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Conserved domains on  [gi|75813626|ref|NP_001028750|]
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serine/threonine-protein kinase Sgk3 isoform 1 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase Sgk3( domain architecture ID 10160715)

serine/threonine-protein kinase Sgk3 (serum/glucocorticoid-regulated kinase 3) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
165-490 0e+00

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: 697.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd05604  81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRL 404
Cdd:cd05604 161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 405 GAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNASVLEADDAFVG 484
Cdd:cd05604 241 GAKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMVPYSVCVSSDYSIVNASVLEADDAFVG 320

                ....*.
gi 75813626 485 FSYAPP 490
Cdd:cd05604 321 FSYAPP 326
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
12-120 2.35e-65

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It 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. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


:

Pssm-ID: 132780  Cd Length: 109  Bit Score: 206.49  E-value: 2.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  12 SCPSVSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMALKIPAKRIFGDNFDPDFIKQRR 91
Cdd:cd06870   1 SCPSVSIPSSDEDREKKKRFTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPASNLKIPGKRLFGNNFDPDFIKQRR 80
                        90       100
                ....*....|....*....|....*....
gi 75813626  92 AGLNEFIQNLVRYPELYNHPDVRAFLQMD 120
Cdd:cd06870  81 AGLDEFIQRLVSDPKLLNHPDVRAFLQMD 109
 
Name Accession Description Interval E-value
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
165-490 0e+00

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: 697.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd05604  81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRL 404
Cdd:cd05604 161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 405 GAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNASVLEADDAFVG 484
Cdd:cd05604 241 GAKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMVPYSVCVSSDYSIVNASVLEADDAFVG 320

                ....*.
gi 75813626 485 FSYAPP 490
Cdd:cd05604 321 FSYAPP 326
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
162-419 8.50e-104

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 310.62  E-value: 8.50e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIK-ILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTF 321
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD-VAEMYDNILHKPLSLRP---GVSLTAWSILEELLE 397
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPpewDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|..
gi 75813626    398 KDRQNRLGAKedflEIQNHPFF 419
Cdd:smart00220 237 KDPEKRLTAE----EALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
158-450 4.23e-94

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 288.64  E-value: 4.23e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLY 237
Cdd:PTZ00263  16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILME-LSHPFIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaISDT 317
Cdd:PTZ00263  95 FLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK---VPDR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLE 397
Cdd:PTZ00263 172 TFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQ 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 75813626  398 KDRQNRLGA-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFD 450
Cdd:PTZ00263 252 TDHTKRLGTlKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE 305
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
12-120 2.35e-65

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It 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. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 206.49  E-value: 2.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  12 SCPSVSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMALKIPAKRIFGDNFDPDFIKQRR 91
Cdd:cd06870   1 SCPSVSIPSSDEDREKKKRFTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPASNLKIPGKRLFGNNFDPDFIKQRR 80
                        90       100
                ....*....|....*....|....*....
gi 75813626  92 AGLNEFIQNLVRYPELYNHPDVRAFLQMD 120
Cdd:cd06870  81 AGLDEFIQRLVSDPKLLNHPDVRAFLQMD 109
Pkinase pfam00069
Protein kinase domain;
162-419 5.93e-64

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 206.71  E-value: 5.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLqKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKI-KKEKIKKKKDKNILREIKIL-KKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   242 FVNGGELFFHLQRERSFPEHRARFYAAEIAsalgylhsikivyrdlkpenilldsvghvvltdfglckEGIAISDTTTTF 321
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQIL--------------------------------------EGLESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR---PGVSLTAWSILEELLEK 398
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPelpSNLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|.
gi 75813626   399 DRQNRLGAKedflEIQNHPFF 419
Cdd:pfam00069 201 DPSKRLTAT----QALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
165-412 2.86e-62

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 210.64  E-value: 2.86e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREAR-ALARLNHPNIVRVYDVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT-TTTFCG 323
Cdd:COG0515  91 GESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTqTGTVVG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK----PLSLRPGVSLTAWSILEELLEKD 399
Cdd:COG0515 171 TPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREppppPSELRPDLPPALDAIVLRALAKD 250
                       250
                ....*....|...
gi 75813626 400 RQNRLGAKEDFLE 412
Cdd:COG0515 251 PEERYQSAAELAA 263
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
237-361 1.29e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.94  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  237 YFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISD 316
Cdd:NF033483  83 YIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR---ALSS 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 75813626  317 TTTTFC----GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:NF033483 160 TTMTQTnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
23-118 4.63e-20

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 85.09  E-value: 4.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626     23 EHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMAL-KIPAKRIFG--DNFDPDFIKQRRAGLNEFIQ 99
Cdd:smart00312   6 KIGDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILpPLPGKKLFGrlNNFSEEFIEKRRRGLEKYLQ 85
                           90       100
                   ....*....|....*....|
gi 75813626    100 NLVRYPELYNH-PDVRAFLQ 118
Cdd:smart00312  86 SLLNHPELINHsEVVLEFLE 105
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
41-118 2.09e-18

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 79.59  E-value: 2.09e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626    41 GRSEWFVFRRYAEFDKLYNTLKKQFPA-MALKIPAKRIFGdNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQ 118
Cdd:pfam00787   5 SLEEWSVRRRYSDFVELHKKLLRKFPSvIIPPLPPKRWLG-RYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLE 82
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
5-148 1.19e-11

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 66.74  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   5 HTMDYKESCPsVSIPSSDEHR-EKKKRFTVYKV-----LVSVGRSE---WFVFRRYAEFDKLYNTLKKQFPAMAL-KIPA 74
Cdd:COG5391 125 TILDYFISST-VSNPQSLTLLvDSRDKHTSYEIitvtnLPSFQLREsrpLVVRRRYSDFESLHSILIKLLPLCAIpPLPS 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  75 KR----IFGDNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDV------RAFLQM--DSPKHQSDPSEDEDERSSQKLHS 142
Cdd:COG5391 204 KKsnseYYGDRFSDEFIEERRQSLQNFLRRVSTHPLLSNYKNSksweshSTLLSSfiENRKSVPTPLSLDLTSTTQELDM 283

                ....*.
gi 75813626 143 TSQNIN 148
Cdd:COG5391 284 ERKELN 289
 
Name Accession Description Interval E-value
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
165-490 0e+00

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: 697.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd05604   1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKVILNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd05604  81 GGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRL 404
Cdd:cd05604 161 PEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 405 GAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNASVLEADDAFVG 484
Cdd:cd05604 241 GAKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMVPYSVCVSSDYSIVNASVLEADDAFVG 320

                ....*.
gi 75813626 485 FSYAPP 490
Cdd:cd05604 321 FSYAPP 326
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
166-488 0e+00

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: 683.66  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKHIMAERNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05575  81 GELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05575 161 EYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNASVLEADDAFVGF 485
Cdd:cd05575 241 SGNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVPASVGKSADSVAVSASVQEADNAFDGF 320

                ...
gi 75813626 486 SYA 488
Cdd:cd05575 321 SYV 323
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
166-489 0e+00

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: 571.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05603  81 GELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05603 161 EYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRLG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDysiVNASVLEADDAFVGF 485
Cdd:cd05603 241 AKADFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSVGRTPD---LTASSSSSSSAFLGF 317

                ....
gi 75813626 486 SYAP 489
Cdd:cd05603 318 SYAP 321
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
154-492 0e+00

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: 560.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 154 NPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTT 233
Cdd:cd05602   1 NPHAKPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLLKNVKHPFLVGLHFSFQTT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA 313
Cdd:cd05602  81 DKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILE 393
Cdd:cd05602 161 PNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 394 ELLEKDRQNRLGAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNA 473
Cdd:cd05602 241 GLLQKDRTKRLGAKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPVPNSIGQSPDSILVTA 320
                       330
                ....*....|....*....
gi 75813626 474 SVLEADDAFVGFSYAPPSE 492
Cdd:cd05602 321 SIKEAAEAFLGFSYAPPMD 339
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
168-419 4.41e-147

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: 420.77  E-value: 4.41e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILER-VNHPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTPEY 327
Cdd:cd05123  80 LFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTPEY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 328 LAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLGAK 407
Cdd:cd05123 160 LAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLGSG 239
                       250
                ....*....|..
gi 75813626 408 eDFLEIQNHPFF 419
Cdd:cd05123 240 -GAEEIKAHPFF 250
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
166-487 2.84e-142

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: 411.22  E-value: 2.84e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKVLKKEVIIEDDDVECTMTEKRVLALANRHPFLTGLHACFQTEDRLYFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05570  81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05570 161 DYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRLG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 A-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVpysvcvssDYSIVNASVLEADD--AF 482
Cdd:cd05570 241 CgPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESP--------RLTPVDSDLLTNIDqeEF 312

                ....*
gi 75813626 483 VGFSY 487
Cdd:cd05570 313 RGFSY 317
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
166-490 1.54e-141

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: 409.44  E-value: 1.54e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAErNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAHTLTE-NRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05571  80 GELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCGTP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05571 160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 -AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSvcvSSDYSIVNASVLEADDAFVG 484
Cdd:cd05571 240 gGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELT---PPDRGDLLGLEEEERPHFEQ 316

                ....*.
gi 75813626 485 FSYAPP 490
Cdd:cd05571 317 FSYSAS 322
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
165-490 1.57e-132

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: 386.76  E-value: 1.57e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAkRKLD----GKFYAVKVLQK-KIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd05584   1 LKVLGKGGYGKVFQV-RKTTgsdkGKIFAMKVLKKaSIVRNQKDTAHTKAERNIL-EAVKHPFIVDLHYAFQTGGKLYLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd05584  79 LEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd05584 159 TFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRN 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 400 RQNRLGA-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETvpysVCVSSDYSIVNASvleA 478
Cdd:cd05584 239 VSSRLGSgPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQT----PVDSPDDSTLSES---A 311
                       330
                ....*....|..
gi 75813626 479 DDAFVGFSYAPP 490
Cdd:cd05584 312 NQVFQGFTYVAP 323
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
166-488 2.00e-119

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: 353.16  E-value: 2.00e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVL-QNTRHPFLTALKYAFQTHDRLCFVMEYANG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05595  80 GELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRL- 404
Cdd:cd05595 160 EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLg 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 405 GAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVpySVCVSSDYSIVNASVLEADDAFVG 484
Cdd:cd05595 240 GGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSI--TITPPDRYDSLDLLESDQRTHFPQ 317

                ....
gi 75813626 485 FSYA 488
Cdd:cd05595 318 FSYS 321
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
160-451 7.80e-116

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: 342.64  E-value: 7.80e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEHVLNEKRIL-SEVRHPFIVNLLGSFQDDRNLYMV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaISDTTT 319
Cdd:cd05580  80 MEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKR---VKDRTY 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd05580 157 TLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVD 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 75813626 400 RQNRLGA-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDT 451
Cdd:cd05580 237 LTKRLGNlKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFDK 289
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
167-487 1.50e-115

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: 343.01  E-value: 1.50e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVTHTLAERTVLAQ-VDCPFIVPLKFSFQSPEKLYLVLAFINGG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTPE 326
Cdd:cd05585  80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGTPE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 327 YLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLGA 406
Cdd:cd05585 160 YLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGY 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 407 KeDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEEtVPYSvcvssdySIVNASVLEADDA--FVG 484
Cdd:cd05585 240 N-GAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTRE-KPID-------SVVDDSHLSESVQqqFEG 310

                ...
gi 75813626 485 FSY 487
Cdd:cd05585 311 WSY 313
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
166-490 2.06e-112

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: 335.12  E-value: 2.06e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKALKKDVVLEDDDVECTMIERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05592  81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05592 161 DYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 AKEDFL-EIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVpysvcvssDYSIVNASVLEADD--AF 482
Cdd:cd05592 241 VPECPAgDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKP--------VLTPVDKKLLASMDqeQF 312

                ....*...
gi 75813626 483 VGFSYAPP 490
Cdd:cd05592 313 KGFSFTNP 320
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
165-487 5.65e-111

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: 331.66  E-value: 5.65e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd05587   1 LMVLGKGSFGKVMLAERKGTDELYAIKILKKDVIIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd05587  81 GGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTFCGT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRL 404
Cdd:cd05587 161 PDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 405 GAKEDF-LEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETvpysvcvsSDYSIVNASVLEA--DDA 481
Cdd:cd05587 241 GCGPTGeRDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEP--------PVLTPTDKLVIMNidQSE 312

                ....*.
gi 75813626 482 FVGFSY 487
Cdd:cd05587 313 FEGFSF 318
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
166-488 9.53e-110

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: 328.30  E-value: 9.53e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKVLKKDVILQDDDVDCTMTEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05591  81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05591 161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 ---AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETvpySVCVSSDYSIVNASvleADDAF 482
Cdd:cd05591 241 cvaSQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEE---PVLTPVDPAVIKQI---NQEEF 314

                ....*.
gi 75813626 483 VGFSYA 488
Cdd:cd05591 315 RGFSFV 320
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
152-488 1.60e-109

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: 328.96  E-value: 1.60e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 152 SGNPHAKPT--DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYS 229
Cdd:cd05593   5 STTHHKRKTmnDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL-KNTRHPFLTSLKYS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 230 FQTTEKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd05593  84 FQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 EGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAW 389
Cdd:cd05593 164 EGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAK 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 390 SILEELLEKDRQNRL-GAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDY 468
Cdd:cd05593 244 SLLSGLLIKDPNKRLgGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITPPEKYDE 323
                       330       340
                ....*....|....*....|
gi 75813626 469 SIVNASVLEADDAFVGFSYA 488
Cdd:cd05593 324 DGMDCMDNERRPHFPQFSYS 343
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
161-458 3.75e-109

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: 328.14  E-value: 3.75e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAErNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05594  26 DFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTE-NRVLQNSRHPFLTALKYSFQTHDRLCFVM 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK-IVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd05594 105 EYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMK 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd05594 185 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKD 264
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 400 RQNRL-GAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETV 458
Cdd:cd05594 265 PKQRLgGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQMI 324
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
162-456 6.39e-109

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: 326.56  E-value: 6.39e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd05589   1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMCEKRIFetVNSARHPFLVNLFACFQTPEHVCFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRErSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd05589  81 MEYAAGGDLMMHIHED-VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd05589 160 TFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKN 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 400 RQNRLGAKE-DFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEE 456
Cdd:cd05589 240 PERRLGASErDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSE 297
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
166-458 1.05e-107

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: 323.60  E-value: 1.05e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDWVQTEKHVFETASNHPFLVGLHSCFQTESRLFFVIEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05588  81 GDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycrDVAEMYDN------------ILHKPLSLRPGVSLTAWSILE 393
Cdd:cd05588 161 NYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPF---DIVGSSDNpdqntedylfqvILEKPIRIPRSLSVKAASVLK 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 394 ELLEKDRQNRLGAKED--FLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETV 458
Cdd:cd05588 238 GFLNKNPAERLGCHPQtgFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPV 304
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
166-487 3.19e-107

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: 321.66  E-value: 3.19e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAkRKLDGK----FYAVKVLqKKIVLNRKEQKHIMAERNVLLkNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05582   1 KVLGQGSFGKVFLV-RKITGPdagtLYAMKVL-KKATLKVRDRVRTKMERDILA-DVNHPFIVKLHYAFQTEGKLYLILD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTF 321
Cdd:cd05582  78 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQ 401
Cdd:cd05582 158 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 402 NRLGAKED-FLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSivnasvleADD 480
Cdd:cd05582 238 NRLGAGPDgVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSAN--------AHQ 309

                ....*..
gi 75813626 481 AFVGFSY 487
Cdd:cd05582 310 LFRGFSF 316
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
166-490 9.43e-106

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: 318.39  E-value: 9.43e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05590  81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05590 161 DYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 AKEDFLE--IQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNasvleaDDAFV 483
Cdd:cd05590 241 SLTLGGEeaILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPIEESLLPMIN------QDEFR 314

                ....*..
gi 75813626 484 GFSYAPP 490
Cdd:cd05590 315 NFSYTAP 321
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
162-419 8.50e-104

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 310.62  E-value: 8.50e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKK--KIKKDRERILREIK-ILKKLKHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTF 321
Cdd:smart00220  78 YCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD-VAEMYDNILHKPLSLRP---GVSLTAWSILEELLE 397
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPpewDISPEAKDLIRKLLV 236
                          250       260
                   ....*....|....*....|..
gi 75813626    398 KDRQNRLGAKedflEIQNHPFF 419
Cdd:smart00220 237 KDPEKRLTAE----EALQHPFF 254
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
161-487 1.38e-101

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: 307.70  E-value: 1.38e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05616   1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd05616  81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd05616 161 FCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 401 QNRLG-AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGpDDIRNFDTAFTEEtvPYSVCVSSDYSIVNASvleaD 479
Cdd:cd05616 241 GKRLGcGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKACG-RNAENFDRFFTRH--PPVLTPPDQEVIRNID----Q 313

                ....*...
gi 75813626 480 DAFVGFSY 487
Cdd:cd05616 314 SEFEGFSF 321
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
161-487 1.42e-100

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: 306.13  E-value: 1.42e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05573   2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDIL-ADADSPWIVRLHYAFQDEDHLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK----------- 309
Cdd:cd05573  81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTkmnksgdresy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 ------------EGIAISDTT------TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYD 371
Cdd:cd05573 161 lndsvntlfqdnVLARRRPHKqrrvraYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 372 NILHKPLSLR----PGVSLTAWSILEELLeKDRQNRLGAKEdflEIQNHPFFESLSWADLVQkkIPPPFNPNVAGPDDIR 447
Cdd:cd05573 241 KIMNWKESLVfpddPDVSPEAIDLIRRLL-CDPEDRLGSAE---EIKAHPFFKGIDWENLRE--SPPPFVPELSSPTDTS 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 75813626 448 NFDtAFTEETVPYSVCVSSDYSIVNASVLeaddAFVGFSY 487
Cdd:cd05573 315 NFD-DFEDDLLLSEYLSNGSPLLGKGKQL----AFVGFTF 349
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
168-487 7.86e-100

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: 303.34  E-value: 7.86e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNV--KHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAHTIGERNILVRTAldESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05586  81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFCGTT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGV-SLTAWSILEELLEKDRQNR 403
Cdd:cd05586 161 EYLAPEVLLDEKgYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDVlSDEGRSFVKGLLNRNPKHR 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 404 LGAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIV----NASVLEA- 478
Cdd:cd05586 241 LGAHDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFTNASLLNANIVPWAQRPGlpgaTSTPLSPs 320
                       330
                ....*....|
gi 75813626 479 -DDAFVGFSY 487
Cdd:cd05586 321 vQANFRGFTF 330
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
161-450 1.42e-98

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: 298.55  E-value: 1.42e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLkNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14209   2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLNEKRILQ-AINFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaISDTTTT 320
Cdd:cd14209  81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKR---VKGRTWT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd14209 158 LCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDL 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 401 QNRLG-AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFD 450
Cdd:cd14209 238 TKRFGnLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFD 288
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
161-458 6.87e-97

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: 296.94  E-value: 6.87e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05618  21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd05618 101 EYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycrDVAEMYDN------------ILHKPLSLRPGVSLTA 388
Cdd:cd05618 181 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPF---DIVGSSDNpdqntedylfqvILEKQIRIPRSLSVKA 257
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 389 WSILEELLEKDRQNRLGA--KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETV 458
Cdd:cd05618 258 ASVLKSFLNKDPKERLGChpQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPV 329
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
161-451 9.14e-96

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: 291.65  E-value: 9.14e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05612   2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVL-KEVSHPFIIRLFWTEHDQRFLYMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaISDTTTT 320
Cdd:cd05612  81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKK---LRDRTWT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd05612 158 LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDR 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 401 QNRLGA-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDT 451
Cdd:cd05612 238 TRRLGNmKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDD 289
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
161-458 1.64e-95

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: 293.47  E-value: 1.64e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05617  16 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd05617  96 EYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTST 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF-YCRDVAEM------YDNILHKPLSLRPGVSLTAWSILE 393
Cdd:cd05617 176 FCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdIITDNPDMntedylFQVILEKPIRIPRFLSVKASHVLK 255
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 394 ELLEKDRQNRLGA--KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETV 458
Cdd:cd05617 256 GFLNKDPKERLGCqpQTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEPV 322
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
161-461 5.58e-95

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: 291.05  E-value: 5.58e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAkRKLDG----KFYAVKVLQK-KIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEK 235
Cdd:cd05614   1 NFELLKVLGTGAYGKVFLV-RKVSGhdanKLYAMKVLRKaALVQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQTDAK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA-I 314
Cdd:cd05614  80 LHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTeE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 SDTTTTFCGTPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCR----DVAEMYDNILHKPLSLRPGVSLTAW 389
Cdd:cd05614 160 KERTYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLTGASPFTLEgeknTQSEVSRRILKCDPPFPSFIGPVAR 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75813626 390 SILEELLEKDRQNRLGA-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYS 461
Cdd:cd05614 240 DLLQKLLCKDPKKRLGAgPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYS 312
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
166-490 8.28e-95

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: 289.92  E-value: 8.28e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd05620  81 GDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFCGTP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd05620 161 DYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 406 AKEDfleIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCvssDYSIVNASvleADDAFVGF 485
Cdd:cd05620 241 VVGN---IRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSYS---DKNLIDSM---DQSAFAGF 311

                ....*
gi 75813626 486 SYAPP 490
Cdd:cd05620 312 SFINP 316
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
160-445 1.63e-94

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: 289.14  E-value: 1.63e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLkNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd05574   1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILA-TLDHPFLPTLYASFQTSTHLCFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEG------ 311
Cdd:cd05574  80 MDYCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSsvtppp 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 312 ----------------------IAISDT-TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAE 368
Cdd:cd05574 160 vrkslrkgsrrssvksieketfVAEPSArSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDE 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 369 MYDNILHKPLSL--RPGVSLTAWSILEELLEKDRQNRLGAKEDFLEIQNHPFFESLSWADLvqKKIPPPFNPNVAGPDD 445
Cdd:cd05574 240 TFSNILKKELTFpeSPPVSSEAKDLIRKLLVKDPSKRLGSKRGASEIKRHPFFRGVNWALI--RNMTPPIIPRPDDPID 316
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
158-450 4.23e-94

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 288.64  E-value: 4.23e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLY 237
Cdd:PTZ00263  16 KLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILME-LSHPFIVNMMCSFQDENRVY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaISDT 317
Cdd:PTZ00263  95 FLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKK---VPDR 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLE 397
Cdd:PTZ00263 172 TFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQ 251
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 75813626  398 KDRQNRLGA-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFD 450
Cdd:PTZ00263 252 TDHTKRLGTlKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE 305
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
158-490 6.95e-94

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: 288.43  E-value: 6.95e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd05615   8 RLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFQTVDRLY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT 317
Cdd:cd05615  88 FVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLE 397
Cdd:cd05615 168 TRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMT 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 398 KDRQNRLG-AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGpDDIRNFDTAFTeETVPysVCVSSDySIVNASVL 476
Cdd:cd05615 248 KHPAKRLGcGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVCG-KGAENFDKFFT-RGQP--VLTPPD-QLVIANID 322
                       330
                ....*....|....
gi 75813626 477 EADdaFVGFSYAPP 490
Cdd:cd05615 323 QAD--FEGFSYVNP 334
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
167-422 1.05e-93

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: 285.44  E-value: 1.05e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAkRKL----DGKFYAVKVLQK-KIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05583   1 VLGTGAYGKVFLV-RKVgghdAGKLYAMKVLKKaTIVQKAKTAEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHL-QRERsFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAIS-DTTT 319
Cdd:cd05583  80 YVNGGELFTHLyQREH-FTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGEnDRAY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQP--YDNTVDWWCLGAVLYEMLYGLPPFYCRDV----AEMYDNILHKPLSLRPGVSLTAWSILE 393
Cdd:cd05583 159 SFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLTGASPFTVDGErnsqSEISKRILKSHPPIPKTFSAEAKDFIL 238
                       250       260       270
                ....*....|....*....|....*....|
gi 75813626 394 ELLEKDRQNRLGAK-EDFLEIQNHPFFESL 422
Cdd:cd05583 239 KLLEKDPKKRLGAGpRGAHEIKEHPFFKGL 268
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
161-490 1.06e-92

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: 285.28  E-value: 1.06e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05619   6 DFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENLFFVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd05619  86 EYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTST 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI-LHKPLSLRpGVSLTAWSILEELLEKD 399
Cdd:cd05619 166 FCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIrMDNPFYPR-WLEKEAKDILVKLFVRE 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 400 RQNRLGAKEDfleIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVcvsSDYSIVNASvleAD 479
Cdd:cd05619 245 PERRLGVRGD---IRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPRLSF---ADRALINSM---DQ 315
                       330
                ....*....|.
gi 75813626 480 DAFVGFSYAPP 490
Cdd:cd05619 316 NMFRNFSFVNP 326
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
168-424 4.15e-90

