQMCTAL-LFLATPELSIIHCDLKPENILLCNPKRSAiKIVDFGSSCq 304
Cdd:cd05120    64 DGWEYLLMERIEGETLSEVWPRLSEeekeKIADQLAEILaALHRIDSSVLTHGDLHPGNILVKPDGKLS-GIIDWEFAG- 141

                  ....*....
gi 1113820495 305 LGQRIYQYI 313
Cdd:cd05120   142 YGPPAFDYA 150
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
156-375 9.59e-04

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 41.98  E-value: 9.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKA-----YDRVEQEWVAIKIIKnKKAFLNQAQIEVRLLELMNK--HDTemkyyIVHLKRHFMFRNHLCLV 228
Cdd:cd05048    13 LGEGAFGKVYKGellgpSSEESAISVAIKTLK-ENASPKTQQDFRREAELMSDlqHPN-----IVCLLGVCTKEQPQCML 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 229 FEMLSY-NLYD-LLRNTNFRGVSLNLT-RKFAQQM-CTALLFLAT------PELS---IIHCDLKPENILLcNPKRSaIK 295
Cdd:cd05048    87 FEYMAHgDLHEfLVRHSPHSDVGVSSDdDGTASSLdQSDFLHIAIqiaagmEYLSshhYVHRDLAARNCLV-GDGLT-VK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 296 IVDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHT--GEPLFSGAN-EVDQMNKIVEV 367
Cdd:cd05048   165 ISDFGLSRDIYSSDYYRVQSKSllpvrWMPPEAILYGKFTTESDVWSFGVVLWEIFSygLQPYYGYSNqEVIEMIRSRQL 244
                         250
                  ....*....|.
gi 1113820495 368 LGIP---PAHI 375
Cdd:cd05048   245 LPCPedcPARV 255
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
156-300 1.62e-03

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 41.26  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRVEQEWVAIKI--IKNKKAflnQAQIEVRLLELMNKHDTEMK-YYIVHLKRHFmfrnhlCLVFEML 232
Cdd:cd14126     8 IGCGNFGELRLGKNLYNNEHVAIKLepMKSRAP---QLHLEYRFYKLLGQAEGLPQvYYFGPCGKYN------AMVLELL 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 233 SYNLYDLLRNTNfRGVSLNLTRKFAQQMCTALLFLATPELsiIHCDLKPENILL---CNPKRSAIKIVDFG 300
Cdd:cd14126    79 GPSLEDLFDLCD-RTFSLKTVLMIAIQLISRIEYVHSKHL--IYRDVKPENFLIgrqSTKKQHVIHIIDFG 146
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
156-357 1.67e-03

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 40.91  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVV-----KAYDRVEQEWVAIKIIKN------KKAFlnqaQIEVRLLELMnKHDTEMKYYIVHLKRhfmfrNH 224
Cdd:cd05049    13 LGEGAFGKVFlgecyNLEPEQDKMLVAVKTLKDasspdaRKDF----EREAELLTNL-QHENIVKFYGVCTEG-----DP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 225 LCLVFE-MLSYNLYDLLRNTNFRGVSL--------NLTR----KFAQQMCTALLFLATpeLSIIHCDLKPENILL-CNpk 290
Cdd:cd05049    83 LLMVFEyMEHGDLNKFLRSHGPDAAFLasedsapgELTLsqllHIAVQIASGMVYLAS--QHFVHRDLATRNCLVgTN-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 291 rSAIKIVDFGSScqlgQRIYQyiqSRFYR------------SPEVLLGMPYDLAIDMWSLGCILVEMHT--GEPLFSGAN 356
Cdd:cd05049   159 -LVVKIGDFGMS----RDIYS---TDYYRvgghtmlpirwmPPESILYRKFTTESDVWSFGVVLWEIFTygKQPWFQLSN 230

                  .
gi 1113820495 357 E 357
Cdd:cd05049   231 T 231
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
256-345 1.83e-03

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 41.12  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 256 FAQQMCTALLFLATPElsIIHCDLKPENILLCnpKRSAIKIVDFGsscqLGQRIYQ---YIQ---SRF---YRSPEVLLG 326
Cdd:cd05103   184 YSFQVAKGMEFLASRK--CIHRDLAARNILLS--ENNVVKICDFG----LARDIYKdpdYVRkgdARLplkWMAPETIFD 255
                          90
                  ....*....|....*....
gi 1113820495 327 MPYDLAIDMWSLGCILVEM 345
Cdd:cd05103   256 RVYTIQSDVWSFGVLLWEI 274
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
156-345 2.15e-03

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 40.72  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDRveQEWVAIKII--KNKKAFLNQAQI-EVRLLelmnKHDTEMKYYIVHLK-RHFMfrNHLCLVFEM 231
Cdd:cd14056     3 IGKGRYGEVWLGKYR--GEKVAVKIFssRDEDSWFRETEIyQTVML----RHENILGFIAADIKsTGSW--TQLWLITEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 232 LSY-NLYDLLRNTNfrgVSLNLTRKFAQQMCTALLFLATP------ELSIIHCDLKPENILLCNPKRSAikIVDFG---- 300
Cdd:cd14056    75 HEHgSLYDYLQRNT---LDTEEALRLAYSAASGLAHLHTEivgtqgKPAIAHRDLKSKNILVKRDGTCC--IADLGlavr 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1113820495 301 ---SSCQLGQRIYQYIQSRFYRSPEVL---LGM----PYDLAiDMWSLGCILVEM 345
Cdd:cd14056   150 ydsDTNTIDIPPNPRVGTKRYMAPEVLddsINPksfeSFKMA-DIYSFGLVLWEI 203
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
274-348 2.81e-03