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: 276.40  E-value: 4.15e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd05579   1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQ-AQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGI--------------- 312
Cdd:cd05579  80 LYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLvrrqiklsiqkksng 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLT--AWS 390
Cdd:cd05579 160 APEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDPEVSdeAKD 239
                       250       260       270
                ....*....|....*....|....*....|....
gi 75813626 391 ILEELLEKDRQNRLGAKeDFLEIQNHPFFESLSW 424
Cdd:cd05579 240 LISKLLTPDPEKRLGAK-GIEEIKNHPFFKGIDW 272
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
161-419 1.20e-86

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: 267.54  E-value: 1.20e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05581   2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSR-LAHPGIVKLYYTFQDESKLYFVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG----LCKEGIAISD 316
Cdd:cd05581  81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvLGPDSSPEST 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 T-------------TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPG 383
Cdd:cd05581 161 KgdadsqiaynqarAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPEN 240
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75813626 384 VSLTAWSILEELLEKDRQNRLGAKEDFL--EIQNHPFF 419
Cdd:cd05581 241 FPPDAKDLIQKLLVLDPSKRLGVNENGGydELKAHPFF 278
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
161-438 6.93e-86

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: 266.10  E-value: 6.93e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAkRKLDG----KFYAVKVLQK-KIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEK 235
Cdd:cd05613   1 NFELLKVLGTGAYGKVFLV-RKVSGhdagKLYAMKVLKKaTIVQKAKTAEHTRTERQVLEHIRQSPFLVTLHYAFQTDTK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHL-QRERsFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAI 314
Cdd:cd05613  80 LHLILDYINGGELFTHLsQRER-FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 -SDTTTTFCGTPEYLAPEVIR--KQPYDNTVDWWCLGAVLYEMLYGLPPFYC----RDVAEMYDNILHKPLSLRPGVSLT 387
Cdd:cd05613 159 eNERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTVdgekNSQAEISRRILKSEPPYPQEMSAL 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 388 AWSILEELLEKDRQNRLG-AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNP 438
Cdd:cd05613 239 AKDIIQRLLMKDPKKRLGcGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
161-487 1.55e-85

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: 266.40  E-value: 1.55e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05599   2 DFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEMLEKEQVAHVRAERDILAE-ADNPWVVKLYYSFQDEENLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKeGIAISDTTTT 320
Cdd:cd05599  81 EFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT-GLKKSHLAYS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH--KPLSLRPGVSLT--AWSILEELL 396
Cdd:cd05599 160 TVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNwrETLVFPPEVPISpeAKDLIERLL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 397 eKDRQNRLGAKeDFLEIQNHPFFESLSWADLVQKkiPPPFNPNVAGPDDIRNFDtafTEETVPYSVCVSSDYSIVNASVL 476
Cdd:cd05599 240 -CDAEHRLGAN-GVEEIKSHPFFKGVDWDHIRER--PAPILPEVKSILDTSNFD---EFEEVDLQIPSSPEAGKDSKELK 312
                       330
                ....*....|.
gi 75813626 477 EADDAFVGFSY 487
Cdd:cd05599 313 SKDWVFIGYTY 323
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
162-419 8.21e-84

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: 259.50  E-value: 8.21e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELE-ILQELEHPFLVNLWYSFQDEEDMYMVVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFglckeGIAI----SDT 317
Cdd:cd05578  81 LLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDF-----NIATkltdGTL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDvAEMYDNILHKPLSLRP----GVSLTAWSILE 393
Cdd:cd05578 156 ATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHS-RTSIEEIRAKFETASVlypaGWSEEAIDLIN 234
                       250       260
                ....*....|....*....|....*.
gi 75813626 394 ELLEKDRQNRLGakeDFLEIQNHPFF 419
Cdd:cd05578 235 KLLERDPQKRLG---DLSDLKNHPYF 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
161-418 6.13e-83

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: 257.02  E-value: 6.13e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHImaERNV-LLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14007   1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQL--RREIeIQSHLRHPNILRLYGYFEDKKRIYLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiAISDTTT 319
Cdd:cd14007  79 LEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVH--APSNRRK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd14007 157 TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKD 236
                       250
                ....*....|....*....
gi 75813626 400 RQNRLGAKedflEIQNHPF 418
Cdd:cd14007 237 PSKRLSLE----QVLNHPW 251
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
161-418 3.22e-82

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: 255.48  E-value: 3.22e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKhIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEM-LRREIEIL-KRLDHPNIVKLYEVFEDDKNLYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV---GHVVLTDFGLCKEgIAISDT 317
Cdd:cd05117  79 ELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpdSPIKIIDFGLAKI-FEEGEK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILE 393
Cdd:cd05117 158 LKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSpewkNVSEEAKDLIK 237
                       250       260
                ....*....|....*....|....*
gi 75813626 394 ELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd05117 238 RLLVVDPKKRLTAA----EALNHPW 258
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
161-487 3.86e-80

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: 252.65  E-value: 3.86e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKhPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05597   2 DFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDR-RWITKLHYAFQDENYLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQR-ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC----KEGIAIS 315
Cdd:cd05597  81 DYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClklrEDGTVQS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 dttTTFCGTPEYLAPEVIR-----KQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR-----PGVS 385
Cdd:cd05597 161 ---SVAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHKEHFSfpddeDDVS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 386 LTAWSILEELLeKDRQNRLGaKEDFLEIQNHPFFESLSWADLvqKKIPPPFNPNVAGPDDIRNFDTAFTEETVPysvcvS 465
Cdd:cd05597 238 EEAKDLIRRLI-CSRERRLG-QNGIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFDVDDDDLRHT-----D 308
                       330       340
                ....*....|....*....|..
gi 75813626 466 SDYSIVNASVLEADDAFVGFSY 487
Cdd:cd05597 309 SLPPPSNAAFSGLHLPFVGFTY 330
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
161-452 1.17e-79

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: 251.47  E-value: 1.17e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05598   2 MFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDVLKRNQVAHVKAERDIL-AEADNEWVVKLYYSFQDKENLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCkegiaisdttTT 320
Cdd:cd05598  81 DYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLC----------TG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 F--------------CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----P 382
Cdd:cd05598 151 FrwthdskyylahslVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRTTLKipheA 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 383 GVSLTAWSILEELLeKDRQNRLGaKEDFLEIQNHPFFESLSWADLVQKKipPPFNPNVAGPDDIRNFDTA 452
Cdd:cd05598 231 NLSPEAKDLILRLC-CDAEDRLG-RNGADEIKAHPFFAGIDWEKLRKQK--APYIPTIRHPTDTSNFDPV 296
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
161-487 3.66e-78

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: 249.56  E-value: 3.66e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLkNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05600  12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILT-TTNSPWLVKLLYAFQDPENVYLAM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA------- 313
Cdd:cd05600  91 EYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLSpkkiesm 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ----------------ISDTTTTF--------------CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC 363
Cdd:cd05600 171 kirleevkntafleltAKERRNIYramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 364 RDVAEMYDNI------LHKPLS----LRPGVSLTAWSILEELLEkDRQNRLGAKEDfleIQNHPFFESLSWADLVqKKIP 433
Cdd:cd05600 251 STPNETWANLyhwkktLQRPVYtdpdLEFNLSDEAWDLITKLIT-DPQDRLQSPEQ---IKNHPFFKNIDWDRLR-EGSK 325
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 434 PPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSDYSIVNASVLEADD-----AFVGFSY 487
Cdd:cd05600 326 PPFIPELESEIDTSYFDDFNDEADMAKYKDVHEKQKSLEGSGKNGGDngnrsLFVGFTF 384
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
168-424 1.64e-76

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: 240.98  E-value: 1.64e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEIL-EECNSPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTFCGTPEY 327
Cdd:cd05572  80 LWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKK-LGSGRKTWTFCGTPEY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 328 LAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEM--YDNILH--KPLSLRPGVSLTAWSILEELLEKDRQNR 403
Cdd:cd05572 159 VAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMkiYNIILKgiDKIEFPKYIDKNAKNLIKQLLRRNPEER 238
                       250       260
                ....*....|....*....|..
gi 75813626 404 LG-AKEDFLEIQNHPFFESLSW 424
Cdd:cd05572 239 LGyLKGGIRDIKKHKWFEGFDW 260
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
138-488 2.64e-76

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: 243.44  E-value: 2.64e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 138 QKLHSTSQNINlgpsgNPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRK------EQKHIMAER 211
Cdd:cd05596   9 NRYEKPVNEIT-----KLRMNAEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSdsaffwEERDIMAHA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 212 NvllknvkHPFLVGLHYSFQTTEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPEN 291
Cdd:cd05596  84 N-------SEWIVQLHYAFQDDKYLYMVMDYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 292 ILLDSVGHVVLTDFGLC----KEGIAISDTTTtfcGTPEYLAPEVIRKQP----YDNTVDWWCLGAVLYEMLYGLPPFYC 363
Cdd:cd05596 156 MLLDASGHLKLADFGTCmkmdKDGLVRSDTAV---GTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFYA 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 364 RDVAEMYDNILHKPLSLR----PGVSLTAWSILEELLEkDRQNRLGaKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPN 439
Cdd:cd05596 233 DSLVGTYGKIMNHKNSLQfpddVEISKDAKSLICAFLT-DREVRLG-RNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPE 310
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 75813626 440 VAGPDDIRNFDTAFTEETVPYSVCVSSDYSivnASVLeaddAFVGFSYA 488
Cdd:cd05596 311 LSSDIDTSNFDDIEEDETPEETFPVPKAFV---GNHL----PFVGFTYS 352
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
161-418 3.21e-75

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: 237.03  E-value: 3.21e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKS-KLKEEIEEKIKREIEIM-KLLNHPNIIKLYEVIETENKIYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTT 320
Cdd:cd14003  79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE-FRGGSLLKT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd14003 158 FCGTPAYAAPEVLLGRKYDGPkADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVD 237
                       250
                ....*....|....*....
gi 75813626 400 RQNRLGAKedflEIQNHPF 418
Cdd:cd14003 238 PSKRITIE----EILNHPW 252
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
160-487 1.24e-74

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: 238.36  E-value: 1.24e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNvKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKA-NSPWITKLQYAFQDSENLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQR-ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG----LCKEGIAI 314
Cdd:cd05601  80 MEYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGsaakLSSDKTVT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 SDTTTtfcGTPEYLAPEVI------RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI------LHKPLSLRp 382
Cdd:cd05601 160 SKMPV---GTPDYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNImnfkkfLKFPEDPK- 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 383 gVSLTAWSILEELLEkDRQNRLGakedFLEIQNHPFFESLSWADLVQKkiPPPFNPNVAGPDDIRNFDTAFTEETVPYSV 462
Cdd:cd05601 236 -VSESAVDLIKGLLT-DAKERLG----YEGLCCHPFFSGIDWNNLRQT--VPPFVPTLTSDDDTSNFDEFEPKKTRPSYE 307
                       330       340
                ....*....|....*....|....*
gi 75813626 463 CVSSDysivnASVLEADDAFVGFSY 487
Cdd:cd05601 308 NFNKS-----KGFSGKDLPFVGFTF 327
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
162-439 5.18e-74

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: 235.33  E-value: 5.18e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05605   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEK-VNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTT 319
Cdd:cd05605  81 IMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGETIR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCR----DVAEMYDNILHKPLSLRPGVSLTAWSILEEL 395
Cdd:cd05605 160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARkekvKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 75813626 396 LEKDRQNRLGAKED-FLEIQNHPFFESLSWADLVQKKIPPPFNPN 439
Cdd:cd05605 240 LQKDPKTRLGCRGEgAEDVKSHPFFKSINFKRLEAGLLEPPFVPD 284
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
165-424 1.76e-73

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: 233.14  E-value: 1.76e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd05611   1 LKPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIaISDTTTTFCGT 324
Cdd:cd05611  81 GGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGL-EKRHNKKFVGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK----PLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd05611 160 PDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRrinwPEEVKEFCSPEAVDLINRLLCMDP 239
                       250       260
                ....*....|....*....|....
gi 75813626 401 QNRLGAKeDFLEIQNHPFFESLSW 424
Cdd:cd05611 240 AKRLGAN-GYQEIKSHPFFKSINW 262
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
168-439 4.20e-73

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: 232.80  E-value: 4.20e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEK-VSSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTFCGTP 325
Cdd:cd05577  80 LKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVGTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQ-PYDNTVDWWCLGAVLYEMLYGLPPFYCR----DVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd05577 159 GYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDP 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75813626 401 QNRLGAKEDFL-EIQNHPFFESLSWADLVQKKIPPPFNPN 439
Cdd:cd05577 239 ERRLGCRGGSAdEVKEHPFFRSLNWQRLEAGMLEPPFVPD 278
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
163-439 1.44e-72

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: 231.69  E-value: 1.44e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 163 DFlKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd05608   5 DF-RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKGYEGAMVEKRILAK-VHSRFIVSLAYAFQTKTDLCLVMTI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHL----QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT 318
Cdd:cd05608  83 MNGGDLRYHIynvdEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCR----DVAEMYDNILHKPLSLRPGVSLTAWSILEE 394
Cdd:cd05608 163 KGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASKSICEA 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 395 LLEKDRQNRLGAKE-DFLEIQNHPFFESLSWADLVQKKIPPPFNPN 439
Cdd:cd05608 243 LLAKDPEKRLGFRDgNCDGLRTHPFFRDINWRKLEAGILPPPFVPD 288
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
161-450 2.00e-67

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: 222.19  E-value: 2.00e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLkNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05624  73 DFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLV-NGDCQWITTLHYAFQDENYLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQR-ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC----KEGIAIS 315
Cdd:cd05624 152 DYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSClkmnDDGTVQS 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTtfcGTPEYLAPEVIRKQ-----PYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL-HKPLSLRPG----VS 385
Cdd:cd05624 232 SVAV---GTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnHEERFQFPShvtdVS 308
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 386 LTAWSILEELLeKDRQNRLGAK--EDFleiQNHPFFESLSWADLvqKKIPPPFNPNVAGPDDIRNFD 450
Cdd:cd05624 309 EEAKDLIQRLI-CSRERRLGQNgiEDF---KKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFD 369
PX_CISK cd06870
The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The ...
12-120 2.35e-65

The phosphoinositide binding Phox Homology Domain of Cytokine-Independent Survival Kinase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Cytokine-independent survival kinase (CISK), also called Serum- and Glucocorticoid-induced Kinase 3 (SGK3), plays a role in cell growth and survival. It 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. CISK/SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. N-terminal to a catalytic kinase domain, CISK contains a PX domain which binds highly phosphorylated PIs, directs membrane localization, and regulates the enzyme's activity.


Pssm-ID: 132780  Cd Length: 109  Bit Score: 206.49  E-value: 2.35e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  12 SCPSVSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMALKIPAKRIFGDNFDPDFIKQRR 91
Cdd:cd06870   1 SCPSVSIPSSDEDREKKKRFTVYKVVVSVGRSSWFVFRRYAEFDKLYESLKKQFPASNLKIPGKRLFGNNFDPDFIKQRR 80
                        90       100
                ....*....|....*....|....*....
gi 75813626  92 AGLNEFIQNLVRYPELYNHPDVRAFLQMD 120
Cdd:cd06870  81 AGLDEFIQRLVSDPKLLNHPDVRAFLQMD 109
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
161-424 2.68e-65

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: 212.65  E-value: 2.68e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDIL-TFAENPFVVSMYCSFETKRHLCMVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGI-------- 312
Cdd:cd05609  80 EYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLmslttnly 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 --AISDTTTTF-----CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPG-- 383
Cdd:cd05609 160 egHIEKDTREFldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGdd 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75813626 384 -VSLTAWSILEELLEKDRQNRLGAKeDFLEIQNHPFFESLSW 424
Cdd:cd05609 240 aLPDDAQDLITRLLQQNPLERLGTG-GAEEVKQHPFFQDLDW 280
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
158-467 1.80e-64

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 212.53  E-value: 1.80e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  158 KPTDFDFLKVIGKGSFGKVLLAKRKlDGKF--YAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEK 235
Cdd:PTZ00426  28 KYEDFNFIRTLGTGSFGRVILATYK-NEDFppVAIKRFEKSKIIKQKQVDHVFSERKIL-NYINHPFCVNLYGSFKDESY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  236 LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAIS 315
Cdd:PTZ00426 106 LYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAK---VVD 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEEL 395
Cdd:PTZ00426 183 TRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKL 262
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75813626  396 LEKDRQNRLG-AKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCVSSD 467
Cdd:PTZ00426 263 LSHDLTKRYGnLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFERVQEDLTIADKITNEND 335
Pkinase pfam00069
Protein kinase domain;
162-419 5.93e-64

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 206.71  E-value: 5.93e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLqKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKI-KKEKIKKKKDKNILREIKIL-KKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   242 FVNGGELFFHLQRERSFPEHRARFYAAEIAsalgylhsikivyrdlkpenilldsvghvvltdfglckEGIAISDTTTTF 321
Cdd:pfam00069  79 YVEGGSLFDLLSEKGAFSEREAKFIMKQIL--------------------------------------EGLESGSSLTTF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR---PGVSLTAWSILEELLEK 398
Cdd:pfam00069 121 VGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPelpSNLSEEAKDLLKKLLKK 200
                         250       260
                  ....*....|....*....|.
gi 75813626   399 DRQNRLGAKedflEIQNHPFF 419
Cdd:pfam00069 201 DPSKRLTAT----QALQHPWF 217
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
161-450 7.27e-64

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: 210.89  E-value: 7.27e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNvKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05610   5 EFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALS-KSPFIVHLYYSLQSANNVYLVM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK----EGIAISD 316
Cdd:cd05610  84 EYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnRELNMMD 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTT-------------------------------------------------FCGTPEYLAPEVIRKQPYDNTVDWWCL 347
Cdd:cd05610 164 ILTTpsmakpkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWWAL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 348 GAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPG---VSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFFESLSW 424
Cdd:cd05610 244 GVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGeeeLSVNAQNAIEILLTMDPTKRAGLK----ELKQHPLFHGVDW 319
                       330       340
                ....*....|....*....|....*.
gi 75813626 425 ADLVQKkiPPPFNPNVAGPDDIRNFD 450
Cdd:cd05610 320 ENLQNQ--TMPFIPQPDDETDTSYFE 343
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
161-487 1.08e-63

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: 211.63  E-value: 1.08e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNvKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05629   2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAES-DSPWVVSLYYSFQDAQYLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC------------ 308
Cdd:cd05629  81 EFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsayy 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 309 ---------------KEGIAISDTTTTF--------------------CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYE 353
Cdd:cd05629 161 qkllqgksnknridnRNSVAVDSINLTMsskdqiatwkknrrlmaystVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 354 MLYGLPPFYCRDVAEMYDNILHKPLSLR-PG---VSLTAWSILEELLeKDRQNRLGaKEDFLEIQNHPFFESLSWADLvq 429
Cdd:cd05629 241 CLIGWPPFCSENSHETYRKIINWRETLYfPDdihLSVEAEDLIRRLI-TNAENRLG-RGGAHEIKSHPFFRGVDWDTI-- 316
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 430 KKIPPPFNPNVAGPDDIRNFDTAFTEEtVPYSVCVSSDYSIVNASVLEADDAFVGFSY 487
Cdd:cd05629 317 RQIRAPFIPQLKSITDTSYFPTDELEQ-VPEAPALKQAAPAQQEESVELDLAFIGYTY 373
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
165-412 1.63e-63

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: 207.05  E-value: 1.63e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd14014   5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREAR-ALARLSHPNIVRVYDVGEDDGRPYIVMEYVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK-EGIAISDTTTTFCG 323
Cdd:cd14014  84 GGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARaLGDSGLTQTGSVLG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK----PLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd14014 164 TPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEapppPSPLNPDVPPALDAIILRALAKD 243
                       250
                ....*....|...
gi 75813626 400 RQNRLGAKEDFLE 412
Cdd:cd14014 244 PEERPQSAAELLA 256
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
161-419 3.80e-63

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: 206.16  E-value: 3.80e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKV--LQKkivLNRKEQKhiMAERNV-LLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEidLSN---MSEKERE--EALNEVkLLSKLKHPNIVKYYESFEENGKLC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERS----FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA 313
Cdd:cd08215  76 IVMEYADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLES 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK---PLSlrPGVSLTAWS 390
Cdd:cd08215 156 TTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGqypPIP--SQYSSELRD 233
                       250       260
                ....*....|....*....|....*....
gi 75813626 391 ILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd08215 234 LVNSMLQKDPEKRPSAN----EILSSPFI 258
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
161-467 9.95e-63

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 209.87  E-value: 9.95e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLkNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05623  73 DFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLV-NGDSQWITTLHYAFQDDNNLYLVM 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQR-ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC----KEGIAIS 315
Cdd:cd05623 152 DYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSClklmEDGTVQS 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTtfcGTPEYLAPEVIR-----KQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL-HK-----PLSLrPGV 384
Cdd:cd05623 232 SVAV---GTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnHKerfqfPTQV-TDV 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 385 SLTAWSILEELLeKDRQNRLGAK--EDFleiQNHPFFESLSWADLvqKKIPPPFNPNVAGPDDIRNFD------------ 450
Cdd:cd05623 308 SENAKDLIRRLI-CSREHRLGQNgiEDF---KNHPFFVGIDWDNI--RNCEAPYIPEVSSPTDTSNFDvdddclkncetm 381
                       330       340
                ....*....|....*....|....*...
gi 75813626 451 -----TAFTEETVPY------SVCVSSD 467
Cdd:cd05623 382 pppthTAFSGHHLPFvgftytSSCVLSD 409
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
167-438 1.86e-62

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: 204.98  E-value: 1.86e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLlAKRKLD-GKFYAVKVLQKKIVLNRKEQKHIMAERNVLLK---NVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd05606   1 IIGRGGFGEVY-GCRKADtGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstGGDCPFIVCMTYAFQTPDKLCFILDL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaISDTTTTFC 322
Cdd:cd05606  80 MNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACD---FSKKKPHAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 -GTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFY---CRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLE 397
Cdd:cd05606 157 vGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRqhkTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQ 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75813626 398 KDRQNRLGAK-EDFLEIQNHPFFESLSWADLVQKKIPPPFNP 438
Cdd:cd05606 237 RDVSKRLGCLgRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
165-412 2.86e-62

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 210.64  E-value: 2.86e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREAR-ALARLNHPNIVRVYDVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT-TTTFCG 323
Cdd:COG0515  91 GESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATLTqTGTVVG 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK----PLSLRPGVSLTAWSILEELLEKD 399
Cdd:COG0515 171 TPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREppppPSELRPDLPPALDAIVLRALAKD 250
                       250
                ....*....|...
gi 75813626 400 RQNRLGAKEDFLE 412
Cdd:COG0515 251 PEERYQSAAELAA 263
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
165-461 4.49e-62

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: 207.56  E-value: 4.49e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd05626   6 IKTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAE-ADNEWVVKLYYSFQDKDNLYFVMDYIP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC------------KEGI 312
Cdd:cd05626  85 GGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCtgfrwthnskyyQKGS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AI-----------SDTTTTFC------------------------GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG 357
Cdd:cd05626 165 HIrqdsmepsdlwDDVSNCRCgdrlktleqratkqhqrclahslvGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVG 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 358 LPPFYCRDVAEM------YDNILHKPLSLRpgVSLTAWSILEELL--EKDRQNRLGAKedflEIQNHPFFESLSWADLVQ 429
Cdd:cd05626 245 QPPFLAPTPTETqlkvinWENTLHIPPQVK--LSPEAVDLITKLCcsAEERLGRNGAD----DIKAHPFFSEVDFSSDIR 318
                       330       340       350
                ....*....|....*....|....*....|..
gi 75813626 430 KKiPPPFNPNVAGPDDIRNFDTafTEETVPYS 461
Cdd:cd05626 319 TQ-PAPYVPKISHPMDTSNFDP--VEEESPWN 347
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
162-439 1.27e-61

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: 203.33  E-value: 1.27e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05630   2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEK-VNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTT 319
Cdd:cd05630  81 LMNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQTIK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVA----EMYDNILHKPLSLRPGVSLTAWSILEEL 395
Cdd:cd05630 160 GRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKikreEVERLVKEVPEEYSEKFSPQARSLCSML 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 75813626 396 LEKDRQNRLGAK-EDFLEIQNHPFFESLSWADLVQKKIPPPFNPN 439
Cdd:cd05630 240 LCKDPAERLGCRgGGAREVKEHPLFKKLNFKRLGAGMLEPPFKPD 284
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
162-439 5.96e-60

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: 198.68  E-value: 5.96e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05631   2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEK-VNSRFVVSLAYAYETKDALCLVLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTT 319
Cdd:cd05631  81 IMNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGETVR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK----PLSLRPGVSLTAWSILEEL 395
Cdd:cd05631 160 GRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDRRvkedQEEYSEKFSEDAKSICRML 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 75813626 396 LEKDRQNRLGAKED-FLEIQNHPFFESLSWADLVQKKIPPPFNPN 439
Cdd:cd05631 240 LTKNPKERLGCRGNgAAGVKQHPIFKNINFKRLEANMLEPPFCPD 284
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
161-418 6.29e-60

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: 197.47  E-value: 6.29e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14002   2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKR-GKSEKELRNLRQEIEIL-RKLNHPNIIEMLDSFETKKEFVVVT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGgELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISDTT-- 318
Cdd:cd14002  80 EYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAR---AMSCNTlv 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 -TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLE 397
Cdd:cd14002 156 lTSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLN 235
                       250       260
                ....*....|....*....|.
gi 75813626 398 KDRQNRLGAkEDFLEiqnHPF 418
Cdd:cd14002 236 KDPSKRLSW-PDLLE---HPF 252
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
168-354 3.41e-59

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: 194.41  E-value: 3.41e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVAVKVIPKE--KLKKLLEELLREIEILKK-LNHPNIVKLYDVFETENFLYLVMEYCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHL-QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGIAISDTTTTFCGT 324
Cdd:cd00180  78 LKDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdlDSDDSLLKTTGGTTP 157
                       170       180       190
                ....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEM 354
Cdd:cd00180 158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
162-451 3.79e-58

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: 194.81  E-value: 3.79e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05632   4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEK-VNSQFVVNLAYAYETKDALCLVLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTT 319
Cdd:cd05632  83 IMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGESIR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDV----AEMYDNILHKPLSLRPGVSLTAWSILEEL 395
Cdd:cd05632 162 GRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEkvkrEEVDRRVLETEEVYSAKFSEEAKSICKML 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 396 LEKDRQNRLGAKED-FLEIQNHPFFESLSWADLVQKKIPPPFNPN---VAGPD--DIRNFDT 451
Cdd:cd05632 242 LTKDPKQRLGCQEEgAGEVKRHPFFRNMNFKRLEAGMLDPPFVPDpraVYCKDvlDIEQFST 303
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
162-439 8.50e-58

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: 193.20  E-value: 8.50e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05607   4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEK-VNSPFIVSLAYAFETKTHLCLVMS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC---KEGiaisD 316
Cdd:cd05607  83 LMNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAvevKEG----K 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycRDVAEMYDNILHKPLSLRPGVSLTAWSILEE-- 394
Cdd:cd05607 159 PITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPF--RDHKEKVSKEELKRRTLEDEVKFEHQNFTEEak 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 395 -----LLEKDRQNRLGAKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPN 439
Cdd:cd05607 237 dicrlFLAKKPENRLGSRTNDDDPRKHEFFKSINFPRLEAGLIDPPFVPD 286
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
161-487 1.29e-57

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: 195.28  E-value: 1.29e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05627   3 DFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVE-ADGAWVVKMFYSFQDKRNLYLIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKeGIAISDTTTT 320
Cdd:cd05627  82 EFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCT-GLKKAHRTEF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 F------------------------------------CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCR 364
Cdd:cd05627 161 YrnlthnppsdfsfqnmnskrkaetwkknrrqlaystVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 365 DVAEMYDNILH--KPLSLRPGVSLTAWSilEELLEK---DRQNRLGAKeDFLEIQNHPFFESLSWADLVQKkiPPPFNPN 439
Cdd:cd05627 241 TPQETYRKVMNwkETLVFPPEVPISEKA--KDLILRfctDAENRIGSN-GVEEIKSHPFFEGVDWEHIRER--PAAIPIE 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 440 VAGPDDIRNFDTaFTEETV--PYSVCVSSDYSivnasvlEADDAFVGFSY 487
Cdd:cd05627 316 IKSIDDTSNFDD-FPESDIlqPAPNTTEPDYK-------SKDWVFLNYTY 357
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
158-487 1.79e-56

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: 193.30  E-value: 1.79e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd05622  71 KAEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIM-AFANSPWVVQLFYAFQDDRYLY 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC----KEGIA 313
Cdd:cd05622 150 MVMEYMPGGDLV-NLMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmnKEGMV 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTtfcGTPEYLAPEVIRKQP----YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVS 385
Cdd:cd05622 229 RCDTAV---GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTfpddNDIS 305
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 386 LTAWSILEELLeKDRQNRLGaKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFD----TAFTEETVPys 461
Cdd:cd05622 306 KEAKNLICAFL-TDREVRLG-RNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDdleeDKGEEETFP-- 381
                       330       340
                ....*....|....*....|....*.
gi 75813626 462 vcvssdysiVNASVLEADDAFVGFSY 487
Cdd:cd05622 382 ---------IPKAFVGNQLPFVGFTY 398
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
158-450 1.08e-55

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: 190.60  E-value: 1.08e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd05621  50 KAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIM-AFANSPWVVQLFCAFQDDKYLY 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC----KEGIA 313
Cdd:cd05621 129 MVMEYMPGGDLV-NLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCmkmdETGMV 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTtfcGTPEYLAPEVIRKQP----YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVS 385
Cdd:cd05621 208 HCDTAV---GTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMDHKNSLNfpddVEIS 284
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 386 LTAWSILEELLeKDRQNRLGaKEDFLEIQNHPFFESLSWADLVQKKIPPPFNPNVAGPDDIRNFD 450
Cdd:cd05621 285 KHAKNLICAFL-TDREVRLG-RNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFD 347
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
161-404 1.17e-55

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: 186.46  E-value: 1.17e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14663   1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIM-KLLRHPNIVELHEVMATKTKIFFVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC--KEGIAISDTT 318
Cdd:cd14663  80 ELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQDGLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLE 397
Cdd:cd14663 160 HTTCGTPNYVAPEVLARRGYDGAkADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILD 239

                ....*..
gi 75813626 398 KDRQNRL 404
Cdd:cd14663 240 PNPSTRI 246
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
166-419 2.39e-55

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: 185.80  E-value: 2.39e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMA-ERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAVK----EVELSGDSEEELEAlEREIrILSSLKHPNIVRYLGTERTENTLNIFLEYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGIAISDTTTTF 321
Cdd:cd06606  82 PGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGEGTKSL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYcrDVAEMYDNILH-----KPLSLRPGVSLTAWSILEELL 396
Cdd:cd06606 162 RGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWS--ELGNPVAALFKigssgEPPPIPEHLSEEAKDFLRKCL 239
                       250       260
                ....*....|....*....|...
gi 75813626 397 EKDRQNRLGAKEdFLeiqNHPFF 419
Cdd:cd06606 240 QRDPKKRPTADE-LL---QHPFL 258
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
161-455 1.14e-54

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: 186.02  E-value: 1.14e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLslVSTGDCPFIVCMSYAFHTPDKLSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT 318
Cdd:cd14223  81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTfcGTPEYLAPEVIRKQ-PYDNTVDWWCLGAVLYEMLYGLPPFY---CRDVAEMYDNILHKPLSLRPGVSLTAWSILEE 394
Cdd:cd14223 161 SV--GTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTMAVELPDSFSPELRSLLEG 238
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 395 LLEKDRQNRLGA-KEDFLEIQNHPFFESLSWADLVQKKIPPPFNP-----NVAGPDDIRNFDTAFTE 455
Cdd:cd14223 239 LLQRDVNRRLGCmGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPprgevNAADAFDIGSFDEEDTK 305
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
161-419 2.58e-54

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: 182.79  E-value: 2.58e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKV--LQKKivlnrKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKinLESK-----EKKESILNEIAIL-KKCKHPNIVKYYGSYLKKDELWI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDT 317
Cdd:cd05122  75 VMEFCSGGSLKDLLKnTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-LSDGKT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILHKPLSLRpgvSLTAWS-----I 391
Cdd:cd05122 154 RNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSeLPPMKALFLIATNGPPGLR---NPKKWSkefkdF 230
                       250       260
                ....*....|....*....|....*...
gi 75813626 392 LEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd05122 231 LKKCLQKDPEKRPTAE----QLLKHPFI 254
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
168-418 7.13e-54

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: 181.65  E-value: 7.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRK-KLNKKLQENLESEIAIL-KSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH---VVLTDFGLCKEgIAISDTTTTFCGT 324
Cdd:cd14009  79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDdpvLKIADFGFARS-LQPASMAETLCGS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI----LHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd14009 158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIersdAVIPFPIAAQLSPDCKDLLRRLLRRDP 237
                       250
                ....*....|....*...
gi 75813626 401 QNRLGakedFLEIQNHPF 418
Cdd:cd14009 238 AERIS----FEEFFAHPF 251
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
168-419 5.28e-53

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: 179.67  E-value: 5.28e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVK----------HPFLVGLH----YSFQtt 233
Cdd:cd14008   1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKRREGKNDRGKIKNALDDVRreiaimkkldHPNIVRLYevidDPES-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGGELFF--HLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEG 311
Cdd:cd14008  79 DKLYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 312 IAISDTTTTFCGTPEYLAPEVIRK--QPYD-NTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH--KPLSLRPGVSL 386
Cdd:cd14008 159 EDGNDTLQKTAGTPAFLAPELCDGdsKTYSgKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNqnDEFPIPPELSP 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 75813626 387 TAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd14008 239 ELKDLLRRMLEKDPEKRITLK----EIKEHPWV 267
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
165-450 5.65e-53

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: 183.32  E-value: 5.65e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd05625   6 IKTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAE-ADNEWVVRLYYSFQDKDNLYFVMDYIP 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC---------------- 308
Cdd:cd05625  85 GGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthdskyyqsgd 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 309 ---KEGIAIS----DTTTTFC------------------------GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG 357
Cdd:cd05625 165 hlrQDSMDFSnewgDPENCRCgdrlkplerraarqhqrclahslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVG 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 358 LPPFYCRDVAEM------YDNILHKPLSLRpgVSLTAWSILEELLeKDRQNRLGaKEDFLEIQNHPFFESLSW-ADLVQK 430
Cdd:cd05625 245 QPPFLAQTPLETqmkvinWQTSLHIPPQAK--LSPEASDLIIKLC-RGPEDRLG-KNGADEIKAHPFFKTIDFsSDLRQQ 320
                       330       340
                ....*....|....*....|
gi 75813626 431 kiPPPFNPNVAGPDDIRNFD 450
Cdd:cd05625 321 --SAPYIPKITHPTDTSNFD 338
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
161-487 1.06e-52

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: 182.55  E-value: 1.06e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05628   2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVE-ADSLWVVKMFYSFQDKLNLYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKeGIAISDTTTT 320
Cdd:cd05628  81 EFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCT-GLKKAHRTEF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 F------------------------------------CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCR 364
Cdd:cd05628 160 YrnlnhslpsdftfqnmnskrkaetwkrnrrqlafstVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 365 DVAEMYDNILH--KPLSLRPGVSLTAWSilEELLEK---DRQNRLGAKeDFLEIQNHPFFESLSWADLVQKkiPPPFNPN 439
Cdd:cd05628 240 TPQETYKKVMNwkETLIFPPEVPISEKA--KDLILRfccEWEHRIGAP-GVEEIKTNPFFEGVDWEHIRER--PAAIPIE 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 440 VAGPDDIRNFDtAFTEETVPYSVCVSSDYSivNASVLEADDAFVGFSY 487
Cdd:cd05628 315 IKSIDDTSNFD-EFPDSDILKPSVAVSNHP--ETDYKNKDWVFINYTY 359
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
156-455 1.70e-52

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: 181.03  E-value: 1.70e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 156 HAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTT 233
Cdd:cd05633   1 HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLslVSTGDCPFIVCMTYAFHTP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA 313
Cdd:cd05633  81 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTfcGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFY---CRDVAEMYDNILHKPLSLRPGVSLTAW 389
Cdd:cd05633 161 KKPHASV--GTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRqhkTKDKHEIDRMTLTVNVELPDSFSPELK 238
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 390 SILEELLEKDRQNRLGAK-EDFLEIQNHPFFESLSWADLVQKKIPPPFNP-----NVAGPDDIRNFDTAFTE 455
Cdd:cd05633 239 SLLEGLLQRDVSKRLGCHgRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPprgevNAADAFDIGSFDEEDTK 310
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
162-417 5.57e-52

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: 176.75  E-value: 5.57e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNrKEqkHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKG-KE--HMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFGLCKEgiaISDT 317
Cdd:cd14095  79 LVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLATE---VKEP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC--RDVAEMYDNILHKPLSLRP----GVSLTAWSI 391
Cdd:cd14095 156 LFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSpdRDQEELFDLILAGEFEFLSpywdNISDSAKDL 235
                       250       260
                ....*....|....*....|....*.
gi 75813626 392 LEELLEKDRQNRLGAKedflEIQNHP 417
Cdd:cd14095 236 ISRMLVVDPEKRYSAG----QVLDHP 257
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
164-419 7.28e-52

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: 176.60  E-value: 7.28e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLA--KRKLDGKFYAVKVLQKKIVlNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14080   4 LGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKA-PKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG-----LCKEGIAISD 316
Cdd:cd14080  83 YAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGfarlcPDDDGDVLSK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 tttTFCGTPEYLAPEVIRKQPYDNTV-DWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP---GVSLTAWSIL 392
Cdd:cd14080 163 ---TFCGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSsvkKLSPECKDLI 239
                       250       260
                ....*....|....*....|....*..
gi 75813626 393 EELLEKDRQNRLGAkedfLEIQNHPFF 419
Cdd:cd14080 240 DQLLEPDPTKRATI----EEILNHPWL 262
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
166-419 8.26e-52

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: 176.29  E-value: 8.26e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHImaERN-VLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd14081   7 KTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKV--EREiAIMKLIEHPNVLKLYDVYENKKYLYLVLEYVS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG---LCKEGIAISdtttTF 321
Cdd:cd14081  85 GGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGmasLQPEGSLLE----TS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd14081 161 CGSPHYACPEVIKGEKYDGrKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNP 240
                       250
                ....*....|....*....
gi 75813626 401 QNRLGAKedflEIQNHPFF 419
Cdd:cd14081 241 EKRITIE----EIKKHPWF 255
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
162-374 9.19e-51

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: 173.71  E-value: 9.19e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEqKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14083   5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKK-ALKGKE-DSLENEIAVL-RKIKHPNIVQLLDIYESKSHLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL---LDSVGHVVLTDFGLCKegIAISDTT 318
Cdd:cd14083  82 LVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--MEDSGVM 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL 374
Cdd:cd14083 160 STACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQIL 215
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
162-418 1.47e-49

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: 171.33  E-value: 1.47e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAernvLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14166   5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLENEIA----VLKRIKHENIVTLEDIYESTTHYYLVMQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLCKegIAISDTT 318
Cdd:cd14166  81 LVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--MEQNGIM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI------LHKPlsLRPGVSLTAWSIL 392
Cdd:cd14166 159 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIkegyyeFESP--FWDDISESAKDFI 236
                       250       260
                ....*....|....*....|....*.
gi 75813626 393 EELLEKDRQNRLGAKEDFleiqNHPF 418
Cdd:cd14166 237 RHLLEKNPSKRYTCEKAL----SHPW 258
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
166-419 2.07e-49

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: 170.04  E-value: 2.07e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14099   7 KFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIK-IHRSLKHPNIVKFHDCFEDEENVYILLELCSN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd14099  86 GSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLCGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVI-RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSL--RPGVSLTAWSILEELLEKDRQN 402
Cdd:cd14099 166 NYIAPEVLeKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFpsHLSISDEAKDLIRSMLQPDPTK 245
                       250
                ....*....|....*..
gi 75813626 403 RLGAKedflEIQNHPFF 419
Cdd:cd14099 246 RPSLD----EILSHPFF 258
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
162-403 2.45e-49

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: 170.21  E-value: 2.45e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKhiMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14167   5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKK-ALEGKETS--IENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL---LDSVGHVVLTDFGLCK-EGIAisDT 317
Cdd:cd14167  82 LVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKiEGSG--SV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILE 393
Cdd:cd14167 160 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywdDISDSAKDFIQ 239
                       250
                ....*....|
gi 75813626 394 ELLEKDRQNR 403
Cdd:cd14167 240 HLMEKDPEKR 249
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
162-365 2.31e-48

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: 167.18  E-value: 2.31e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSS-LNHPHIIRIYEVFENKDKIVIVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISDTT--T 319
Cdd:cd14073  82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSN---LYSKDKllQ 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPFYCRD 365
Cdd:cd14073 159 TFCGSPLYASPEIVNGTPYQGpEVDCWSLGVLLYTLVYGTMPFDGSD 205
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
161-419 3.49e-48

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: 166.95  E-value: 3.49e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLqKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSF--QTTEKLYF 238
Cdd:cd08217   1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEI-DYGKMSEKEKQQLVSEVN-ILRELKHPNIVRYYDRIvdRANTTLYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGEL---FFHLQRERSF-PEHRARFYAAEIASALGYLH-----SIKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd08217  79 VMEYCEGGDLaqlIKKCKKENQYiPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLAR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 EGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLS-LRPGVSLTA 388
Cdd:cd08217 159 VLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPrIPSRYSSEL 238
                       250       260       270
                ....*....|....*....|....*....|.
gi 75813626 389 WSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd08217 239 NEVIKSMLNVDPDKRPSVE----ELLQLPLI 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
161-374 7.26e-48

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: 166.03  E-value: 7.26e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAE-RnvLLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLG-SLSQKEREDSVNEiR--LLASVNHPNIIRYKEAFLDGNRLCIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQR----ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAIS 315
Cdd:cd08530  78 MEYAPFGDLSKLISKrkkkRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--VLKK 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL 374
Cdd:cd08530 156 NLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVC 214
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
161-418 1.55e-47

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: 165.13  E-value: 1.55e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14116   6 DFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKA-QLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLIL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiAISDTTTT 320
Cdd:cd14116  85 EYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVH--APSSRRTT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd14116 163 LCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNP 242
                       250
                ....*....|....*...
gi 75813626 401 QNRLGAKedflEIQNHPF 418
Cdd:cd14116 243 SQRPMLR----EVLEHPW 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
166-417 1.80e-47

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 165.64  E-value: 1.80e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvLNRKEQKHIMAERNVL-----LKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14084  12 RTLGSGACGEVKLAYDKSTCKKVAIKIINKRK-FTIGSRREINKPRNIEteieiLKKLSHPCIIKIEDFFDAEDDYYIVL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH---VVLTDFGLCKegiaISDT 317
Cdd:cd14084  91 ELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSK----ILGE 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TT---TFCGTPEYLAPEVIR---KQPYDNTVDWWCLGAVLYEMLYGLPPF--YCRDVaEMYDNILHKPLSLRP----GVS 385
Cdd:cd14084 167 TSlmkTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFseEYTQM-SLKEQILSGKYTFIPkawkNVS 245
                       250       260       270
                ....*....|....*....|....*....|..
gi 75813626 386 LTAWSILEELLEKDRQNRLGAKedflEIQNHP 417
Cdd:cd14084 246 EEAKDLVKKMLVVDPSRRPSIE----EALEHP 273
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
162-406 3.73e-47

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: 164.24  E-value: 3.73e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETK----CRGREVCESELNVL-RRVRHTNIIQLIEVFETKERVYMVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH---VVLTDFGLCKEGIAISDTT 318
Cdd:cd14087  78 LATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTRKKGPNCL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 -TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSILE 393
Cdd:cd14087 158 mKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSgepwPSVSNLAKDFID 237
                       250
                ....*....|...
gi 75813626 394 ELLEKDRQNRLGA 406
Cdd:cd14087 238 RLLTVNPGERLSA 250
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
161-418 1.27e-45

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 160.33  E-value: 1.27e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQK-KIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKrKVAGNDKNLQLFQREINIL-KSLEHPGIVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG--HVVLTDFGLCKEgIAISDT 317
Cdd:cd14098  80 MEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKV-IHTGTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQP------YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI----LHKPLSLRPGVSLT 387
Cdd:cd14098 159 LVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIrkgrYTQPPLVDFNISEE 238
                       250       260       270
                ....*....|....*....|....*....|.
gi 75813626 388 AWSILEELLEKDRQNRLGAkedfLEIQNHPF 418
Cdd:cd14098 239 AIDFILRLLDVDPEKRMTA----AQALDHPW 265
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
168-418 1.67e-45

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: 159.38  E-value: 1.67e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFY-AVKVLQKKiVLNRKEQKHIMAERNvLLKNVKHPFLVGLHySFQTTEK-LYFVLDFVNG 245
Cdd:cd14121   3 LGSGTYATVYKAYRKSGAREVvAVKCVSKS-SLNKASTENLLTEIE-LLKKLKHPHIVELK-DFQWDEEhIYLIMEYCSG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVL--TDFGLCKEgIAISDTTTTFCG 323
Cdd:cd14121  80 GDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLklADFGFAQH-LKPNDEAHSLRG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL-HKPLSL--RPGVSLTAWSILEELLEKDR 400
Cdd:cd14121 159 SPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRsSKPIEIptRPELSADCRDLLLRLLQRDP 238
                       250
                ....*....|....*...
gi 75813626 401 QNRLGAKEDFleiqNHPF 418
Cdd:cd14121 239 DRRISFEEFF----AHPF 252
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
167-419 1.68e-45

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: 160.21  E-value: 1.68e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVKVLQK---KIVLNRKE--QKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14093  10 ILGRGVSSTVRRCIEKETGQEFAVKIIDItgeKSSENEAEelREATRREIEILRQVSGHPNIIELHDVFESPTFIFLVFE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTF 321
Cdd:cd14093  90 LCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR-LDEGEKLREL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNT------VDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSI 391
Cdd:cd14093 169 CGTPGYLAPEVLKCSMYDNApgygkeVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGSpewdDISDTAKDL 248
                       250       260
                ....*....|....*....|....*...
gi 75813626 392 LEELLEKDRQNRLGAKEDfLEiqnHPFF 419
Cdd:cd14093 249 ISKLLVVDPKKRLTAEEA-LE---HPFF 272
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
161-418 4.51e-45

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: 159.51  E-value: 4.51e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHimaERNV-LLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14086   2 EYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKL---EREArICRLLKHPNIVRLHDSISEEGFHYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV---GHVVLTDFGLckeGIAISD 316
Cdd:cd14086  79 FDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKskgAAVKLADFGL---AIEVQG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTT---FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAW 389
Cdd:cd14086 156 DQQAwfgFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAK 235
                       250       260
                ....*....|....*....|....*....
gi 75813626 390 SILEELLEKDRQNRLGAKEDFleiqNHPF 418
Cdd:cd14086 236 DLINQMLTVNPAKRITAAEAL----KHPW 260
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
162-417 6.76e-45

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: 157.93  E-value: 6.76e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIV---LNRKeQKHIMAernvlLKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALgddLPRV-KTEIEA-----LKNLSHQHICRLYHVIETDNKIFM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC-KEGIAISDT 317
Cdd:cd14078  79 VLEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCaKPKGGMDHH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPY-DNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL----HKPLSLRPGVSLtawsIL 392
Cdd:cd14078 159 LETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQsgkyEEPEWLSPSSKL----LL 234
                       250       260
                ....*....|....*....|....*
gi 75813626 393 EELLEKDRQNRLGAKedflEIQNHP 417
Cdd:cd14078 235 DQMLQVDPKKRITVK----ELLNHP 255
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
160-418 1.71e-44

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: 158.37  E-value: 1.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLA-KRKLDGKFYAVKVLQKK----IVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTE 234
Cdd:cd14096   1 ENYRLINKIGEGAFSNVYKAvPLRNTGKPVAIKVVRKAdlssDNLKGSSRANILKEVQ-IMKRLSHPNIVKLLDFQESDE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS------------------ 296
Cdd:cd14096  80 YYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfipsivklrkadddet 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 297 ---------------VGHVVLTDFGLCKegIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14096 160 kvdegefipgvggggIGIVKLADFGLSK--QVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 362 YCRDVAEMYDNILHKPLS-LRP---GVSLTAWSILEELLEKDRQNRLgakeDFLEIQNHPF 418
Cdd:cd14096 238 YDESIETLTEKISRGDYTfLSPwwdEISKSAKDLISHLLTVDPAKRY----DIDEFLAHPW 294
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
168-418 1.71e-44