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 40.58  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 274 IIHCDLKPENILLCNPKRsaIKIVDFGSSCQLGQRI---YQYIQSRFYRSPEVL-----LGMpYD-LAIDMWSLGCILVE 344
Cdd:PLN00034  189 IVHRDIKPSNLLINSAKN--VKIADFGVSRILAQTMdpcNSSVGTIAYMSPERIntdlnHGA-YDgYAGDIWSLGVSILE 265

                  ....
gi 1113820495 345 MHTG 348
Cdd:PLN00034  266 FYLG 269
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
156-348 3.01e-03

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 40.19  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYDR------------VEQEWVAIKiiknkKAFLNQAQIEVRLlelmnKHDTemkyyIVHLKRHFMFRN 223
Cdd:cd14159     1 IGEGGFGCVYQAVMRnteyavkrlkedSELDWSVVK-----NSFLTEVEKLSRF-----RHPN-----IVDLAGYSAQQG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 224 HLCLVFEML-SYNLYDLLR-NTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILL---CNPKRSAIKIVD 298
Cdd:cd14159    66 NYCLIYVYLpNGSLEDRLHcQVSCPCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNILLdaaLNPKLGDFGLAR 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1113820495 299 F-------GSSCQLGQRiyQYIQSRF-YRSPEVLLGMPYDLAIDMWSLGCILVEMHTG 348
Cdd:cd14159   146 FsrrpkqpGMSSTLART--QTVRGTLaYLPEEYVKTGTLSVEIDVYSFGVVLLELLTG 201
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
152-372 4.01e-03

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 39.66  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 152 IDSLIGKGSFGQVVKAYDRV---EQEWVAIKIIK------NKKAFLNQAQIevrllelMNKHDTEmkyYIVHLKRHFMFR 222
Cdd:cd05033     8 IEKVIGGGEFGEVCSGSLKLpgkKEIDVAIKTLKsgysdkQRLDFLTEASI-------MGQFDHP---NVIRLEGVVTKS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 223 NHLCLVFE-MLSYNLYDLLRNTNFRGVSLNLTRkFAQQMCTALLFLAtpELSIIHCDLKPENILLCNPKRSaiKIVDFGS 301
Cdd:cd05033    78 RPVMIVTEyMENGSLDKFLRENDGKFTVTQLVG-MLRGIASGMKYLS--EMNYVHRDLAARNILVNSDLVC--KVSDFGL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1113820495 302 SCQLGQRIYQY------IQSRfYRSPEVLLGMPYDLAIDMWSLGCILVE-MHTGE-PLFSGANEvDQMNKIVEVLGIPP 372
Cdd:cd05033   153 SRRLEDSEATYttkggkIPIR-WTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGErPYWDMSNQ-DVIKAVEDGYRLPP 229
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
156-347 6.69e-03

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


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 39.24  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKA----------------YDRVEQEWVAIKIIKN------KKAFLNQAQIEVRLlelmnKHDTemkyyIV 213
Cdd:cd05051    13 LGEGQFGEVHLCeanglsdltsddfignDNKDEPVLVAVKMLRPdasknaREDFLKEVKIMSQL-----KDPN-----IV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 214 HLKRHFMFRNHLCLVFEMLSY-NLYDLLRNTNFRGVSLNLTrkfAQQMCTA--LLFLAT---------PELSIIHCDLKP 281
Cdd:cd05051    83 RLLGVCTRDEPLCMIVEYMENgDLNQFLQKHEAETQGASAT---NSKTLSYgtLLYMATqiasgmkylESLNFVHRDLAT 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1113820495 282 ENILLcnPKRSAIKIVDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGMPYDLAIDMWSLGCILVEMHT 347
Cdd:cd05051   160 RNCLV--GPNYTIKIADFGMSRNLYSGDYYRIEGRAvlpirWMAWESILLGKFTTKSDVWAFGVTLWEILT 228
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
156-366 9.69e-03

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 38.63  E-value: 9.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 156 IGKGSFGQVVKAYdRVEQEWVAIKIIKNKKAFLNQAQIEVRLLEL-MNKHDTemkyyIVHLKRHFMFRNHLCLVFE-MLS 233
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLgMIRHRN-----IVRLRGYCSNPTTNLLVYEyMPN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113820495 234 YNLYDLLRNTNFRGVSLNL-TR-KFAQQMCTALLFL---ATPElsIIHCDLKPENILLCNPKRSaiKIVDFGSScqlgqR 308
Cdd:cd14664    75 GSLGELLHSRPESQPPLDWeTRqRIALGSARGLAYLhhdCSPL--IIHRDVKSNNILLDEEFEA--HVADFGLA-----K 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113820495 309 IYQYIQSRF---------YRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFsGANEVDQMNKIVE 366
Cdd:cd14664   146 LMDDKDSHVmssvagsygYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF-DEAFLDDGVDIVD 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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