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


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 157.46  E-value: 1.71e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnrkeQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14010   8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKS-------KRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGL-CKEGIAISDTTTTFC---- 322
Cdd:cd14010  81 LETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLaRREGEILKELFGQFSdegn 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 -----------GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK-PLSLRPGVSLTA-- 388
Cdd:cd14010 161 vnkvskkqakrGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEdPPPPPPKVSSKPsp 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 75813626 389 --WSILEELLEKDRQNRLgakeDFLEIQNHPF 418
Cdd:cd14010 241 dfKSLLKGLLEKDPAKRL----SWDELVKHPF 268
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
168-361 1.95e-43

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: 153.85  E-value: 1.95e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKrkLDGKFYAVKVLQKKIVLNRKEQkhiMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd13999   1 IGSGSFGEVYKGK--WRGTDVAIKKLKVEDDNDELLK---EFRREVsILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd13999  76 SLYDLLHkKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTP 155
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd13999 156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPF 191
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
168-419 2.08e-43

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: 153.92  E-value: 2.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQ---KHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd06627   8 IGRGAFGSVYKGLNLNTGEFVAIK----QISLEKIPKsdlKSVMGEID-LLKKLNHPNIVKYIGSVKTKDSLYIILEYVE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd06627  83 NGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENSVVGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD-VAEMYdNIL---HKPLSlrPGVSLTAWSILEELLEKDR 400
Cdd:cd06627 163 PYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQpMAALF-RIVqddHPPLP--ENISPELRDFLLQCFQKDP 239
                       250
                ....*....|....*....
gi 75813626 401 QNRLGAKedflEIQNHPFF 419
Cdd:cd06627 240 TLRPSAK----ELLKHPWL 254
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
162-420 3.20e-43

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: 153.52  E-value: 3.20e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERnVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRATGKEVAIK----KMRLRKQNKELIINEI-LIMKECKHPNIVDYYDSYLVGDELWVVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHL-QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd06614  77 YMDGGSLTDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKSKRNS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPfYCRDVAE--MY---DNILHkPLSLRPGVSLTAWSILEEL 395
Cdd:cd06614 157 VVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPP-YLEEPPLraLFlitTKGIP-PLKNPEKWSPEFKDFLNKC 234
                       250       260
                ....*....|....*....|....*
gi 75813626 396 LEKDRQNRLGAKedflEIQNHPFFE 420
Cdd:cd06614 235 LVKDPEKRPSAE----ELLQHPFLK 255
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
168-408 8.31e-43

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: 153.12  E-value: 8.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQkhiMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14169  11 LGEGAFSEVVLAQERGSQRLVALKCIPKK-ALRGKEA---MVENEIaVLRRINHENIVSLEDIYESPTHLYLAMELVTGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV---GHVVLTDFGLCKegIAISDTTTTFCG 323
Cdd:cd14169  87 ELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfedSKIMISDFGLSK--IEAQGMLSTACG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILEELLEKD 399
Cdd:cd14169 165 TPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSpywdDISESAKDFIRHLLERD 244

                ....*....
gi 75813626 400 RQNRLGAKE 408
Cdd:cd14169 245 PEKRFTCEQ 253
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
162-403 1.47e-42

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: 153.28  E-value: 1.47e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVlnrKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14168  12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKAL---KGKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLCK-EGIAisDT 317
Cdd:cd14168  89 LVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKmEGKG--DV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILE 393
Cdd:cd14168 167 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSpywdDISDSAKDFIR 246
                       250
                ....*....|
gi 75813626 394 ELLEKDRQNR 403
Cdd:cd14168 247 NLMEKDPNKR 256
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
161-435 1.51e-42

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: 152.33  E-value: 1.51e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14117   7 DFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKS-QIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiAISDTTTT 320
Cdd:cd14117  86 EYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVH--APSLRRRT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDR 400
Cdd:cd14117 164 MCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHP 243
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75813626 401 QNRLGAKedflEIQNHPffeslsWADLVQKKIPPP 435
Cdd:cd14117 244 SERLPLK----GVMEHP------WVKANSRRVLPP 268
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
161-418 1.86e-42

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: 151.59  E-value: 1.86e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd06623   2 DLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIH--VDGDEEFRKQLLRELKTLRS-CESPYVVKCYGAFYKEGEISIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSI-KIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd06623  79 EYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY---CRDVAEMYDNILHKPL-SLRPG-VSLTAWSILEE 394
Cdd:cd06623 159 TFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLppgQPSFFELMQAICDGPPpSLPAEeFSPEFRDFISA 238
                       250       260
                ....*....|....*....|....
gi 75813626 395 LLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd06623 239 CLQKDPKKRPSAA----ELLQHPF 258
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
166-419 2.15e-42

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: 151.27  E-value: 2.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14079   8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQ-ILKLFRHPHIIRLYEVIETPTDIFMVMEYVSG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC---KEGiaisDTTTTFC 322
Cdd:cd14079  87 GELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSnimRDG----EFLKTSC 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQ 401
Cdd:cd14079 163 GSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPL 242
                       250
                ....*....|....*...
gi 75813626 402 NRLGAKedflEIQNHPFF 419
Cdd:cd14079 243 KRITIP----EIRQHPWF 256
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
162-408 6.52e-42

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: 150.39  E-value: 6.52e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhiMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVK---LLEREVdILKHVNHAHIIHLEEVFETPKRMYLVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG-------HVVLTDFGLC--KEG 311
Cdd:cd14097  80 ELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIidnndklNIKVTDFGLSvqKYG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 312 IAISDTTTTfCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGV----SLT 387
Cdd:cd14097 160 LGEDMLQET-CGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVwqsvSDA 238
                       250       260
                ....*....|....*....|.
gi 75813626 388 AWSILEELLEKDRQNRLGAKE 408
Cdd:cd14097 239 AKNVLQQLLKVDPAHRMTASE 259
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
166-418 8.59e-42

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: 149.86  E-value: 8.59e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLqkKIVLNRKEQKHIMA--ERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDTGDFFAVKEV--SLVDDDKKSRESVKqlEQEIaLLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTFC 322
Cdd:cd06632  84 VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKH-VEAFSFAKSFK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQ--PYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILHKPLSLRP-GVSLTAWSILEELLEK 398
Cdd:cd06632 163 GSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSqYEGVAAIFKIGNSGELPPIPdHLSPDAKDFIRLCLQR 242
                       250       260
                ....*....|....*....|
gi 75813626 399 DRQNRLGAKedflEIQNHPF 418
Cdd:cd06632 243 DPEDRPTAS----QLLEHPF 258
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
162-374 9.19e-42

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: 149.59  E-value: 9.19e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14072   2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKT-QLNPSSLQKLFREVRIM-KILNHPNIVKLFEVIETEKTLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTF 321
Cdd:cd14072  80 YASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE-FTPGNKLDTF 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75813626 322 CGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL 374
Cdd:cd14072 159 CGSPPYAAPELFQGKKYDGpEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVL 212
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
161-419 1.14e-41

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: 149.40  E-value: 1.14e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14069   2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMK--RAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC-------KEGIa 313
Cdd:cd14069  80 EYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfrykgKERL- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 isdtTTTFCGTPEYLAPEVIRKQPYD-NTVDWWCLGAVLYEMLYG-LPPFYCRDVAEMY-DNILHKPLSLRP--GVSLTA 388
Cdd:cd14069 159 ----LNKMCGTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLAGeLPWDQPSDSCQEYsDWKENKKTYLTPwkKIDTAA 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 75813626 389 WSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd14069 235 LSLLRKILTENPNKRITIE----DIKKHPWY 261
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
161-361 1.18e-41

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: 149.48  E-value: 1.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKV--LQKkivLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQidISR---MSRKMREEAIDEARVLSK-LNSPYVIKYYDSFVDKGKLNI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGEL--FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISD 316
Cdd:cd08529  77 VMEYAENGDLhsLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTN 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd08529 157 FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPF 201
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
165-419 1.35e-41

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 149.62  E-value: 1.35e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  165 LKVIgKGSFGKVLLAKRKLDGKFYavkvLQKKIvlnrkEQKHIMA-ERNV--LLKNvkHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:PHA03390  22 LKLI-DGKFGKVSVLKHKPTQKLF----VQKII-----KAKNFNAiEPMVhqLMKD--NPNFIKLYYSVTTLKGHVLIMD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD-SVGHVVLTDFGLCKegiaISDTTTT 320
Cdd:PHA03390  90 YIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCK----IIGTPSC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYcRDVAEMYD-----NILHKPLSLRPGVSLTAWSILEEL 395
Cdd:PHA03390 166 YDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK-EDEDEELDlesllKRQQKKLPFIKNVSKNANDFVQSM 244
                        250       260
                 ....*....|....*....|....
gi 75813626  396 LEKDRQNRLgakEDFLEIQNHPFF 419
Cdd:PHA03390 245 LKYNINYRL---TNYNEIIKHPFL 265
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
166-361 2.20e-41

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: 148.60  E-value: 2.20e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14162   6 KTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVI-KGLKHPNLICFYEAIETTSRVYIIMELAEN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT----TTTF 321
Cdd:cd14162  85 GDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTKDGkpklSETY 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTV-DWWCLGAVLYEMLYGLPPF 361
Cdd:cd14162 165 CGSYAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPF 205
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
162-403 4.54e-41

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: 147.80  E-value: 4.54e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERN--VLLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIK----EIDLTKMPVKEKEASKKevILLAKMKHPNIVTFFASFQENGRLFIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERS--FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVV-LTDFGLCKEgiaISD 316
Cdd:cd08225  78 MEYCDGGDLMKRINRQRGvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVAkLGDFGIARQ---LND 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTT---TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH---KPLSlrPGVSLTAWS 390
Cdd:cd08225 155 SMElayTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQgyfAPIS--PNFSRDLRS 232
                       250
                ....*....|...
gi 75813626 391 ILEELLEKDRQNR 403
Cdd:cd08225 233 LISQLFKVSPRDR 245
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
168-408 4.77e-41

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: 147.87  E-value: 4.77e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKhiMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14075  10 LGSGNFSQVKLGIHQLTKEKVAIKILDKT-KLDQKTQR--LLSREIsSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG---LCKEGiaisDTTTTFCG 323
Cdd:cd14075  87 ELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGfstHAKRG----ETLNTFCG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQN 402
Cdd:cd14075 163 SPPYAAPELFKDEHYIGIyVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPVPSD 242

                ....*.
gi 75813626 403 RLGAKE 408
Cdd:cd14075 243 RYSIDE 248
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
167-418 6.42e-41

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: 148.33  E-value: 6.42e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEqkhIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14090   9 LLGEGAYASVQTCINLYTGKEYAVKIIEKHPGHSRSR---VFREVETLHQCQGHPNILQLIEYFEDDERFYLVFEKMRGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL---LDSVGHVVLTDFGL---CKEGIAISDTTTT 320
Cdd:cd14090  86 PLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLgsgIKLSSTSMTPVTT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 -----FCGTPEYLAPEVI-----RKQPYDNTVDWWCLGAVLYEMLYGLPPFY--------------CRDVAEMydnILHk 376
Cdd:cd14090 166 pelltPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYgrcgedcgwdrgeaCQDCQEL---LFH- 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 75813626 377 plSLRPG-----------VSLTAWSILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14090 242 --SIQEGeyefpekewshISAEAKDLISHLLVRDASQRYTAE----QVLQHPW 288
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
168-417 1.79e-40

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


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 145.87  E-value: 1.79e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAAKFIPKR----DKKKEAVLREISIL-NQLQHPRIIQLHEAYESPTELVLILELCSGGE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG--HVVLTDFGLCKEgIAISDTTTTFCGTP 325
Cdd:cd14006  76 LLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARK-LNPGEELKEIFGTP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILEELLEKDRQ 401
Cdd:cd14006 155 EFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFSEeyfsSVSQEAKDFIRKLLVKEPR 234
                       250
                ....*....|....*.
gi 75813626 402 NRLGAkEDFLEiqnHP 417
Cdd:cd14006 235 KRPTA-QEALQ---HP 246
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
165-355 2.83e-40

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: 145.72  E-value: 2.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNR---KEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd08218   5 IKKIGEGSFGKALLVKSKEDGKQYVIK----EINISKmspKEREESRKEVAVL-SKMKHPNIVQYQESFEENGNLYIVMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELF--FHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd08218  80 YCDGGDLYkrINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELAR 159
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd08218 160 TCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMC 195
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
166-418 4.27e-40

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: 145.48  E-value: 4.27e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlNRKEQKHIMAERNVLL-KNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd14185   6 RTIGDGNFAVVKECRHWNENQEYAMKIIDK----SKLKGKEDMIESEILIiKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFGLCKEgiaISDTTTT 320
Cdd:cd14185  82 GGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKY---VTGPIFT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC--RDVAEMYDNILHKPLSLRP----GVSLTAWSILEE 394
Cdd:cd14185 159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpeRDQEELFQIIQLGHYEFLPpywdNISEAAKDLISR 238
                       250       260
                ....*....|....*....|....
gi 75813626 395 LLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14185 239 LLVVDPEKRYTAK----QVLQHPW 258
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
162-418 1.21e-39

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: 144.09  E-value: 1.21e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkIVLNRKEQKHIMAERnVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDK-TKLDDVSKAHLFQEV-RCMKLVQHPNVVRLYEVIDTQTKLYLILE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQR-ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-DSVGHVVLTDFGLCKEGIAiSDTTT 319
Cdd:cd14074  83 LGDGGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQP-GEKLE 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEK 398
Cdd:cd14074 162 TSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIR 241
                       250       260
                ....*....|....*....|
gi 75813626 399 DRQNRLGAKedflEIQNHPF 418
Cdd:cd14074 242 DPKKRASLE----EIENHPW 257
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
165-418 1.25e-39

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: 144.55  E-value: 1.25e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLL-----AKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14076   6 GRTLGEGEFGKVKLgwplpKANHRSGVQVAIKLIRRDTQQENCQTSKIMREINIL-KGLTHPNIVRLLDVLKTKKYIGIV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GIAISDTT 318
Cdd:cd14076  85 LEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDLM 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTFCGTPEYLAPE-VIRKQPYDNT-VDWWCLGAVLYEMLYGLPPF-------YCRDVAEMYDNILHKPLSLRPGVSLTAW 389
Cdd:cd14076 165 STSCGSPCYAAPElVVSDSMYAGRkADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKAR 244
                       250       260
                ....*....|....*....|....*....
gi 75813626 390 SILEELLEKDRQNRLgakeDFLEIQNHPF 418
Cdd:cd14076 245 DLLRRILVPNPRKRI----RLSAIMRHAW 269
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
162-392 2.10e-39

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: 143.56  E-value: 2.10e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAkRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14161   5 YEFLETLGKGTYGRVKKA-RDSSGRLVAIKSIRKDRIKDEQDLLHIRREIEIM-SSLNHPHIISVYEVFENSSKIVIVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLckEGIAISDT-TTT 320
Cdd:cd14161  83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGL--SNLYNQDKfLQT 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 321 FCGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPFYCRD----VAEMYDNILHKPLSLRPGVSLTAWSIL 392
Cdd:cd14161 161 YCGSPLYASPEIVNGRPYIGpEVDSWSLGVLLYILVHGTMPFDGHDykilVKQISSGAYREPTKPSDACGLIRWLLM 237
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
166-419 2.56e-39

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: 143.65  E-value: 2.56e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnRKEQ---KHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd14106  14 TPLGRGKFAVVRKCIHKETGKEYAAKFLRKR----RRGQdcrNEILHEIAVLELCKDCPRVVNLHEVYETRSELILILEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV---GHVVLTDFGLCK---EGIAISD 316
Cdd:cd14106  90 AAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplGDIKLCDFGISRvigEGEEIRE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 ttttFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI----LHKPLSLRPGVSLTAWSIL 392
Cdd:cd14106 170 ----ILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNIsqcnLDFPEELFKDVSPLAIDFI 245
                       250       260
                ....*....|....*....|....*..
gi 75813626 393 EELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd14106 246 KRLLVKDPEKRLTAK----ECLEHPWL 268
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
161-438 6.08e-39

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: 143.16  E-value: 6.08e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlnrkEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14091   1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDK-------SKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH----VVLTDFGLCKEGIAISD 316
Cdd:cd14091  74 ELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFAKQLRAENG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC--RDVAEMydnILHK----PLSLRPG----VSL 386
Cdd:cd14091 154 LLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASgpNDTPEV---ILARigsgKIDLSGGnwdhVSD 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 387 TAWSILEELLEKDRQNRLGAKedflEIQNHPFFesLSWADLVQKKIPPPFNP 438
Cdd:cd14091 231 SAKDLVRKMLHVDPSQRPTAA----QVLQHPWI--RNRDSLPQRQLTDPQDA 276
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
166-418 1.32e-38

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: 141.32  E-value: 1.32e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKeqkHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14184   7 KVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKE---HLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFGLckeGIAISDTTTTF 321
Cdd:cd14184  84 GDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGL---ATVVEGPLYTV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD--VAEMYDNI----LHKPLSLRPGVSLTAWSILEEL 395
Cdd:cd14184 161 CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQIllgkLEFPSPYWDNITDSAKELISHM 240
                       250       260
                ....*....|....*....|...
gi 75813626 396 LEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14184 241 LQVNVEARYTAE----QILSHPW 259
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
165-419 2.59e-38

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 140.06  E-value: 2.59e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSF--QTTEKLYFVLDF 242
Cdd:cd05118   4 LRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKAALREIKLLKH-LNDVEGHPNIVKLLDVFehRGGNHLCLVFEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VngGELFFHLQRERS--FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV-GHVVLTDFGLCKegIAISDTTT 319
Cdd:cd05118  83 M--GMNLYELIKDYPrgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLAR--SFTSPPYT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVI-RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD----VAEMYDnILHKPLSLrpgvsltawSILEE 394
Cdd:cd05118 159 PYVATRWYRAPEVLlGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSevdqLAKIVR-LLGTPEAL---------DLLSK 228
                       250       260
                ....*....|....*....|....*
gi 75813626 395 LLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd05118 229 MLKYDPAKRITAS----QALAHPYF 249
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
161-418 6.81e-38

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: 139.50  E-value: 6.81e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAE----------RNVLLKNV-KHPFLVGLHYS 229
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEkeisrdirtiREAALSSLlNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 230 FQTTEKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 egiaISDTTT---TFCGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVS 385
Cdd:cd14077 162 ----LYDPRRllrTFCGSLYFAAPELLQAQPYTGpEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLS 237
                       250       260       270
                ....*....|....*....|....*....|...
gi 75813626 386 LTAWSILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14077 238 SECKSLISRMLVVDPKKRATLE----QVLNHPW 266
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
161-420 1.23e-37

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: 138.99  E-value: 1.23e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKF-YAVKVLQKKivlNRKEQKHIMAERNVLLKNVKHPFLVGLhYSFQT-TEKLYF 238
Cdd:cd14202   3 EFSRKDLIGHGAFAVVFKGRHKEKHDLeVAVKCINKK---NLAKSQTLLGKEIKILKELKHENIVAL-YDFQEiANSVYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG---------HVVLTDFGLCK 309
Cdd:cd14202  79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFAR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 EgIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC---RDVAEMYDnilhKPLSLRPGVSL 386
Cdd:cd14202 159 Y-LQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQAsspQDLRLFYE----KNKSLSPNIPR 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75813626 387 TAWSILEE----LLEKDRQNRLgakeDFLEIQNHPFFE 420
Cdd:cd14202 234 ETSSHLRQlllgLLQRNQKDRM----DFDEFFHHPFLD 267
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
161-419 2.55e-37

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: 137.86  E-value: 2.55e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvlNRKEQKHIMAERNVLLKNVKhPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd06605   2 DLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEI--DEALQKQILRELDVLHKCNS-PYIVGFYGAFYSEGDISICM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHS-IKIVYRDLKPENILLDSVGHVVLTDFGLckEGIAISDTTT 319
Cdd:cd06605  79 EYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGV--SGQLVDSLAK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG---LPPFYCRD---VAEMYDNILHKPLSLRPG--VSLTAWSI 391
Cdd:cd06605 157 TFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGrfpYPPPNAKPsmmIFELLSYIVDEPPPLLPSgkFSPDFQDF 236
                       250       260
                ....*....|....*....|....*...
gi 75813626 392 LEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd06605 237 VSQCLQKDPTERPSYK----ELMEHPFI 260
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
162-419 1.21e-36

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: 136.64  E-value: 1.21e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQ---KKIVLNR-KEQKHIMAERNVLLKNVK-HPFLVGLHYSFQTTEKL 236
Cdd:cd14181  12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaERLSPEQlEEVRSSTLKEIHILRQVSgHPSIITLIDSYESSTFI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGL-CKegIAIS 315
Cdd:cd14181  92 FLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFsCH--LEPG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTTFCGTPEYLAPEVIR------KQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVS 385
Cdd:cd14181 170 EKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFSSpewdDRS 249
                       250       260       270
                ....*....|....*....|....*....|....
gi 75813626 386 LTAWSILEELLEKDRQNRLGAKEDFleiqNHPFF 419
Cdd:cd14181 250 STVKDLISRLLVVDPEIRLTAEQAL----QHPFF 279
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
162-408 1.41e-36

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: 135.92  E-value: 1.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvlNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14088   3 YDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRD--GRKVRKAAKNEINIL-KMVKHPNILQLVDVFETRKEYFIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGH--VVLTDFGLCK-EGIAISDT 317
Cdd:cd14088  80 LATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyYNRLKNskIVISDFHLAKlENGLIKEP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 tttfCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDN--------ILHKPLSLRP----GVS 385
Cdd:cd14088 160 ----CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENhdknlfrkILAGDYEFDSpywdDIS 235
                       250       260
                ....*....|....*....|...
gi 75813626 386 LTAWSILEELLEKDRQNRLGAKE 408
Cdd:cd14088 236 QAAKDLVTRLMEVEQDQRITAEE 258
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
166-419 1.43e-36

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: 135.95  E-value: 1.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkIVLNRKEQKHIMA-ERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd06625   6 KLLGQGAFGQVYLCYDADTGRELAVKQVEI-DPINTEASKEVKAlECEIqLLKNLQHERIVQYYGCLQDEKSLSIFMEYM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGIAISDTTTTF 321
Cdd:cd06625  85 PGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSSTGMKSV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYdNILHKPLS--LRPGVSLTAWSILEELLEK 398
Cdd:cd06625 165 TGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAeFEPMAAIF-KIATQPTNpqLPPHVSEDARDFLSLIFVR 243
                       250       260
                ....*....|....*....|.
gi 75813626 399 DRQNRLGAkedfLEIQNHPFF 419
Cdd:cd06625 244 NKKQRPSA----EELLSHSFV 260
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
162-361 4.18e-36

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: 134.44  E-value: 4.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKS-QLDEENLKKIYREVQIM-KMLNHPHIIKLYQVMETKDMLYLVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG---LCKEGiaisDTT 318
Cdd:cd14071  80 YASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGfsnFFKPG----ELL 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14071 156 KTWCGSPPYAAPEVFEGKEYEGpQLDIWSLGVVLYVLVCGALPF 199
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
166-408 4.80e-36

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: 134.56  E-value: 4.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKK-------IVLNRKEQKHIMaernvllKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd14070   8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKkakkdsyVTKNLRREGRIQ-------QMIRHPNITQLLDILETENSYYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGL--CKEGIAISD 316
Cdd:cd14070  81 VMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLsnCAGILGYSD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCR--DVAEMYDNILHKPLS-LRPGVSLTAWSILE 393
Cdd:cd14070 161 PFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEpfSLRALHQKMVDKEMNpLPTDLSPGAISFLR 240
                       250
                ....*....|....*
gi 75813626 394 ELLEKDRQNRLGAKE 408
Cdd:cd14070 241 SLLEPDPLKRPNIKQ 255
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
160-362 5.08e-36

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 134.32  E-value: 5.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkiVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKV-----VPVEEDLQEIIKEIS-ILKQCDSPYIVKYYGSYFKNTDLWIV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQ-RERSFPEhrarfyaAEIAS-------ALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEG 311
Cdd:cd06612  77 MEYCGAGSVSDIMKiTNKTLTE-------EEIAAilyqtlkGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 312 IAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd06612 150 TDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYS 200
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
161-420 5.58e-36

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: 134.75  E-value: 5.58e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLK--VIGKGSFGKVLLAK-RKLDGKFYAVKVLQKKivlNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd14201   5 DFEYSRkdLVGHGAFAVVFKGRhRKKTDWEVAIKSINKK---NLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG---------HVVLTDFGLC 308
Cdd:cd14201  82 LVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 309 KEgIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC---RDVAEMYDnilhKPLSLRPGV- 384
Cdd:cd14201 162 RY-LQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQAnspQDLRMFYE----KNKNLQPSIp 236
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 75813626 385 ---SLTAWSILEELLEKDRQNRLgakeDFLEIQNHPFFE 420
Cdd:cd14201 237 retSPYLADLLLGLLQRNQKDRM----DFEAFFSHPFLE 271
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
168-418 6.05e-36

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: 134.03  E-value: 6.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAK-RKLDGKFYAVKVLQKKivlNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14120   1 IGHGAFAVVFKGRhRKKPDLPVAIKCITKK---NLSKSQNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG---------HVVLTDFGLCK--EGiaiS 315
Cdd:cd14120  78 DLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARflQD---G 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMyDNILHKPLSLRP----GVSLTAWSI 391
Cdd:cd14120 155 MMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQEL-KAFYEKNANLRPnipsGTSPALKDL 233
                       250       260
                ....*....|....*....|....*..
gi 75813626 392 LEELLEKDRQNRLgakeDFLEIQNHPF 418
Cdd:cd14120 234 LLGLLKRNPKDRI----DFEDFFSHPF 256
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
162-418 6.08e-36

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: 133.96  E-value: 6.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVllknvKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14665   2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKIDENVQREIINHRSL-----RHPNIVRFKEVILTPTHLAIVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD--SVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd14665  77 YAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSKSSVLHSQPKS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TfCGTPEYLAPEVIRKQPYDNTV-DWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPG------VSLTAWSIL 392
Cdd:cd14665 157 T-VGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDPEEPRNFRKTIQRILSVQYSipdyvhISPECRHLI 235
                       250       260
                ....*....|....*....|....*.
gi 75813626 393 EELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14665 236 SRIFVADPATRITIP----EIRNHEW 257
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
152-419 6.45e-36

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: 134.11  E-value: 6.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 152 SGNPHAKPTDFdflKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQ 231
Cdd:cd06648   2 PGDPRSDLDNF---VKIGEGSTGIVCIATDKSTGRQVAVK----KMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 232 TTEKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAeIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEg 311
Cdd:cd06648  75 VGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCRA-VLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQ- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 312 iaISDTT---TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL-HKPLSLR--PGVS 385
Cdd:cd06648 153 --VSKEVprrKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRdNEPPKLKnlHKVS 230
                       250       260       270
                ....*....|....*....|....*....|....
gi 75813626 386 LTAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd06648 231 PRLRSFLDRMLVRDPAQRATAA----ELLNHPFL 260
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
159-423 6.48e-36

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: 134.49  E-value: 6.48e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDF-DFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd06611   3 PNDIwEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE---SEEELEDFMVEIDIL-SECKHPNIVGLYEAYFYENKLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGEL-FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISD 316
Cdd:cd06611  79 ILIEFCDGGALdSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVI-----RKQPYDNTVDWWCLGAVLYEMLYGLPPFYcrDVAEMydNILHKPLSLRPGVSLTA--W 389
Cdd:cd06611 159 KRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHH--ELNPM--RVLLKILKSEPPTLDQPskW 234
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 75813626 390 S-----ILEELLEKDRQNRLGAKedflEIQNHPFFESLS 423
Cdd:cd06611 235 SssfndFLKSCLVKDPDDRPTAA----ELLKHPFVSDQS 269
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
162-408 6.56e-36

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: 134.95  E-value: 6.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvlnrkEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTV-----DKKIVRTEIGVLLR-LSHPNIIKLKEIFETPTEISLVLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH---VVLTDFGLCKegiaISD-- 316
Cdd:cd14085  79 LVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSK----IVDqq 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 -TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC-RDVAEMYDNILHKPLS-LRP---GVSLTAWS 390
Cdd:cd14085 155 vTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDeRGDQYMFKRILNCDYDfVSPwwdDVSLNAKD 234
                       250
                ....*....|....*...
gi 75813626 391 ILEELLEKDRQNRLGAKE 408
Cdd:cd14085 235 LVKKLIVLDPKKRLTTQQ 252
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
161-419 2.16e-35

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: 132.43  E-value: 2.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkIVLNRKE-----QKHIMaernvLLKNVKHPFLVGLHYSFQTTEK 235
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATGELAAVKV----IKLEPGDdfeiiQQEIS-----MLKECRHPNIVAYFGSYLRRDK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAIS 315
Cdd:cd06613  72 LWIVMEYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPfycrdvaeMYDniLHK-------PLSLRPGVS 385
Cdd:cd06613 152 AKRKSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPP--------MFD--LHPmralfliPKSNFDPPK 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75813626 386 LTA---WS-----ILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd06613 222 LKDkekWSpdfhdFIKKCLTKNPKKRPTAT----KLLQHPFV 259
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
166-362 2.81e-35

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: 132.41  E-value: 2.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLqkkivlnRKEQKhimAERNVLL--KNVKHPFLVGL----HYSFQTTEKLYFV 239
Cdd:cd14089   7 QVLGLGINGKVLECFHKKTGEKFALKVL-------RDNPK---ARREVELhwRASGCPHIVRIidvyENTYQGRKCLLVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-----LDSVghVVLTDFGLCKEGI 312
Cdd:cd14089  77 MECMEGGELFSRIQEraDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLysskgPNAI--LKLTDFGFAKETT 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AiSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd14089 155 T-KKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY 203
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
161-407 3.24e-35

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: 132.18  E-value: 3.24e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVlNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEK-LYFV 239
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNA-SKRERKAAEQEAK-LLSKLKHPNIVSYKESFEGEDGfLYIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHL--QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT 317
Cdd:cd08223  79 MGFCEGGDLYTRLkeQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP-GVSLTAWSILEELL 396
Cdd:cd08223 159 ATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLPPMPkQYSPELGELIKAML 238
                       250
                ....*....|.
gi 75813626 397 EKDRQNRLGAK 407
Cdd:cd08223 239 HQDPEKRPSVK 249
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
161-362 3.86e-35

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: 132.24  E-value: 3.86e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDG-KFYAVK-VLQKKIVLNRKEQK------HIMAERNVLLKNVKHPFLVGLHYSFQT 232
Cdd:cd08528   1 EYAVLELLGSGAFGCVYKVRKKSNGqTLLALKeINMTNPAFGRTEQErdksvgDIISEVNIIKEQLRHPNIVRYYKTFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 TEKLYFVLDFVNG---GELFFHL-QRERSFPEHRARFYAAEIASALGYLHSIK-IVYRDLKPENILLDSVGHVVLTDFGL 307
Cdd:cd08528  81 NDRLYIVMELIEGaplGEHFSSLkEKNEHFTEDRIWNIFVQMVLALRYLHKEKqIVHRDLKPNNIMLGEDDKVTITDFGL 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 308 CKEGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd08528 161 AKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFY 215
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
166-421 3.91e-35

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: 133.19  E-value: 3.91e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhimaernvLLKNVK-HPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd14092  12 EALGDGSFSVCRKCVHKKTGQEFAVKIVSRRLDTSREVQ---------LLRLCQgHPNIVKLHEVFQDELHTYLVMELLR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLCK---EgiaiSDTT 318
Cdd:cd14092  83 GGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARlkpE----NQPL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTFCGTPEYLAPEVIR----KQPYDNTVDWWCLGAVLYEMLYGLPPF----YCRDVAEMYDNILHKPLSLR----PGVSL 386
Cdd:cd14092 159 KTPCFTLPYAAPEVLKqalsTQGYDESCDLWSLGVILYTMLSGQVPFqspsRNESAAEIMKRIKSGDFSFDgeewKNVSS 238
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75813626 387 TAWSILEELLEKDRQNRLGAKedflEIQNHPFFES 421
Cdd:cd14092 239 EAKSLIQGLLTVDPSKRLTMS----ELRNHPWLQG 269
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
160-408 3.95e-35

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: 132.49  E-value: 3.95e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQ--KHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd14046   6 TDFEELQVLGKGAFGQVVKVRNKLDGRYYAIK----KIKLRSESKnnSRILREVM-LLSRLNHQHVVRYYQAWIERANLY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT 317
Cdd:cd14046  81 IQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVEL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 T------------------TTFCGTPEYLAPEVI--RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMY---DNIL 374
Cdd:cd14046 161 AtqdinkstsaalgssgdlTGNVGTALYVAPEVQsgTKSTYNEKVDMYSLGIIFFEMCYPFSTGMERVQILTAlrsVSIE 240
                       250       260       270
                ....*....|....*....|....*....|....
gi 75813626 375 HkPLSLRPGVSLTAWSILEELLEKDRQNRLGAKE 408
Cdd:cd14046 241 F-PPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQE 273
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
166-419 7.74e-35

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: 130.82  E-value: 7.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14189   7 RLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIE-LHRDLHHKHVVKFSHHFEDAENIYIFLELCSR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFfHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd14189  86 KSLA-HIWKARhTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICGT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRL 404
Cdd:cd14189 165 PNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRL 244
                       250
                ....*....|....*
gi 75813626 405 GAKedflEIQNHPFF 419
Cdd:cd14189 245 TLD----QILEHEFF 255
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
166-418 9.39e-35

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: 131.27  E-value: 9.39e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVlnrKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14183  12 RTIGDGNFAVVKECVERSTGREYALKIINKSKC---RGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFGLckeGIAISDTTTTF 321
Cdd:cd14183  89 GDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGL---ATVVDGPLYTV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF--YCRDVAEMYDNILHK----PLSLRPGVSLTAWSILEEL 395
Cdd:cd14183 166 CGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFrgSGDDQEVLFDQILMGqvdfPSPYWDNVSDSAKELITMM 245
                       250       260
                ....*....|....*....|...
gi 75813626 396 LEKDRQNRLGAkedfLEIQNHPF 418
Cdd:cd14183 246 LQVDVDQRYSA----LQVLEHPW 264
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
161-419 1.05e-34

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: 130.58  E-value: 1.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVL------NRKEQK-----HIMAErnvlLKNVKHPFLVGLHYS 229
Cdd:cd14004   1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERILvdtwvrDRKLGTvpleiHILDT----LNKRSHPNIVKLLDF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 230 FQTTEKLYFVLD-FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG-- 306
Cdd:cd14004  77 FEDDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGsa 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 -LCKEGiaisdTTTTFCGTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGLPPFYcrDVAEMYDNILHKPLSlrpgV 384
Cdd:cd14004 157 aYIKSG-----PFDTFVGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENPFY--NIEEILEADLRIPYA----V 225
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75813626 385 SLTAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd14004 226 SEDLIDLISRMLNRDVGDRPTIE----ELLTDPWL 256
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
166-419 2.47e-34

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: 129.75  E-value: 2.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14188   7 KVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIE-LHRILHHKHVVQFYHYFEDKENIYILLEYCSR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd14188  86 RSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICGTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRlg 405
Cdd:cd14188 166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDR-- 243
                       250
                ....*....|....
gi 75813626 406 akEDFLEIQNHPFF 419
Cdd:cd14188 244 --PSLDEIIRHDFF 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
168-419 2.74e-34

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: 129.52  E-value: 2.74e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTE-KLYFVLDFVNGG 246
Cdd:cd14165   9 LGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILAR-LNHKSIIKTYEIFETSDgKVYIVMELGVQG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK------EG-IAISdttT 319
Cdd:cd14165  88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKrclrdeNGrIVLS---K 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTV-DWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTA--WSILEELL 396
Cdd:cd14165 165 TFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSecKDLIYRLL 244
                       250       260
                ....*....|....*....|...
gi 75813626 397 EKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd14165 245 QPDVSQRLCID----EVLSHPWL 263
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
161-362 2.78e-34

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: 129.70  E-value: 2.78e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd08224   1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQIFEMMDAKARQDCLKEID-LLQQLNHPNIIKYLASFIENNELNIVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGEL---FFHLQRE-RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLckeGIAISD 316
Cdd:cd08224  80 ELADAGDLsrlIKHFKKQkRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL---GRFFSS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75813626 317 TTT---TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd08224 157 KTTaahSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFY 205
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
163-419 3.01e-34

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: 130.49  E-value: 3.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 163 DFLKvIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd06659  25 NYVK-IGEGSTGVVCIAREKHSGRQVAVKMMD----LRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEY 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERSFPEHRARFYAAeIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFC 322
Cdd:cd06659 100 LQGGALTDIVSQTRLNEEQIATVCEA-VLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLV 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKP---LSLRPGVSLTAWSILEELLEKD 399
Cdd:cd06659 179 GTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPppkLKNSHKASPVLRDFLERMLVRD 258
                       250       260
                ....*....|....*....|
gi 75813626 400 RQNRLGAKedflEIQNHPFF 419
Cdd:cd06659 259 PQERATAQ----ELLDHPFL 274
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
168-417 3.77e-34

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: 129.79  E-value: 3.77e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLN----------RKEQKHIMAERNVL---------LKNVKHPFLVGLHY 228
Cdd:cd14118   2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKqagffrrpppRRKPGALGKPLDPLdrvyreiaiLKKLDHPNVVKLVE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 229 SFQ--TTEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd14118  82 VLDdpNEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 LCKEGIAISDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSL--R 381
Cdd:cd14118 161 VSNEFEGDDALLSSTAGTPAFMAPEALsesRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFpdD 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 75813626 382 PGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHP 417
Cdd:cd14118 241 PVVSEQLKDLILRMLDKNPSERITLP----EIKEHP 272
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
166-404 4.73e-34

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: 130.55  E-value: 4.73e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNrkEQKHIMAernvlLKNVK-HPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd14179  13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEAN--TQREIAA-----LKLCEgHPNIVKLHEVYHDQLHTFLVMELLK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLCKEGIAISDTTTTF 321
Cdd:cd14179  86 GGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQPLKTP 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPG-----------VSLTAWS 390
Cdd:cd14179 166 CFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTSAEEIMKKIKQGdfsfegeawknVSQEAKD 245
                       250
                ....*....|....
gi 75813626 391 ILEELLEKDRQNRL 404
Cdd:cd14179 246 LIQGLLTVDPNKRI 259
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
161-361 4.90e-34

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: 128.94  E-value: 4.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAernVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd08219   1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEA---VLLAKMKHPNIVAFKESFEADGHLYIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELF--FHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT 318
Cdd:cd08219  78 EYCDGGDLMqkIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYA 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd08219 158 CTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPF 200
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
166-418 5.89e-34

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: 128.96  E-value: 5.89e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVL-----QKKIVLNRKEQKHIMaernvllKNVKHPFLVG-----LHysfqtTEK 235
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGELMAMKEIrfqdnDPKTIKEIADEMKVL-------EGLDHPNLVRyygveVH-----REE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaIS 315
Cdd:cd06626  74 VYIFMEYCQEGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVK---LK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTT--------FCGTPEYLAPEVIRKQP---YDNTVDWWCLGAVLYEMLYGLPPFYCRD--VAEMYD-NILHKP-LSL 380
Cdd:cd06626 151 NNTTTmapgevnsLVGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEMATGKRPWSELDneWAIMYHvGMGHKPpIPD 230
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75813626 381 RPGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd06626 231 SLQLSPEGKDFLSRCLESDPKKRPTAS----ELLDHPF 264
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
159-418 7.88e-34

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: 128.57  E-value: 7.88e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTD-FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLqkKIVLNRKEQkhIMAERNVLLKNVKHPFLVGLHYSFQTT---- 233
Cdd:cd06608   4 PAGiFELVEVIGEGTYGKVYKARHKKTGQLAAIKIM--DIIEDEEEE--IKLEINILRKFSNHPNIATFYGAFIKKdppg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 --EKLYFVLDFVNGG---ELFFHL-QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGL 307
Cdd:cd06608  80 gdDQLWLVMEYCGGGsvtDLVKGLrKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 308 CkegiAISDTTT----TFCGTPEYLAPEVI--RKQP---YDNTVDWWCLGAVLYEMLYGLPPFycrdvAEMY-DNILHK- 376
Cdd:cd06608 160 S----AQLDSTLgrrnTFIGTPYWMAPEVIacDQQPdasYDARCDVWSLGITAIELADGKPPL-----CDMHpMRALFKi 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 377 PLSLRPGV-SLTAWS-----ILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd06608 231 PRNPPPTLkSPEKWSkefndFISECLIKNYEQRPFTE----ELLEHPF 274
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
162-418 9.37e-34

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: 128.37  E-value: 9.37e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKK-IVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14105   7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRrSKASRRGVSREDIEREVsILRQVLHPNIITLHDVFENKTDVVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFGLCKEgIAIS 315
Cdd:cd14105  87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLldknVPIPRIKLIDFGLAHK-IEDG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSI 391
Cdd:cd14105 166 NEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDdeyfSNTSELAKDF 245
                       250       260
                ....*....|....*....|....*..
gi 75813626 392 LEELLEKDRQNRLGAKEDFleiqNHPF 418
Cdd:cd14105 246 IRQLLVKDPRKRMTIQESL----RHPW 268
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
168-423 9.55e-34

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: 129.00  E-value: 9.55e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd06644  20 LGDGAFGKVYKAKNKETGALAAAKVIETK---SEEELEDYMVEIEIL-ATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGA 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 L-FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTPE 326
Cdd:cd06644  96 VdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGTPY 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 327 YLAPEVI-----RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMydnILHKPLSLRPGVSL-TAWSI-----LEEL 395
Cdd:cd06644 176 WMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRV---LLKIAKSEPPTLSQpSKWSMefrdfLKTA 252
                       250       260
                ....*....|....*....|....*...
gi 75813626 396 LEKDRQNRLGAKEdFLEiqnHPFFESLS 423
Cdd:cd06644 253 LDKHPETRPSAAQ-LLE---HPFVSSVT 276
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
161-418 1.42e-33

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: 127.67  E-value: 1.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14186   2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQ-LKHPSILELYNYFEDSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd14186  81 EMCHNGEMSRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd14186 161 TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKN 240
                       250
                ....*....|....*....
gi 75813626 400 RQNRLGAKedflEIQNHPF 418
Cdd:cd14186 241 PADRLSLS----SVLDHPF 255
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
168-419 1.57e-33

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: 127.37  E-value: 1.57e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVllaKRKLDG---KFYAVKVLQKkivlnRKEQKHIMAERNV-----LLKNVKHPFLVGLHYSFQTTE--KLY 237
Cdd:cd14119   1 LGEGSYGKV---KEVLDTetlCRRAVKILKK-----RKLRRIPNGEANVkreiqILRRLNHRNVIKLVDVLYNEEkqKLY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGG--ELFFHLQRERsFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG----LCKeg 311
Cdd:cd14119  73 MVMEYCVGGlqEMLDSAPDKR-LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGvaeaLDL-- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 312 IAISDTTTTFCGTPEYLAPEVIRKQPYDN--TVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAW 389
Cdd:cd14119 150 FAEDDTCTTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQ 229
                       250       260       270
                ....*....|....*....|....*....|
gi 75813626 390 SILEELLEKDRQNRLgakeDFLEIQNHPFF 419
Cdd:cd14119 230 DLLRGMLEKDPEKRF----TIEQIRQHPWF 255
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
166-361 2.52e-33

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: 127.14  E-value: 2.52e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKhiMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14082   9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQ--LRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLHG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG---HVVLTDFGLCKEgIAISDTTTTF 321
Cdd:cd14082  87 DMLEMILSSEKGrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI-IGEKSFRRSV 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14082 166 VGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
159-423 2.81e-33

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: 127.45  E-value: 2.81e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDF-DFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd06643   3 PEDFwEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTK---SEEELEDYMVEIDIL-ASCDHPNIVKLLDAFYYENNLW 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGEL-FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISD 316
Cdd:cd06643  79 ILIEFCAGGAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQ 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVI-----RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH-KPLSLrpgVSLTAWS 390
Cdd:cd06643 159 RRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKsEPPTL---AQPSRWS 235
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75813626 391 -----ILEELLEKDRQNRLGAkedfLEIQNHPFFESLS 423
Cdd:cd06643 236 pefkdFLRKCLEKNVDARWTT----SQLLQHPFVSVLV 269
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
166-421 3.82e-33

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: 126.59  E-value: 3.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLnRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14187  13 RFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLL-KPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTP 325
Cdd:cd14187  92 RSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLCGTP 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLG 405
Cdd:cd14187 172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPT 251
                       250
                ....*....|....*.
gi 75813626 406 AKedflEIQNHPFFES 421
Cdd:cd14187 252 IN----ELLNDEFFTS 263
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
166-418 4.17e-33

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: 127.07  E-value: 4.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEqkhIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14173   8 EVLGEGAYARVQTCINLITNKEYAVKIIEKRPGHSRSR---VFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFEKMRG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS---VGHVVLTDFGLcKEGIAISDTTT--- 319
Cdd:cd14173  85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHpnqVSPVKICDFDL-GSGIKLNSDCSpis 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 -----TFCGTPEYLAPEVI-----RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCR----------DVAEMYDNILHKplS 379
Cdd:cd14173 164 tpellTPCGSAEYMAPEVVeafneEASIYDKRCDLWSLGVILYIMLSGYPPFVGRcgsdcgwdrgEACPACQNMLFE--S 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 380 LRPG-----------VSLTAWSILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14173 242 IQEGkyefpekdwahISCAAKDLISKLLVRDAKQRLSAA----QVLQHPW 287
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
168-418 6.22e-33

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: 126.68  E-value: 6.22e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnrkeQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14175   9 IGVGSYSVCKRCVHKATNMEYAVKVIDKS-------KRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGH---VVLTDFGLCKEGIAISDTTTTFCG 323
Cdd:cd14175  82 LLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFyCRDVAEMYDNILHK----PLSLRPG----VSLTAWSILEEL 395
Cdd:cd14175 162 TANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF-ANGPSDTPEEILTRigsgKFTLSGGnwntVSDAAKDLVSKM 240
                       250       260
                ....*....|....*....|...
gi 75813626 396 LEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14175 241 LHVDPHQRLTAK----QVLQHPW 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
162-418 7.35e-33

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: 125.84  E-value: 7.35e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIV-LNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14196   7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSrASRRGVSREEIEREVsILRQVLHPNIITLHDVYENRTDVVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENI-LLDS---VGHVVLTDFGLCKEgIAIS 315
Cdd:cd14196  87 LELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKnipIPHIKLIDFGLAHE-IEDG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSI 391
Cdd:cd14196 166 VEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDeeffSHTSELAKDF 245
                       250       260
                ....*....|....*....|....*..
gi 75813626 392 LEELLEKDRQNRLGAKEDFleiqNHPF 418
Cdd:cd14196 246 IRKLLVKETRKRLTIQEAL----RHPW 268
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
164-418 9.44e-33

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: 125.89  E-value: 9.44e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNR--KEQK------HIMAERNVLlKNVKHPFLVGLHYSFQT-TE 234
Cdd:cd13990   4 LLNLLGKGGFSEVYKAFDLVEQRYVACKIHQ----LNKdwSEEKkqnyikHALREYEIH-KSLDHPRIVKLYDVFEIdTD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILLDS---VGHVVLTDFGLCK 309
Cdd:cd13990  79 SFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSgnvSGEIKITDFGLSK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 ---------EGIaisDTTTTFCGTPEYLAPE--VIRKQP--YDNTVDWWCLGAVLYEMLYGLPPF---YCRDVAEMYDNI 373
Cdd:cd13990 159 imddesynsDGM---ELTSQGAGTYWYLPPEcfVVGKTPpkISSKVDVWSVGVIFYQMLYGRKPFghnQSQEAILEENTI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 374 LHK---PLSLRPGVSLTAWSILEELLEKDRQNRLgakeDFLEIQNHPF 418
Cdd:cd13990 236 LKAtevEFPSKPVVSSEAKDFIRRCLTYRKEDRP----DVLQLANDPY 279
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
166-420 9.92e-33

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: 126.30  E-value: 9.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEqkhIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14174   8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNAGHSRSR---VFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLcKEGIAISD-----T 317
Cdd:cd14174  85 GSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDL-GSGVKLNSactpiT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 T---TTFCGTPEYLAPEVI-----RKQPYDNTVDWWCLGAVLYEMLYGLPPF--------------YCRDVA-EMYDNIL 374
Cdd:cd14174 164 TpelTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgwdrgeVCRVCQnKLFESIQ 243
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 375 HKPLSLRPG----VSLTAWSILEELLEKDRQNRLGAkedfLEIQNHPFFE 420
Cdd:cd14174 244 EGKYEFPDKdwshISSEAKDLISKLLVRDAKERLSA----AQVLQHPWVQ 289
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
161-418 1.26e-32

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 125.43  E-value: 1.26e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkIVLNRKE------QKHIMaernvLLKNVKHPFLVGLHYSFQTTE 234
Cdd:cd06609   2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKV----IDLEEAEdeiediQQEIQ-----FLSQCDSPYITKYYGSFLKGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaI 314
Cdd:cd06609  73 KLWIIMEYCGGGSVL-DLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQ---L 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 SDTTT---TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPfYCrDVAEMYDNIL---HKPLSL-RPGVSLT 387
Cdd:cd06609 149 TSTMSkrnTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPP-LS-DLHPMRVLFLipkNNPPSLeGNKFSKP 226
                       250       260       270
                ....*....|....*....|....*....|.
gi 75813626 388 AWSILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd06609 227 FKDFVELCLNKDPKERPSAK----ELLKHKF 253
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
160-356 1.46e-32

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: 125.10  E-value: 1.46e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd13996   6 NDFEEIELLGSGGFGSVYKVRNKVDGVTYAIK----KIRLTEKSSASEKVLREVkALAKLNHPNIVRYYTAWVEEPPLYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRERSFP---EHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVV-LTDFGLCKEGIA- 313
Cdd:cd13996  82 QMELCEGGTLRDWIDRRNSSSkndRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQVkIGDFGLATSIGNq 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 314 -------------ISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY 356
Cdd:cd13996 162 krelnnlnnnnngNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH 217
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
162-419 3.49e-32

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: 124.57  E-value: 3.49e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEqkHIMAERNV--LLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKK--FYSWE--ECMNLREVksLRKLNEHPNIVKLKEVFRENDELYFV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGelFFHLQRER---SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISD 316
Cdd:cd07830  77 FEYMEGN--LYQLMKDRkgkPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLARE-IRSRP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEmLYGLPPFYC--RDVAEMY----------------------- 370
Cdd:cd07830 154 PYTDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAE-LYTLRPLFPgsSEIDQLYkicsvlgtptkqdwpegyklask 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 371 -----DNILHKPLS-LRPGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd07830 233 lgfrfPQFAPTSLHqLIPNASPEAIDLIKDMLRWDPKKRPTAS----QALQHPYF 283
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
162-418 4.14e-32

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 123.73  E-value: 4.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVllknvKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQREIINHRSL-----RHPNIIRFKEVVLTPTHLAIVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS--VGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd14662  77 YAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGspAPRLKICDFGYSKSSVLHSQPKS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TfCGTPEYLAPEVIRKQPYDNTV-DWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR---PG---VSLTAWSIL 392
Cdd:cd14662 157 T-VGTPAYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVGAYPFEDPDDPKNFRKTIQRIMSVQykiPDyvrVSQDCRHLL 235
                       250       260
                ....*....|....*....|....*.
gi 75813626 393 EELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14662 236 SRIFVANPAKRITIP----EIKNHPW 257
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
166-419 4.79e-32

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: 123.89  E-value: 4.79e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnRKEQK---HIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd14197  15 RELGRGKFAVVRKCVEKDSGKEFAAKFMRKR----RKGQDcrmEIIHEIAVLELAQANPWVINLHEVYETASEMILVLEY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHL--QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS---VGHVVLTDFGLCKEgIAISDT 317
Cdd:cd14197  91 AAGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSespLGDIKIVDFGLSRI-LKNSEE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILE 393
Cdd:cd14197 170 LREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEeefeHLSESAIDFIK 249
                       250       260
                ....*....|....*....|....*.
gi 75813626 394 ELLEKDRQNRLGAkEDFLEiqnHPFF 419
Cdd:cd14197 250 TLLIKKPENRATA-EDCLK---HPWL 271
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
168-406 6.92e-32

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: 123.16  E-value: 6.92e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvLNRKEQKHIMAernvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14113  15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKL-MKRDQVTHELG----VLQSLQHPQLVGLLDTFETPTSYILVLEMADQGR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD---SVGHVVLTDFglckeGIAISDTTTTFC-- 322
Cdd:cd14113  90 LLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIKLADF-----GDAVQLNTTYYIhq 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 --GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSILEELL 396
Cdd:cd14113 165 llGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLL 244
                       250
                ....*....|
gi 75813626 397 EKDRQNRLGA 406
Cdd:cd14113 245 QMDPAKRPSA 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
168-418 1.17e-31

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: 122.82  E-value: 1.17e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKK-IVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14194  13 LGSGQFAVVKKCREKSTGLQYAAKFIKKRrTKSSRRGVSREDIEREVsILKEIQHPNVITLHEVYENKTDVILILELVAG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL--DSVGH--VVLTDFGLCKEgIAISDTTTTF 321
Cdd:cd14194  93 GELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLldRNVPKprIKIIDFGLAHK-IDFGNEFKNI 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSILEELLE 397
Cdd:cd14194 172 FGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEdeyfSNTSALAKDFIRRLLV 251
                       250       260
                ....*....|....*....|.
gi 75813626 398 KDRQNRLGAKEDFLeiqnHPF 418
Cdd:cd14194 252 KDPKKRMTIQDSLQ----HPW 268
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
166-403 1.23e-31

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 127.29  E-value: 1.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLLkNVKHPFLVGLHYSF--------QTTEKLY 237
Cdd:PTZ00283  38 RVLGSGATGTVLCAKRVSDGEPFAVKVVDME-GMSEADKNRAQAEVCCLL-NCDFFSIVKCHEDFakkdprnpENVLMIA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  238 FVLDFVNGGELFFHLQRE----RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA 313
Cdd:PTZ00283 116 LVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  314 I--SDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycrDVAEMYDnILHKPLS-----LRPGVSL 386
Cdd:PTZ00283 196 TvsDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPF---DGENMEE-VMHKTLAgrydpLPPSISP 271
                        250
                 ....*....|....*..
gi 75813626  387 TAWSILEELLEKDRQNR 403
Cdd:PTZ00283 272 EMQEIVTALLSSDPKRR 288
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
168-374 1.44e-31

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: 121.95  E-value: 1.44e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlnRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKC-----RKAKDREDVRNEIeIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELF-------FHLQrersfpEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGHVV-LTDFGLCKEGIAISDT 317
Cdd:cd14103  76 ELFervvdddFELT------ERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNQIkIIDFGLARKYDPDKKL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 318 TTTFcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL 374
Cdd:cd14103 150 KVLF-GTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVT 205
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
168-404 2.33e-31

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: 123.06  E-value: 2.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNrkEQKHIMAERNVllknVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14180  14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEAN--TQREVAALRLC----QSHPNIVALHEVLHDQYHTYLVMELLRGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL--DSVGHVV-LTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd14180  88 LLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYadESDGAVLkVIDFGFARLRPQGSRPLQTPCFT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD-------VAEMYDNILHKPLSLR----PGVSLTAWSILE 393
Cdd:cd14180 168 LQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfhnhAADIMHKIKEGDFSLEgeawKGVSEEAKDLVR 247
                       250
                ....*....|.
gi 75813626 394 ELLEKDRQNRL 404
Cdd:cd14180 248 GLLTVDPAKRL 258
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
162-375 2.42e-31

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: 121.51  E-value: 2.42e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSIL-RRVNHPNIVQMFECIEVANGRLYIVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG-HVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd14164  81 EAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDYPELSTT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 321 FCGTPEYLAPEVIRKQPYD-NTVDWWCLGAVLYEMLYGLPPFY---CRDVAEMYDNILH 375
Cdd:cd14164 161 FCGSRAYTPPEVILGTPYDpKKYDVWSLGVVLYVMVTGTMPFDetnVRRLRLQQRGVLY 219
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
164-361 2.75e-31

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: 121.69  E-value: 2.75e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKE----QKHI-MAERNVLLKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd13993   4 LISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKS-GPNSKDgndfQKLPqLREIDLHRRVSRHPNIITLHDVFETEVAIYI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRERSFP--EHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD-SVGHVVLTDFGLckegiAIS 315
Cdd:cd13993  83 VLEYCPNGDLFEAITENRIYVgkTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGL-----ATT 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75813626 316 DTTTT--FCGTPEYLAPEVIR-----KQPYDN-TVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd13993 158 EKISMdfGVGSEFYMAPECFDevgrsLKGYPCaAGDIWSLGIILLNLTFGRNPW 211
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
166-420 3.74e-31

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: 121.56  E-value: 3.74e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQ--KKIVLNRKEQKHI----MAERNVLLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14182   9 EILGRGVSSVVRRCIHKPTRQEYAVKIIDitGGGSFSPEEVQELreatLKEIDILRKVSGHPNIIQLKDTYETNTFFFLV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTT 319
Cdd:cd14182  89 FDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LDPGEKLR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIR------KQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAW 389
Cdd:cd14182 168 EVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGNYQFGSpewdDRSDTVK 247
                       250       260       270
                ....*....|....*....|....*....|.
gi 75813626 390 SILEELLEKDRQNRLGAKEDFleiqNHPFFE 420
Cdd:cd14182 248 DLISRFLVVQPQKRYTAEEAL----AHPFFQ 274
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
153-420 3.96e-31

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: 120.80  E-value: 3.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 153 GNPHAKPTDFDflkVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQT 232
Cdd:cd06647   3 GDPKKKYTRFE---KIGQGASGTVYTAIDVATGQEVAIK----QMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 TEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGI 312
Cdd:cd06647  76 GDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycrdvaeMYDNILH---------KP-LSLRP 382
Cdd:cd06647 155 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRalyliatngTPeLQNPE 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75813626 383 GVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFFE 420
Cdd:cd06647 228 KLSAIFRDFLNRCLEMDVEKRGSAK----ELLQHPFLK 261
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
166-408 5.54e-31

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: 120.41  E-value: 5.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14190  10 EVLGGGKFGKVHTCTEKRTGLKLAAKVINKQ---NSKDKEMVLLEIQVM-NQLNHRNLIQLYEAIETPNEIVLFMEYVEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-DSVGHVV-LTDFGLCKEGIAISDTTTTFc 322
Cdd:cd14190  86 GELFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHQVkIIDFGLARRYNPREKLKVNF- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSILEELLEK 398
Cdd:cd14190 165 GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDFVSNLIIK 244
                       250
                ....*....|
gi 75813626 399 DRQNRLGAKE 408
Cdd:cd14190 245 ERSARMSATQ 254
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
165-422 8.36e-31

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


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 120.69  E-value: 8.36e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVK-VLQKKIVLNRKEQkhIMaernvllKNVKHPFLVGLHYSFQTTEK------LY 237
Cdd:cd14137   9 EKVIGSGSFGVVYQAKLLETGEVVAIKkVLQDKRYKNRELQ--IM-------RRLKHPNIVKLKYFFYSSGEkkdevyLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNG---GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD-SVGHVVLTDFGLCKEgIA 313
Cdd:cd14137  80 LVMEYMPEtlyRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGSAKR-LV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTPEYLAPEVI-RKQPYDNTVDWWCLGAVLYEMLYGLPPF-------------------YCRDVAEM---- 369
Cdd:cd14137 159 PGEPNVSYICSRYYRAPELIfGATDYTTAIDIWSAGCVLAELLLGQPLFpgessvdqlveiikvlgtpTREQIKAMnpny 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 370 ----YDNILHKPLS--LRPGVSLTAWSILEELLEKDRQNRLGAkedfLEIQNHPFFESL 422
Cdd:cd14137 239 tefkFPQIKPHPWEkvFPKRTPPDAIDLLSKILVYNPSKRLTA----LEALAHPFFDEL 293
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
168-418 9.43e-31

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 120.44  E-value: 9.43e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNR----------------KEQKHIMA------ERNVLLKNVKHPFLVG 225
Cdd:cd14200   8 IGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqGEQAKPLAplervyQEIAILKKLDHVNIVK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 226 LHYSFQ--TTEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLT 303
Cdd:cd14200  88 LIEVLDdpAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 304 DFGLCKEGIAISDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSL 380
Cdd:cd14200 167 DFGVSNQFEGNDALLSSTAGTPAFMAPETLsdsGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVEF 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75813626 381 --RPGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14200 247 peEPEISEELKDLILKMLDKNPETRITVP----EIKVHPW 282
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
168-432 9.92e-31

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: 120.89  E-value: 9.92e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlnrkEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14178  11 IGIGSYSVCKRCVHKATSTEYAVKIIDK-------SKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMRGGE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGH---VVLTDFGLCKEGIAISDTTTTFCG 323
Cdd:cd14178  84 LLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGLLMTPCY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC--RDVA-EMYDNILHKPLSLRPG----VSLTAWSILEELL 396
Cdd:cd14178 164 TANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANgpDDTPeEILARIGSGKYALSGGnwdsISDAAKDIVSKML 243
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 75813626 397 EKDRQNRLGAkedfLEIQNHPFF---ESLSWADLVQKKI 432
Cdd:cd14178 244 HVDPHQRLTA----PQVLRHPWIvnrEYLSQNQLSRQDV 278
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
153-420 1.89e-30

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: 120.21  E-value: 1.89e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 153 GNPHAKPTDFDflkVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQT 232
Cdd:cd06655  15 GDPKKKYTRYE---KIGQGASGTVFTAIDVATGQEVAIK----QINLQKQPKKELIINEILVMKELKNPNIVNFLDSFLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 TEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGI 312
Cdd:cd06655  88 GDELFVVMEYLAGGSLT-DVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQIT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD-------VAEMYDNILHKPLSLRPGVS 385
Cdd:cd06655 167 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENplralylIATNGTPELQNPEKLSPIFR 246
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75813626 386 ltawSILEELLEKDRQNRLGAKedflEIQNHPFFE 420
Cdd:cd06655 247 ----DFLNRCLEMDVEKRGSAK----ELLQHPFLK 273
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
168-418 2.48e-30

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: 120.90  E-value: 2.48e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlnrkEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14176  27 IGVGSYSVCKRCIHKATNMEFAVKIIDK-------SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGH---VVLTDFGLCKEGIAISDTTTTFCG 323
Cdd:cd14176 100 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC--RDVA-EMYDNILHKPLSLRPG----VSLTAWSILEELL 396
Cdd:cd14176 180 TANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTPeEILARIGSGKFSLSGGywnsVSDTAKDLVSKML 259
                       250       260
                ....*....|....*....|..
gi 75813626 397 EKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14176 260 HVDPHQRLTAA----LVLRHPW 277
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
168-418 2.89e-30

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 119.30  E-value: 2.89e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNV----------------------LLKNVKHPFLVG 225
Cdd:cd14199  10 IGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLMRQAGFPRRPPPRGAraapegctqprgpiervyqeiaILKKLDHPNVVK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 226 LHYSFQ--TTEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLT 303
Cdd:cd14199  90 LVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 304 DFGLCKEGIAISDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSL 380
Cdd:cd14199 169 DFGVSNEFEGSDALLTNTVGTPAFMAPETLsetRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQPLEF 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75813626 381 --RPGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd14199 249 pdQPDISDDLKDLLFRMLDKNPESRISVP----EIKLHPW 284
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
161-408 3.67e-30

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: 117.87  E-value: 3.67e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIM-AERNVLLKnvKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALReVEAHAALG--QHPNIVRYYSSWEEGGHLYIQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQR---ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCkegiaiSD 316
Cdd:cd13997  79 MELCENGSLQDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA------TR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFC---GTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLP-PfycrDVAEMYDNILHK--PLSLRPGVSLTAW 389
Cdd:cd13997 153 LETSGDveeGDSRYLAPELLNENYtHLPKADIFSLGVTVYEAATGEPlP----RNGQQWQQLRQGklPLPPGLVLSQELT 228
                       250
                ....*....|....*....
gi 75813626 390 SILEELLEKDRQNRLGAKE 408
Cdd:cd13997 229 RLLKVMLDPDPTRRPTADQ 247
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
162-418 4.94e-30

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 118.80  E-value: 4.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQ-KKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14094   5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDvAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERS----FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH---VVLTDFGLCKEgia 313
Cdd:cd14094  85 EFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQ--- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCG---TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVaEMYDNILHKPLSLRP----GVSL 386
Cdd:cd14094 162 LGESGLVAGGrvgTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKE-RLFEGIIKGKYKMNPrqwsHISE 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 75813626 387 TAWSILEELLEKDRQNRLGAKEDFleiqNHPF 418
Cdd:cd14094 241 SAKDLVRRMLMLDPAERITVYEAL----NHPW 268
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
163-420 5.30e-30

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: 118.60  E-value: 5.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 163 DFLKvIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd06658  26 SFIK-IGEGSTGIVCIATEKHTGKQVAVK----KMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERSFPEHRARFyAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFC 322
Cdd:cd06658 101 LEGGALTDIVTHTRMNEEQIATV-CLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLV 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY----CRDVAEMYDNI------LHKplslrpgVSLTAWSIL 392
Cdd:cd06658 180 GTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFneppLQAMRRIRDNLpprvkdSHK-------VSSVLRGFL 252
                       250       260
                ....*....|....*....|....*...
gi 75813626 393 EELLEKDRQNRLGAkedfLEIQNHPFFE 420
Cdd:cd06658 253 DLMLVREPSQRATA----QELLQHPFLK 276
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
166-362 5.59e-30

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: 118.17  E-value: 5.59e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvllknvkhPFLVGLHYSFQTTEK----LYFVLD 241
Cdd:cd14172  10 QVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWRASGG--------PHIVHILDVYENMHHgkrcLLIIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS---VGHVVLTDFGLCKEgIAISD 316
Cdd:cd14172  82 CMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSkekDAVLKLTDFGFAKE-TTVQN 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd14172 161 ALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFY 206
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
161-354 5.68e-30

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: 117.53  E-value: 5.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVE-QMTKEERQAALNEVKVL-SMLHHPNIIEYYESFLEDKALMIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERS--FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVV-LTDFGLCKEGIAISDT 317
Cdd:cd08220  79 EYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVkIGDFGISKILSSKSKA 158
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75813626 318 TTTFcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEM 354
Cdd:cd08220 159 YTVV-GTPCYISPELCEGKPYNQKSDIWALGCVLYEL 194
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
162-408 8.83e-30

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 117.58  E-value: 8.83e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkIVLNRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLN--LDTDDDDVSDIQKEVALLsqLKLGQPKNIIKYYGSYLKGPSLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTT 319
Cdd:cd06917  81 MDYCEGGSIR-TLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH-KPlslrPGVSLTAWS-ILEEL- 395
Cdd:cd06917 160 TFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKsKP----PRLEGNGYSpLLKEFv 235
                       250
                ....*....|....*.
gi 75813626 396 ---LEKDRQNRLGAKE 408
Cdd:cd06917 236 aacLDEEPKDRLSADE 251
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
166-373 1.86e-29

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: 116.56  E-value: 1.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnRKEQK---HIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTGQEYAAKFLKKR----RRGQDcraEILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERS--FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV---GHVVLTDFGLCKEgIAISDT 317
Cdd:cd14198  90 AAGGEIFNLCVPDLAemVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRK-IGHACE 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI 373
Cdd:cd14198 169 LREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNI 224
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
162-419 2.12e-29

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 116.81  E-value: 2.12e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVL-NRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK----KIRLdNEEEGIPSTALREIsLLKELKHPNIVKLLDVIHTENKLYLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGgELFFHL-QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GIAISDT 317
Cdd:cd07829  77 FEYCDQ-DLKKYLdKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAfGIPLRTY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCgTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI----------------------- 373
Cdd:cd07829 156 THEVV-TLWYRAPEILLGSKhYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIfqilgtpteeswpgvtklpdykp 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 374 ---LHKPLSLR---PGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd07829 235 tfpKWPKNDLEkvlPRLDPEGIDLLSKMLQYNPAKRISAK----EALKHPYF 282
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
166-408 2.91e-29

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: 115.83  E-value: 2.91e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14192  10 EVLGGGRFGQVHKCTELSTGLTLAAKIIK---VKGAKEREEVKNEINIM-NQLNHVNLIQLYDAFESKTNLTLIMEYVDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGHVV-LTDFGLCKEGIAISDTTTTFc 322
Cdd:cd14192  86 GELFDRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNQIkIIDFGLARRYKPREKLKVNF- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILEELLEK 398
Cdd:cd14192 165 GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAeafeNLSEEAKDFISRLLVK 244
                       250
                ....*....|
gi 75813626 399 DRQNRLGAKE 408
Cdd:cd14192 245 EKSCRMSATQ 254
PX_SNX16 cd07276
The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a ...
26-120 4.06e-29

The phosphoinositide binding Phox Homology domain of Sorting Nexin 16; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX16 contains a central PX domain followed by a coiled-coil region. SNX16 is localized in early and recycling endosomes through the binding of its PX domain to phosphatidylinositol-3-phosphate (PI3P). It plays a role in epidermal growth factor (EGF) signaling by regulating EGF receptor membrane trafficking.


Pssm-ID: 132809  Cd Length: 110  Bit Score: 110.58  E-value: 4.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  26 EKKKRFTVYKVLV--SVGRSeWFVFRRYAEFDKLYNTLKKQFPAMALKIPAKRIFGDNFDPDFIKQRRAGLNEFIQNLVR 103
Cdd:cd07276  15 EERARFTVYKIRVenKVGDS-WFVFRRYTDFVRLNDKLKQMFPGFRLSLPPKRWFKDNFDPDFLEERQLGLQAFVNNIMA 93
                        90
                ....*....|....*..
gi 75813626 104 YPELYNHPDVRAFLQMD 120
Cdd:cd07276  94 HKDIAKCKLVREFFCLD 110
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
161-419 4.25e-29

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: 115.53  E-value: 4.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEqkhimAERNVLLKNVK------HPFLVGLHYSFQTTE 234
Cdd:cd06610   2 DYELIEVIGSGATAVVYAAYCLPKKEKVAIK----RIDLEKCQ-----TSMDELRKEIQamsqcnHPNVVSYYTSFVVGD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFfHLQRER----SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG---- 306
Cdd:cd06610  73 ELWLVMPLLSGGSLL-DIMKSSyprgGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGvsas 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 LCKEGIAISDTTTTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL-HKPLSLRPGV 384
Cdd:cd06610 152 LATGGDRTRKVRKTFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLqNDPPSLETGA 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75813626 385 SLTAWS-----ILEELLEKDRQNRLGAKEdFLEiqnHPFF 419
Cdd:cd06610 232 DYKKYSksfrkMISLCLQKDPSKRPTAEE-LLK---HKFF 267
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
168-373 4.49e-29

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: 115.49  E-value: 4.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKK-IVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14195  13 LGSGQFAIVRKCREKGTGKEYAAKFIKKRrLSSSRRGVSREEIEREVnILREIQHPNIITLHDIFENKTDVVLILELVSG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG----HVVLTDFGLCKEGIAISDTTTTF 321
Cdd:cd14195  93 GELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHKIEAGNEFKNIF 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 322 cGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI 373
Cdd:cd14195 173 -GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNI 223
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
168-406 5.03e-29

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: 114.67  E-value: 5.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEQkhiMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14115   1 IGRGRFSIVKKCLHKATRKDVAVKFVSKK--MKKKEQ---AAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD---SVGHVVLTDFGLCKEgIAISDTTTTFCGT 324
Cdd:cd14115  76 LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQ-ISGHRHVHHLLGN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILEELLEKDR 400
Cdd:cd14115 155 PEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDeyfgDVSQAARDFINVILQEDP 234

                ....*.
gi 75813626 401 QNRLGA 406
Cdd:cd14115 235 RRRPTA 240
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
166-424 6.98e-29

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: 114.70  E-value: 6.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTE-KLYFVLDFVN 244
Cdd:cd14163   6 KTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIV-ERLDHKNIIHVYEMLESADgKIYLVMELAE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVgHVVLTDFGLCKE-GIAISDTTTTFCG 323
Cdd:cd14163  85 DGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQlPKGGRELSQTFCG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIRKQPYDNTV-DWWCLGAVLYEMLYGLPPFYCRDVAEMYDNiLHKPLSL--RPGVSLTAWSILEELLEKDR 400
Cdd:cd14163 164 STAYAAPEVLQGVPHDSRKgDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQ-QQKGVSLpgHLGVSRTCQDLLKRLLEPDM 242
                       250       260
                ....*....|....*....|....
gi 75813626 401 QNRlgakedfleiqnhPFFESLSW 424
Cdd:cd14163 243 VLR-------------PSIEEVSW 253
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
166-362 9.68e-29

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: 115.52  E-value: 9.68e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFlvglHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14170   8 QVLGLGINGKVLQIFNKRTQEKFALKMLQDCPKARREVELHWRASQCPHIVRIVDVY----ENLYAGRKCLLIVMECLDG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV---GHVVLTDFGLCKEgIAISDTTTT 320
Cdd:cd14170  84 GELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKE-TTSHNSLTT 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd14170 163 PCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY 204
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
133-420 1.04e-28

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: 115.20  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 133 DERSSQKLHStsqninLGPSGNPHAKPTDFDflkVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERN 212
Cdd:cd06656   1 DEEILEKLRS------IVSVGDPKKKYTRFE---KIGQGASGTVYTAIDIATGQEVAIKQMN----LQQQPKKELIINEI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 213 VLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENI 292
Cdd:cd06656  68 LVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 293 LLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD-VAEMYD 371
Cdd:cd06656 147 LLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENpLRALYL 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 372 NILHKPLSLRPGVSLTA--WSILEELLEKDRQNRLGAKedflEIQNHPFFE 420
Cdd:cd06656 227 IATNGTPELQNPERLSAvfRDFLNRCLEMDVDRRGSAK----ELLQHPFLK 273
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
160-362 1.22e-28

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: 114.35  E-value: 1.22e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEID-LLKQLNHPNVIKYLDSFIEDNELNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGEL-----FFHLQReRSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLckeGIAI 314
Cdd:cd08228  81 LELADAGDLsqmikYFKKQK-RLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGL---GRFF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 315 SDTTT---TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd08228 157 SSKTTaahSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFY 207
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
166-373 1.40e-28

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: 113.79  E-value: 1.40e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAK-RKLDGKFY--AVKVLqkKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLhYSFQTT-EKLYFVLD 241
Cdd:cd00192   1 KKLGEGAFGEVYKGKlKGGDGKTVdvAVKTL--KEDASESERKDFLKEARVM-KKLGHPNVVRL-LGVCTEeEPLYLVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERS-FPEHRARF--------YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgI 312
Cdd:cd00192  77 YMEGGDLLDFLRKSRPvFPSPEPSTlslkdllsFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD-I 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 313 AISDTTTTFCGTPE---YLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:cd00192 156 YDDDYYRKKTGGKLpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFtLGATPYPGLSNEEVLEYL 220
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
168-361 1.76e-28

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: 114.47  E-value: 1.76e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlQKKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGL-----HYSFQTTEKLYFV-L 240
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYVAIK--KCRQELSPSDKNRERWCLEVqIMKKLNHPNVVSArdvppELEKLSPNDLPLLaM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERS---FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-DSVGHVV--LTDFGLCKEgIAI 314
Cdd:cd13989  79 EYCSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRVIykLIDLGYAKE-LDQ 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 315 SDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd13989 158 GSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
168-361 1.84e-28

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: 113.56  E-value: 1.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRK--LDGKFYAVKVLQKK-IVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQT-TEKLYFVLDFV 243
Cdd:cd13994   1 IGKGATSVVRIVTKKnpRSGVLYAVKEYRRRdDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDlHGKWCLVMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC-KEGIAISDTTTTF- 321
Cdd:cd13994  81 PGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPAEKESPMSa 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75813626 322 --CGTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGLPPF 361
Cdd:cd13994 161 glCGSEPYMAPEVFTSGSYDGRaVDVWSCGIVLFALFTGRFPW 203
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
168-360 2.07e-28

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 113.19  E-value: 2.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlNRKEQKHIMAERNVLLKNVKHPFLVGLH-YSFQTTEKLYFVLDFVNGG 246
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPK----PSTKLKDFLREYNISLELSVHPHIIKTYdVAFETEDYYVFAQEYAPYG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL--DSVGHVVLTDFGLCKegiaISDTTTTF-CG 323
Cdd:cd13987  77 DLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTR----RVGSTVKRvSG 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 75813626 324 TPEYLAPEV---IRKQPY--DNTVDWWCLGAVLYEMLYGLPP 360
Cdd:cd13987 153 TIPYTAPEVceaKKNEGFvvDPSIDVWAFGVLLFCCLTGNFP 194
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
166-354 2.39e-28

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: 113.29  E-value: 2.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd08222   6 RKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDETVDANREAkLLSKLDHPAIVKFHDSFVEKESFCIVTEYCE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHL----QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd08222  86 GGDLDDKIseykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGISRILMGTSDLATT 164
                       170       180       190
                ....*....|....*....|....*....|....
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEM 354
Cdd:cd08222 165 FTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEM 198
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
154-419 2.74e-28

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: 113.96  E-value: 2.74e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 154 NPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTT 233
Cdd:cd06657  14 DPGDPRTYLDNFIKIGEGSTGIVCIATVKSSGKLVAVK----KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAeIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA 313
Cdd:cd06657  90 DELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLA-VLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY----CRDVAEMYDNILHKPLSLRPgVSLTAW 389
Cdd:cd06657 169 EVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFneppLKAMKMIRDNLPPKLKNLHK-VSPSLK 247
                       250       260       270
                ....*....|....*....|....*....|
gi 75813626 390 SILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd06657 248 GFLDRLLVRDPAQRATAA----ELLKHPFL 273
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
164-373 2.78e-28

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: 112.98  E-value: 2.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   164 FLKVIGKGSFGKVLLAKRKLDGKFY----AVKVLQKKivLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:pfam07714   3 LGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEG--ADEEEREDFLEEASIM-KKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   240 LDFVNGGELFFHLQRERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTT 318
Cdd:pfam07714  80 TEYMPGGDLLDFLRKHKRKLTLKDLLsMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRD-IYDDDYY 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626   319 TTFCGTPE---YLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:pfam07714 159 RKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFL 217
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
168-419 4.35e-28

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: 113.19  E-value: 4.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKE---QKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALK----KVALRKLEggiPNQALREIKALQACQGHPYVVKLRDVFPHGTGFVLVFEYML 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GG--ELFFHlqRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAISDTTTTF- 321
Cdd:cd07832  84 SSlsEVLRD--EERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLAR--LFSEEDPRLYs 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 --CGTPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCR-DVAEM-----------------------YDNIL 374
Cdd:cd07832 160 hqVATRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNGSPLFPGEnDIEQLaivlrtlgtpnektwpeltslpdYNKIT 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 375 ---HKPLSLR---PGVSLTAWSILEELLEKDRQNRLGAKEDFleiqNHPFF 419
Cdd:cd07832 240 fpeSKGIRLEeifPDCSPEAIDLLKGLLVYNPKKRLSAEEAL----RHPYF 286
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
166-360 5.79e-28

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: 112.47  E-value: 5.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVK---VLQKKIVLNRKEQKHIMAERNV---LLKNVKHPFLVGlHYSFQTTEKLYFV 239
Cdd:cd06629   7 ELIGKGTYGRVYLAMNATTGEMLAVKqveLPKTSSDRADSRQKTVVDALKSeidTLKDLDHPNIVQ-YLGFEETEDYFSI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 -LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGIAISD 316
Cdd:cd06629  86 fLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKksDDIYGNN 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 317 TTTTFCGTPEYLAPEVI--RKQPYDNTVDWWCLGAVLYEMLYGLPP 360
Cdd:cd06629 166 GATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRP 211
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
161-362 7.04e-28

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: 112.55  E-value: 7.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVL------QKKIVLNRK--EQKHIMAERNVLLKNVKHPflvGLHYSfqt 232
Cdd:cd14171   7 EVNWTQKLGTGISGPVRVCVKKSTGERFALKILldrpkaRTEVRLHMMcsGHPNIVQIYDVYANSVQFP---GESSP--- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 TEKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-----DSVghVVLTDFGL 307
Cdd:cd14171  81 RARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnseDAP--IKLCDFGF 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 308 CKEGIAiSDTTTTFcgTPEYLAPEVIRKQ-----------------PYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd14171 159 AKVDQG-DLMTPQF--TPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFY 227
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
171-419 7.24e-28

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: 111.87  E-value: 7.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 171 GSFGKVLLAKRKLDGKFYAVKVLqkkivlnRKEQKHIMAERNVLLKNVkhPFLVGLHYSFQTTEKLYFVLDFVNGGELFF 250
Cdd:cd05576  10 GVIDKVLLVMDTRTQETFILKGL-------RKSSEYSRERKTIIPRCV--PNMVCLRKYIISEESVFLVLQHAEGGKLWS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 251 HLQR---------------ER-------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd05576  81 YLSKflndkeihqlfadldERlaaasrfYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 309 KEgiaISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMydniLHKPLSLRPGVSLTA 388
Cdd:cd05576 161 SE---VEDSCDSDAIENMYCAPEVGGISEETEACDWWSLGALLFELLTGKALVECHPAGIN----THTTLNIPEWVSEEA 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 75813626 389 WSILEELLEKDRQNRLGAKEDFLE-IQNHPFF 419
Cdd:cd05576 234 RSLLQQLLQFNPTERLGAGVAGVEdIKSHPFF 265
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
164-355 7.68e-28

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: 111.75  E-value: 7.68e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKLDGKFyavkVLQKKIVLNR---KEQKHIMAERnVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd08221   4 PVRVLGRGAFGEAVLYRKTEDNSL----VVWKEVNLSRlseKERRDALNEI-DILSLLNHDNIITYYNHFLDGESLFIEM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERS--FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT 318
Cdd:cd08221  79 EYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMA 158
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd08221 159 ESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELL 195
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
164-373 8.24e-28

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: 111.49  E-value: 8.24e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    164 FLKVIGKGSFGKVLLA--KRKLDGKFY--AVKVLQKKIvlNRKEQKHIMAErNVLLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:smart00221   3 LGKKLGEGAFGEVYKGtlKGKGDGKEVevAVKTLKEDA--SEQQIEEFLRE-ARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    240 LDFVNGGEL--FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDT 317
Cdd:smart00221  80 MEYMPGGDLldYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRD-LYDDDY 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626    318 TTTFCGT-P-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:smart00221 159 YKVKGGKlPiRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYL 217
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
133-361 9.69e-28

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: 112.51  E-value: 9.69e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 133 DERSSQKLHStsqninLGPSGNPHAKPTDFDflkVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERN 212
Cdd:cd06654   2 DEEILEKLRS------IVSVGDPKKKYTRFE---KIGQGASGTVYTAMDVATGQEVAIRQMN----LQQQPKKELIINEI 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 213 VLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENI 292
Cdd:cd06654  69 LVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT-DVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNI 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 293 LLDSVGHVVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06654 148 LLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
162-361 1.21e-27

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: 112.03  E-value: 1.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLqKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKF-KESEDDEDVKKTALREVKVL-RQLRHENIVNLKEAFRRKGRLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVnGGELFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT-T 319
Cdd:cd07833  81 YV-ERTLLELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPASPlT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75813626 320 TFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07833 160 DYVATRWYRAPELLVGDTnYGKPVDVWAIGCIMAELLDGEPLF 202
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
164-373 1.38e-27

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 111.08  E-value: 1.38e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    164 FLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLN--RKEQKHIMAErNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKLKGKGGKKKVEVAVKTLKEDasEQQIEEFLRE-ARIMRKLDHPNVVKLLGVCTEEEPLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626    242 FVNGGELFFHLQRERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGiaISDTTTT 320
Cdd:smart00219  82 YMEGGDLLSYLRKNRPKLSLSDLLsFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL--YDDDYYR 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626    321 FCGTPE---YLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:smart00219 160 KRGGKLpirWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYL 216
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
167-418 2.03e-27

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 110.70  E-value: 2.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVK--VLQKKIVLNRKEQKHIMA--ERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06628   7 LIGSGSFGSVYLGMNASSGELMAVKqvELPSVSAENKDRKKSMLDalQREIaLLRELQHENIVQYLGSSSDANHLNIFLE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTT- 320
Cdd:cd06628  87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNn 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 321 -----FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycRDVAEMyDNILHKPLSLRPGV----SLTAWSI 391
Cdd:cd06628 167 garpsLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF--PDCTQM-QAIFKIGENASPTIpsniSSEARDF 243
                       250       260
                ....*....|....*....|....*..
gi 75813626 392 LEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd06628 244 LEKTFEIDHNKRPTAD----ELLKHPF 266
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
167-403 2.35e-27

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 114.73  E-value: 2.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  167 VIGKGSFGKVLLAKRkldGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHpFLVGLHYS-FQTTEKLYFVLDFVNG 245
Cdd:PTZ00267  74 LVGRNPTTAAFVATR---GSDPKEKVVAKFVMLNDERQAAYARSELHCLAACDH-FGIVKHFDdFKSDDKLLLIMEYGSG 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  246 GELFFHLQ---RER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GIAIS-DTTT 319
Cdd:PTZ00267 150 GDLNKQIKqrlKEHlPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQySDSVSlDVAS 229
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP-GVSLTAWSILEELLEK 398
Cdd:PTZ00267 230 SFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYDPFPcPVSSGMKALLDPLLSK 309

                 ....*
gi 75813626  399 DRQNR 403
Cdd:PTZ00267 310 NPALR 314
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
168-378 4.66e-27

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: 109.12  E-value: 4.66e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLakrkldGKFYAVKVLQKKIV-LNRKEQKHimaernvlLKNVKHPFLVglhySFQ---TTEKLYFVL-DF 242
Cdd:cd14059   1 LGSGAQGAVFL------GKFRGEEVAVKKVRdEKETDIKH--------LRKLNHPNII----KFKgvcTQAPCYCILmEY 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISdTTTTFC 322
Cdd:cd14059  63 CPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKS-TKMSFA 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycRDV---AEMY---DNILHKPL 378
Cdd:cd14059 142 GTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY--KDVdssAIIWgvgSNSLQLPV 201
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
168-413 6.64e-27

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: 109.28  E-value: 6.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKlDGKFYAVKVLQKKIVLNRKEQkhimAERNV-LLKNVKHPFLVGLH-YSFQTTEKLyFVLDFVNG 245
Cdd:cd14066   1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAASKKE----FLTELeMLGRLRHPNLVRLLgYCLESDEKL-LVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEH--RARF-YAAEIASALGYLHS---IKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT-- 317
Cdd:cd14066  75 GSLEDRLHCHKGSPPLpwPQRLkIAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVsk 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYcRDVAEMYDNILHKplSLRPGVSLTAWSILEELLE 397
Cdd:cd14066 155 TSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVD-ENRENASRKDLVE--WVESKGKEELEDILDKRLV 231
                       250
                ....*....|....*.
gi 75813626 398 KDRQNRLGAKEDFLEI 413
Cdd:cd14066 232 DDDGVEEEEVEALLRL 247
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
166-408 1.06e-26

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: 108.46  E-value: 1.06e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14193  10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKAR---SQKEKEEVKNEIEVM-NQLNHANLIQLYDAFESRNDIVLVMEYVDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS--VGHVVLTDFGLCKEGIAISDTTTTFc 322
Cdd:cd14193  86 GELFDRIIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSreANQVKIIDFGLARRYKPREKLRVNF- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSILEELLEK 398
Cdd:cd14193 165 GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEdeefADISEEAKDFISKLLIK 244
                       250
                ....*....|
gi 75813626 399 DRQNRLGAKE 408
Cdd:cd14193 245 EKSWRMSASE 254
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
168-419 1.07e-26

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: 109.29  E-value: 1.07e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAE-RNV-LLKNVK---HPFLVGL----HYSFQTTE-KLY 237
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALK----KVRVPLSEEGIPLSTiREIaLLKQLEsfeHPNVVRLldvcHGPRTDRElKLT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGgELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GIAI 314
Cdd:cd07838  83 LVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIySFEM 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 SDTTTTFcgTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH------------------- 375
Cdd:cd07838 162 ALTSVVV--TLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDviglpseeewprnsalprs 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 376 --------KPLSLRPGVSLTAWSILEELLEKDRQNRLGAKEDFleiqNHPFF 419
Cdd:cd07838 240 sfpsytprPFKSFVPEIDEEGLDLLKKMLTFNPHKRISAFEAL----QHPYF 287
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
161-362 2.66e-26

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: 108.19  E-value: 2.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd08229  25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEID-LLKQLNHPNVIKYYASFIEDNELNIVL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGEL---FFHLQRERSF-PEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISD 316
Cdd:cd08229 104 ELADAGDLsrmIKHFKKQKRLiPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTT 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd08229 184 AAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFY 229
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
162-419 2.80e-26

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: 107.40  E-value: 2.80e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14191   4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFK---AYSAKEKENIRQEISIM-NCLHHPKLVQCVDAFEEKANIVMVLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVG-HVVLTDFGLCKEgIAISDTT 318
Cdd:cd14191  80 MVSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARR-LENAGSL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAWSILEE 394
Cdd:cd14191 159 KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISN 238
                       250       260
                ....*....|....*....|....*
gi 75813626 395 LLEKDRQNRLGAKEDFleiqNHPFF 419
Cdd:cd14191 239 LLKKDMKARLTCTQCL----QHPWL 259
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
167-362 3.05e-26

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: 107.49  E-value: 3.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGkVLLAKRKLDGKfyaVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVglHYSFQTTEKLYF--VLDFVN 244
Cdd:cd06624  15 VLGKGTFG-VVYAARDLSTQ---VRIAIKEIPERDSREVQPLHEEIALHSRLSHKNIV--QYLGSVSEDGFFkiFMEQVP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFfHLQRERSFP----EHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVV-LTDFGLCKEGIAISDTTT 319
Cdd:cd06624  89 GGSLS-ALLRSKWGPlkdnENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSGVVkISDFGTSKRLAGINPCTE 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75813626 320 TFCGTPEYLAPEVIRKQP--YDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd06624 168 TFTGTLQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFI 212
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
161-361 3.63e-26

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: 107.66  E-value: 3.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLnrKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd06619   2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDITV--ELQKQIMSELEILYK-CDSPYIIGFYGAFFVENRISICT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHlqreRSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiAISDTTTT 320
Cdd:cd06619  79 EFMDGGSLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQ--LVNSIAKT 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06619 153 YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPY 193
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
159-418 8.71e-26

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: 106.26  E-value: 8.71e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVL--QKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTE-- 234
Cdd:cd06653   1 PVNWRLGKLLGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVNALECEIQ-LLKNLRHDRIVQYYGCLRDPEek 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG-------L 307
Cdd:cd06653  80 KLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskriqtI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 308 CKEGIAISDTTttfcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLS--LRPGVS 385
Cdd:cd06653 160 CMSGTGIKSVT----GTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIATQPTKpqLPDGVS 235
                       250       260       270
                ....*....|....*....|....*....|...
gi 75813626 386 LTAWSILEELLEKDRqnRLGAKEDFLEiqnHPF 418
Cdd:cd06653 236 DACRDFLRQIFVEEK--RRPTAEFLLR---HPF 263
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
159-361 8.85e-26

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: 106.28  E-value: 8.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQ--KKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEK- 235
Cdd:cd06652   1 PTNWRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQfdPESPETSKEVNALECEIQ-LLKNLLHERIVQYYGCLRDPQEr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 -LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGI 312
Cdd:cd06652  80 tLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKrlQTI 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDT-TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06652 160 CLSGTgMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
162-361 9.18e-26

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: 106.74  E-value: 9.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkkIVLNRKEQKHI--MAERNV-LLKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd07846   3 YENLGLVGEGSYGMVMKCRHKETGQIVAIK-----KFLESEDDKMVkkIAMREIkMLKQLRHENLVNLIEVFRRKKRWYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT 318
Cdd:cd07846  78 VFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAAPGEVY 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75813626 319 TTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07846 158 TDYVATRWYRAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLF 201
PX_domain cd06093
The Phox Homology domain, a phosphoinositide binding module; The PX domain is a ...
15-119 1.23e-25

The Phox Homology domain, a phosphoinositide binding module; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to membranes. Proteins containing PX domains interact with PIs and have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. Many members of this superfamily bind phosphatidylinositol-3-phosphate (PI3P) but in some cases, other PIs such as PI4P or PI(3,4)P2, among others, are the preferred substrates. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction, as in the cases of p40phox, p47phox, and some sorting nexins (SNXs). The PX domain is conserved from yeast to humans and is found in more than 100 proteins. The majority of PX domain-containing proteins are SNXs, which play important roles in endosomal sorting.


Pssm-ID: 132768 [Multi-domain]  Cd Length: 106  Bit Score: 100.90  E-value: 1.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  15 SVSIPSSDEHREKKKRFTVYKVLVSV-GRSEWFVFRRYAEFDKLYNTLKKQFPAMAL-KIPAKRIFGdNFDPDFIKQRRA 92
Cdd:cd06093   1 SVSIPDYEKVKDGGKKYVVYIIEVTTqGGEEWTVYRRYSDFEELHEKLKKKFPGVILpPLPPKKLFG-NLDPEFIEERRK 79
                        90       100
                ....*....|....*....|....*..
gi 75813626  93 GLNEFIQNLVRYPELYNHPDVRAFLQM 119
Cdd:cd06093  80 QLEQYLQSLLNHPELRNSEELKEFLEL 106
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
162-419 1.39e-25

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: 105.36  E-value: 1.39e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlknvKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14114   4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQL----HHPKLINLHDAFEDDNEMVLILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRE-RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD--SVGHVVLTDFGLC-----KEGIA 313
Cdd:cd14114  80 FLSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLAthldpKESVK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 IsdttTTfcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI----LHKPLSLRPGVSLTAW 389
Cdd:cd14114 160 V----TT--GTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVkscdWNFDDSAFSGISEEAK 233
                       250       260       270
                ....*....|....*....|....*....|
gi 75813626 390 SILEELLEKDRQNRLGAKEDFLeiqnHPFF 419
Cdd:cd14114 234 DFIRKLLLADPNKRMTIHQALE----HPWL 259
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
162-361 1.52e-25

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: 106.25  E-value: 1.52e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlnrkEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14177   6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDK-------SKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGH---VVLTDFGLCKEGIAISDT 317
Cdd:cd14177  79 LMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENGL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14177 159 LLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF 202
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
162-419 3.53e-25

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: 104.20  E-value: 3.53e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKF----IPLRSSTRARAFQERD-ILARLSHRRLTCLLDQFETRKTLILILE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH--VVLTDFGLCKEgIAISDTTT 319
Cdd:cd14107  79 LCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTRedIKICDFGFAQE-ITPSEHQF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRP----GVSLTAWSILEEL 395
Cdd:cd14107 158 SKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTpeitHLSEDAKDFIKRV 237
                       250       260
                ....*....|....*....|....
gi 75813626 396 LEKDRQNRLGAkedfLEIQNHPFF 419
Cdd:cd14107 238 LQPDPEKRPSA----SECLSHEWF 257
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
165-361 4.69e-25

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: 104.81  E-value: 4.69e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAvkvlqKKIVL---NRKEQKHIMAERNVLlKNVKHPFLVGLHYSF--QTTEKLYFV 239
Cdd:cd06621   6 LSSLGEGAGGSVTKCRLRNTKTIFA-----LKTITtdpNPDVQKQILRELEIN-KSCASPYIVKYYGAFldEQDSSIGIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERS----FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiAIS 315
Cdd:cd06621  80 MEYCEGGSLDSIYKKVKKkggrIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGE--LVN 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06621 158 SLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF 203
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
165-361 8.86e-25

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 103.57  E-value: 8.86e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLqkkIVLNRKEQKHIMAERNVLLKNVKHPFLVGL--HYSFQTTEKLYFVL-- 240
Cdd:cd13985   5 TKQLGEGGFSYVYLAHDVNTGRRYALKRM---YFNDEEQLRVAIKEIEIMKRLCGHPNIVQYydSAILSSEGRKEVLLlm 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVnGGELFFHLQRE--RSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFG---------L 307
Cdd:cd13985  82 EYC-PGSLVDILEKSppSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsattehyplE 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 308 CKEGIAISDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd13985 161 RAEEVNIIEEEIQKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPF 217
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
161-362 1.37e-24

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 102.82  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd06645  12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIK----LEPGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGEL--FFHLQRERSfpEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT 318
Cdd:cd06645  88 EFCGGGSLqdIYHVTGPLS--ESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKR 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 319 TTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd06645 166 KSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMF 212
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
166-419 1.41e-24

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: 102.31  E-value: 1.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIV-----LNRKEQkhIMAERNVLLK--NVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd14005   6 DLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVtewamINGPVP--VPLEIALLLKasKPGVPGVIRLLDWYERPDGFLL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGE-LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV-GHVVLTDFGlCkeGIAISD 316
Cdd:cd14005  84 IMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRtGEVKLIDFG-C--GALLKD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TT-TTFCGTPEYLAPEVIRKQPYDN---TVdwWCLGAVLYEMLYGLPPFYcRDVAEMYDNILHkplslRPGVSLTAWSIL 392
Cdd:cd14005 161 SVyTDFDGTRVYSPPEWIRHGRYHGrpaTV--WSLGILLYDMLCGDIPFE-NDEQILRGNVLF-----RPRLSKECCDLI 232
                       250       260
                ....*....|....*....|....*..
gi 75813626 393 EELLEKDRQNRLgakeDFLEIQNHPFF 419
Cdd:cd14005 233 SRCLQFDPSKRP----SLEQILSHPWF 255
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
157-362 1.74e-24

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: 103.15  E-value: 1.74e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 157 AKPTD-FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkiVLNRKEQkhIMAERNVLLKNVKHPFLVGLHYSFQTTEK 235
Cdd:cd06639  18 ADPSDtWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDP--ISDVDEE--IEAEYNILRSLPNHPNVVKFYGMFYKADQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 -----LYFVLDFVNGG---ELFFH-LQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd06639  94 yvggqLWLVLELCNGGsvtELVKGlLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 307 LCKEGIAISDTTTTFCGTPEYLAPEVIR-KQPYDNT----VDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd06639 174 VSAQLTSARLRRNTSVGTPFWMAPEVIAcEQQYDYSydarCDVWSLGITAIELADGDPPLF 234
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
159-361 1.89e-24

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: 102.78  E-value: 1.89e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTD-FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkiVLNRKEQkhIMAERNVLLKNVKHPFLV---GLHYS--FQT 232
Cdd:cd06638  16 PSDtWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDP--IHDIDEE--IEAEYNILKALSDHPNVVkfyGMYYKkdVKN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 TEKLYFVLDFVNGGELF----FHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd06638  92 GDQLWLVLELCNGGSVTdlvkGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVS 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 309 KEGIAISDTTTTFCGTPEYLAPEVIR-----KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06638 172 AQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPL 229
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
165-361 3.27e-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: 102.35  E-value: 3.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd07870   5 LEKLGEGSYATVYKGISRINGQLVALKV----ISMKTEEGVPFTAIREAsLLKGLKHANIVLLHDIIHTKETLTFVFEYM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCG 323
Cdd:cd07870  81 HTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYSSEVV 160
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 324 TPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07870 161 TLWYRPPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAF 199
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
162-360 3.49e-24

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: 102.05  E-value: 3.49e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLlakRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06640   6 FTKLERIGKGSFGEVF---KGIDNRTQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTF 321
Cdd:cd06640  83 YLGGGSAL-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPP 360
Cdd:cd06640 162 VGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
158-361 4.34e-24

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: 101.75  E-value: 4.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQT-TEKL 236
Cdd:cd06620   3 KNQDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIH--IDAKSSVRKQILRELQIL-HECHSPYIVSFYGAFLNeNNNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSI-KIVYRDLKPENILLDSVGHVVLTDFGLCKEGI-AI 314
Cdd:cd06620  80 IICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELInSI 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 315 SDtttTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06620 160 AD---TFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF 203
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
164-419 4.84e-24

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: 102.06  E-value: 4.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKLDGKFYAVKV--LQKKIVLNRKEQKHIMAERNVLL-KNVKHPFLVGLHYSFQ-TTEKLYFV 239
Cdd:cd14040  10 LLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIhKELDHPRIVKLYDYFSlDTDTFCTV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILL---DSVGHVVLTDFGLCK----- 309
Cdd:cd14040  90 LEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimddd 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 -EGIAISDTTTTFCGTPEYLAPE--VIRKQP--YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAE--MYDNILHKP----L 378
Cdd:cd14040 170 sYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdiLQENTILKAtevqF 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 75813626 379 SLRPGVSLTAWSILEELLEKDRQNRLgakeDFLEIQNHPFF 419
Cdd:cd14040 250 PVKPVVSNEAKAFIRRCLAYRKEDRF----DVHQLASDPYL 286
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
168-361 4.89e-24

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: 101.96  E-value: 4.89e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAErnvLLKNVKHPFLVGLHYSFQTTEKL------YFVLD 241
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQ---IMKRLNHPNVVAARDVPEGLQKLapndlpLLAME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERS---FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS----VGHVVLtDFGLCKEgIAI 314
Cdd:cd14038  79 YCQGGDLRKYLNQFENccgLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQgeqrLIHKII-DLGYAKE-LDQ 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 315 SDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14038 157 GSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
162-418 6.62e-24

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: 101.09  E-value: 6.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKV-----LLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLknvkhpflvgLHYSFQTTEKL 236
Cdd:cd14104   2 YMIAEELGRGQFGIVhrcveTSSKKTYMAKFVKVKGADQVLVKKEISILNIARHRNILR----------LHESFESHEEL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS-VGHVV-LTDFGLCKEgIA 313
Cdd:cd14104  72 VMIFEFISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTrRGSYIkIIEFGQSRQ-LK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR----PGVSLTAW 389
Cdd:cd14104 151 PGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEAL 230
                       250       260
                ....*....|....*....|....*....
gi 75813626 390 SILEELLEKDRQNRLGAKEDFleiqNHPF 418
Cdd:cd14104 231 DFVDRLLVKERKSRMTAQEAL----NHPW 255
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
162-419 1.08e-23

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: 100.42  E-value: 1.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKI-----VLNRKEqkhIMAERNVllknVKHPFLVGLH---YSfQTT 233
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFksleqVNNLRE---IQALRRL----SPHPNILRLIevlFD-RKT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGgELFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVVLTDFGLCKeGI 312
Cdd:cd07831  73 GRLALVFELMDM-NLYELIKgRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGSCR-GI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDTTTTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIlHKPL------------- 378
Cdd:cd07831 150 YSKPPYTEYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKI-HDVLgtpdaevlkkfrk 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 379 -----------------SLRPGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd07831 229 srhmnynfpskkgtglrKLLPNASAEGLDLLKKLLAYDPDERITAK----QALRHPYF 282
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
162-396 1.54e-23

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: 99.51  E-value: 1.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14111   5 YTFLDEKARGRFGVIRRCRENATGKNFPAKI----VPYQAEEKQGVLQEYEIL-KSLHHERIMALHEAYITPRYLVLIAE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAIS-DTTTT 320
Cdd:cd14111  80 FCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSlRQLGR 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL---HKPLSLRPGVSLTAWSILEELL 396
Cdd:cd14111 160 RTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILvakFDAFKLYPNVSQSASLFLKKVL 238
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
161-362 1.55e-23

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 104.82  E-value: 1.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSF--QTTEKLYF 238
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYR-GLKEREKSQLVIEVNVM-RELKHKNIVRYIDRFlnKANQKLYI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   239 VLDFVNGGELFFHLQR-ERSF---PEHRARFYAAEIASALGYLHSIK-------IVYRDLKPENILLDS----VGHVV-- 301
Cdd:PTZ00266   92 LMEFCDAGDLSRNIQKcYKMFgkiEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTgirhIGKITaq 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75813626   302 -----------LTDFGLCKEgIAISDTTTTFCGTPEYLAPEVI--RKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:PTZ00266  172 annlngrpiakIGDFGLSKN-IGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFH 244
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
167-361 1.62e-23

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: 99.39  E-value: 1.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKldGKFYAVKVLQKKIvlnrkEQKHIMAERNV-----LLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14061   1 VIGVGGFGKVYRGIWR--GEEVAVKAARQDP-----DEDISVTLENVrqearLFWMLRHPNIIALRGVCLQPPNLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQReRSFPEHRARFYAAEIASALGYLHS---IKIVYRDLKPENILL------DSVGHVVL--TDFGLCKE 310
Cdd:cd14061  74 YARGGALNRVLAG-RKIPPHVLVDWAIQIARGMNYLHNeapVPIIHRDLKSSNILIleaienEDLENKTLkiTDFGLARE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 311 giaISDTT-TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14061 153 ---WHKTTrMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY 201
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
161-356 1.95e-23

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: 99.49  E-value: 1.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEqkhimAERNV-LLKNVKHPFLVGLHYSFQ-------- 231
Cdd:cd14047   7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIK----RVKLNNEK-----AEREVkALAKLDHPNIVRYNGCWDgfdydpet 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 232 --------TTEKLYFVLDFVNGGELFFHLQRERSFP----EHRARFYaaEIASALGYLHSIKIVYRDLKPENILLDSVGH 299
Cdd:cd14047  78 sssnssrsKTKCLFIQMEFCEKGTLESWIEKRNGEKldkvLALEIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 300 VVLTDFGLCKEgIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY 356
Cdd:cd14047 156 VKIGDFGLVTS-LKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLH 211
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
168-361 2.50e-23

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: 99.06  E-value: 2.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRkEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIE-ERKALLKEAEKMER-ARHSYVLPLLGVCVERRSLGLVMEYMENGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARF-YAAEIASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFGLCKEGIAI-----SDTTT 319
Cdd:cd13978  79 LKSLLEREIQDVPWSLRFrIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSisanrRRGTE 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTV--DWWCLGAVLYEMLYGLPPF 361
Cdd:cd13978 159 NLGGTPIYMAPEAFDDFNKKPTSksDVYSFAIVIWAVLTRKEPF 202
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
167-418 4.54e-23

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 98.28  E-value: 4.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKlDGKFYAVKvlqkKIVLN-----RKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd06631   8 VLGKGAYGTVYCGLTS-TGQLIAVK----QVELDtsdkeKAEKEYEKLQEEVdLLKTLKHVNIVGYLGTCLEDNVVSIFM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGlCKEGIAI------ 314
Cdd:cd06631  83 EFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFG-CAKRLCInlssgs 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 -SDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycRDVAEM----YDNILHKPL-SLRPGVSLTA 388
Cdd:cd06631 162 qSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPW--ADMNPMaaifAIGSGRKPVpRLPDKFSPEA 239
                       250       260       270
                ....*....|....*....|....*....|
gi 75813626 389 WSILEELLEKDRQNRLGAkedfLEIQNHPF 418
Cdd:cd06631 240 RDFVHACLTRDQDERPSA----EQLLKHPF 265
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
162-360 5.01e-23

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: 98.61  E-value: 5.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhiMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIED---IQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTF 321
Cdd:cd06641  83 YLGGGSAL-DLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*F 161
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPP 360
Cdd:cd06641 162 VGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
164-419 6.36e-23

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: 97.68  E-value: 6.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLK---VIGKGSFGKVLLAKRKLDGKFYAVKVLQKKiVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd13983   2 YLKfneVLGRGSFKTVYRAFDTEEGIEVAWNEIKLR-KLPKAERQRFKQEIE-ILKSLKHPNIIKFYDSWESKSKKEVIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 --DFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILLD-SVGHVVLTDFGLCKEGIAis 315
Cdd:cd13983  80 itELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQ-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQpYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILH--KPLSLRPGVSLTAWSIL 392
Cdd:cd13983 158 SFAKSVIGTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYSeCTNAAQIYKKVTSgiKPESLSKVKDPELKDFI 236
                       250       260
                ....*....|....*....|....*..
gi 75813626 393 EELLEKdRQNRLGAKedflEIQNHPFF 419
Cdd:cd13983 237 EKCLKP-PDERPSAR----ELLEHPFF 258
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
162-418 7.46e-23

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: 98.16  E-value: 7.46e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSF------QTTEK 235
Cdd:cd06636  18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTEDEEEEIKLEINMLKKYSHHRNIATYYGAFikksppGHDDQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRER--SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA 313
Cdd:cd06636  94 LWLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTPEYLAPEVI--RKQP---YDNTVDWWCLGAVLYEMLYGLPPFyCrDVAEMYDNILhKPLSLRPGVSLTA 388
Cdd:cd06636 174 TVGRRNTFIGTPYWMAPEVIacDENPdatYDYRSDIWSLGITAIEMAEGAPPL-C-DMHPMRALFL-IPRNPPPKLKSKK 250
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75813626 389 WS-----ILEELLEKDRQNRlGAKEDFLEiqnHPF 418
Cdd:cd06636 251 WSkkfidFIEGCLVKNYLSR-PSTEQLLK---HPF 281
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
164-408 8.11e-23

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: 98.59  E-value: 8.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKLDGKFYAVKV--LQKKIVLNRKEQKHIMAERNVLL-KNVKHPFLVGLHYSFQ-TTEKLYFV 239
Cdd:cd14041  10 LLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKKENYHKHACREYRIhKELDHPRIVKLYDYFSlDTDSFCTV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILL---DSVGHVVLTDFGLCK----- 309
Cdd:cd14041  90 LEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGLSKimddd 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 --EGIAISDTTTTFCGTPEYLAPE--VIRKQP--YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAE--MYDNILHKPLSL- 380
Cdd:cd14041 170 syNSVDGMELTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQdiLQENTILKATEVq 249
                       250       260       270
                ....*....|....*....|....*....|.
gi 75813626 381 ---RPGVSLTAWSILEELLEKDRQNRLGAKE 408
Cdd:cd14041 250 fppKPVVTPEAKAFIRRCLAYRKEDRIDVQQ 280
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
162-408 8.13e-23

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: 98.21  E-value: 8.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhiMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06642   6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDEIED---IQQEITVLSQCDSPYITRYYGSYLKGTKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTF 321
Cdd:cd06642  83 YLGGGSAL-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycRDVAEMYDNIL---HKPLSLRPGVSLTAWSILEELLEK 398
Cdd:cd06642 162 VGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN--SDLHPMRVLFLipkNSPPTLEGQHSKPFKEFVEACLNK 239
                       250
                ....*....|
gi 75813626 399 DRQNRLGAKE 408
Cdd:cd06642 240 DPRFRPTAKE 249
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
166-419 9.44e-23

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: 97.50  E-value: 9.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKvlQKKIVLN-RKEQKHIMA---ERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06630   6 PLLGTGAFSSCYQARDVKTGTLMAVK--QVSFCRNsSSEQEEVVEairEEIRMMARLNHPNIVRMLGATQHKSHFNIFVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG-HVVLTDFG----LCKEGIAISD 316
Cdd:cd06630  84 WMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGaaarLASKGTGAGE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH---------KPLSLRPGVSlt 387
Cdd:cd06630 164 FQGQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKiasattpppIPEHLSPGLR-- 241
                       250       260       270
                ....*....|....*....|....*....|..
gi 75813626 388 awSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd06630 242 --DVTLRCLELQPEDRPPAR----ELLKHPVF 267
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
160-393 1.39e-22

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: 97.25  E-value: 1.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVL--NRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTT---- 233
Cdd:cd14048   6 TDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVK----RIRLpnNELAREKVLREVRALAK-LDHPGIVRYFNAWLERppeg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 --EK-----LYFVLDFVNGGELFFHLQRERSFpEHRARFYA----AEIASALGYLHSIKIVYRDLKPENILLDSVGHVVL 302
Cdd:cd14048  81 wqEKmdevyLYIQMQLCRKENLKDWMNRRCTM-ESRELFVClnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 303 TDFGLC------------KEGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG------------- 357
Cdd:cd14048 160 GDFGLVtamdqgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSfstqmerirtltd 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 75813626 358 -----LPPFYCRDVAEMYDnILHKPLSLRPGVSLTAWSILE 393
Cdd:cd14048 240 vrklkFPALFTNKYPEERD-MVQQMLSPSPSERPEAHEVIE 279
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
161-362 1.64e-22

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 97.02  E-value: 1.64e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd06646  10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIK----LEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGEL--FFHLQRERSfpEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT 318
Cdd:cd06646  86 EYCGGGSLqdIYHVTGPLS--ELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKR 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 319 TTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd06646 164 KSFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPMF 210
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
165-368 2.07e-22

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: 97.00  E-value: 2.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd07871  10 LDKLGEGTYATVFKGRSKLTENLVALK----EIRLEHEEGAPCTAIREVsLLKNLKHANIVTLHDIIHTERCLTLVFEYL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGgELFFHLQRERSFPE-HRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFC 322
Cdd:cd07871  86 DS-DLKQYLDNCGNLMSmHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSNEV 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 323 GTPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAE 368
Cdd:cd07871 165 VTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKE 211
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
165-419 2.31e-22

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: 96.18  E-value: 2.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHImaeR--NVLLKNVK--HPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14133   4 LEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDQSLDEI---RllELLNKKDKadKYHIVRLKDVFYFKNHLCIVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVnGGELFFHLQ--RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG--HVVLTDFGLCKEgiaISD 316
Cdd:cd14133  81 ELL-SQNLYEFLKqnKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGSSCF---LTQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL-------HKPLSLRPGVSLTAW 389
Cdd:cd14133 157 RLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIgtigippAHMLDQGKADDELFV 236
                       250       260       270
                ....*....|....*....|....*....|
gi 75813626 390 SILEELLEKDRQNRLGAKEDFleiqNHPFF 419
Cdd:cd14133 237 DFLKKLLEIDPKERPTASQAL----SHPWL 262
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
162-355 2.76e-22

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: 96.80  E-value: 2.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRK-EQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd07860   2 FQKVEKIGEGTYGVVYKARNKLTGEVVALK----KIRLDTEtEGVPSTAIREIsLLKELNHPNIVKLLDVIHTENKLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGG-ELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GIAISdT 317
Cdd:cd07860  78 FEFLHQDlKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAfGVPVR-T 156
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEML 355
Cdd:cd07860 157 YTHEVVTLWYRAPEILLGCKYYSTaVDIWSLGCIFAEMV 195
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
165-361 3.85e-22

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: 96.30  E-value: 3.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd07844   5 LDKLGEGSYATVYKGRSKLTGQLVALKE----IRLEHEEGAPFTAIREAsLLKDLKHANIVTLHDIIHTKKTLTLVFEYL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGgELFFHLQRERSFPE-HRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISDTTTTFC 322
Cdd:cd07844  81 DT-DLKQYMDDCGGGLSmHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR---AKSVPSKTYS 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75813626 323 G---TPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07844 157 NevvTLWYRPPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLF 199
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
159-423 4.03e-22

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: 97.36  E-value: 4.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKLDGkfyaVKVLQKKivLNRKEQKHIMAERNV----LLKNVKHPFLVGLHYSFQTTE 234
Cdd:cd07851  14 PDRYQNLSPVGSGAYGQVCSAFDTKTG----RKVAIKK--LSRPFQSAIHAKRTYrelrLLKHMKHENVIGLLDVFTPAS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KL------YFVLDFVnGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd07851  88 SLedfqdvYLVTHLM-GADLN-NIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 309 KEgiaISDTTTTFCGTPEYLAPEVI-RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL------------- 374
Cdd:cd07851 166 RH---TDDEMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMnlvgtpdeellkk 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 375 -----------------HKPLS-LRPGVSLTAWSILEELLEKDRQNRLGAKEDFLeiqnHPFFESLS 423
Cdd:cd07851 243 issesarnyiqslpqmpKKDFKeVFSGANPLAIDLLEKMLVLDPDKRITAAEALA----HPYLAEYH 305
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
166-361 4.39e-22

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: 95.92  E-value: 4.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQ--KKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQ--TTEKLYFVLD 241
Cdd:cd06651  13 KLLGQGAFGRVYLCYDVDTGRELAAKQVQfdPESPETSKEVSALECEIQ-LLKNLQHERIVQYYGCLRdrAEKTLTIFME 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG-------LCKEGIAI 314
Cdd:cd06651  92 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrlqtICMSGTGI 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 315 SDTTttfcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06651 172 RSVT----GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW 214
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
157-418 4.74e-22

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 96.29  E-value: 4.74e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 157 AKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkiVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKL 236
Cdd:cd06618  12 ADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRR--SGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVngGELFFHLQR--ERSFPEHRARFYAAEIASALGYL---HSIkiVYRDLKPENILLDSVGHVVLTDFGLckEG 311
Cdd:cd06618  90 FICMELM--STCLDKLLKriQGPIPEDILGKMTVSIVKALHYLkekHGV--IHRDVKPSNILLDESGNVKLCDFGI--SG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 312 IAI-SDTTTTFCGTPEYLAPEVIRKQP---YDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILHKP---LSLRPG 383
Cdd:cd06618 164 RLVdSKAKTRSAGCAAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRnCKTEFEVLTKILNEEppsLPPNEG 243
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75813626 384 VSLTAWSILEELLEKDRQNRlgakEDFLEIQNHPF 418
Cdd:cd06618 244 FSPDFCSFVDLCLTKDHRYR----PKYRELLQHPF 274
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
162-361 5.03e-22

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: 95.83  E-value: 5.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQ-KHIMAERNVLlKNVKHPFLV-----GLHYSFQTTEK 235
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALK----KILCHSKEDvKEAMREIENY-RLFNHPNILrlldsQIVKEAGGKKE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRERS----FPEHRARFYAAEIASALGYLHSIKIV---YRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd13986  77 VYLLLPYYKRGSLQDEIERRLVkgtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSM 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 309 ----------KEGIAISDTTTTFCgTPEYLAPEVIRKQPY---DNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd13986 157 nparieiegrREALALQDWAAEHC-TMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPF 221
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
142-361 6.51e-22

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 96.82  E-value: 6.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  142 STSQNINLGPSGNPHAKP--TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkivlNRKEQKHIMAERNV-LLKNV 218
Cdd:PLN00034  54 SSSSSSSSASGSAPSAAKslSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYG----NHEDTVRRQICREIeILRDV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  219 KHPFLVGLHYSFQTTEKLYFVLDFVNGGELFFHLQRERSFPEHRARfyaaEIASALGYLHSIKIVYRDLKPENILLDSVG 298
Cdd:PLN00034 130 NHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQFLADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAK 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626  299 HVVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVI----RKQPYDNTV-DWWCLGAVLYEMLYGLPPF 361
Cdd:PLN00034 206 NVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERIntdlNHGAYDGYAgDIWSLGVSILEFYLGRFPF 273
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
165-376 8.48e-22

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: 94.97  E-value: 8.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAkRKLDGKFYAVKVLQkkivLNRKEQKHIMAERN--VLLKNVKH-PFLVGLhYSFQTTE---KLYF 238
Cdd:cd14131   6 LKQLGKGGSSKVYKV-LNPKKKIYALKRVD----LEGADEQTLQSYKNeiELLKKLKGsDRIIQL-YDYEVTDeddYLYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFvngGEL----FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVVLTDFGLCKegiAI 314
Cdd:cd14131  80 VMEC---GEIdlatILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAK---AI 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 315 SDTTT-----TFCGTPEYLAPEVIRKQPYDNTV----------DWWCLGAVLYEMLYGLPPFYcrdvaeMYDNILHK 376
Cdd:cd14131 153 QNDTTsivrdSQVGTLNYMSPEAIKDTSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPFQ------HITNPIAK 223
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
162-418 8.94e-22

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: 95.56  E-value: 8.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSF------QTTEK 235
Cdd:cd06637   8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMD----VTGDEEEEIKQEINMLKKYSHHRNIATYYGAFikknppGMDDQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRER--SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIA 313
Cdd:cd06637  84 LWLVMEFCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTPEYLAPEVIR--KQP---YDNTVDWWCLGAVLYEMLYGLPPFyCrDVAEMYDNILhKPLSLRPGVSLTA 388
Cdd:cd06637 164 TVGRRNTFIGTPYWMAPEVIAcdENPdatYDFKSDLWSLGITAIEMAEGAPPL-C-DMHPMRALFL-IPRNPAPRLKSKK 240
                       250       260       270
                ....*....|....*....|....*....|....*
gi 75813626 389 W-----SILEELLEKDRQNRLGAKedflEIQNHPF 418
Cdd:cd06637 241 WskkfqSFIESCLVKNHSQRPSTE----QLMKHPF 271
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
161-353 9.91e-22

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: 94.80  E-value: 9.91e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVL-LAKRKLDGKFYAVKVLqKKIVLNRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd14052   1 RFANVELIGSGEFSQVYkVSERVPTGKVYAVKKL-KPNYAGAKDRLRRLEEVSILreLTLDGHDNIVQLIDSWEYHGHLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQ---RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAI 314
Cdd:cd14052  80 IQTELCENGSLDVFLSelgLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 315 SDTTTTfcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYE 353
Cdd:cd14052 160 RGIERE--GDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
165-422 1.05e-21

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: 96.17  E-value: 1.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAkrkLDGKFYAvKVLQKKivLNRKEQKHIMAERNV----LLKNVKHPFLVGLHYSFQTTEKL---- 236
Cdd:cd07880  20 LKQVGSGAYGTVCSA---LDRRTGA-KVAIKK--LYRPFQSELFAKRAYrelrLLKHMKHENVIGLLDVFTPDLSLdrfh 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 --YFVLDFVnGGELFFHLQRERsFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiai 314
Cdd:cd07880  94 dfYLVMPFM-GTDLGKLMKHEK-LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ---- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 SDTTTT-FCGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH----------------- 375
Cdd:cd07880 168 TDSEMTgYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKvtgtpskefvqklqsed 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 376 -----KPL---------SLRPGVSLTAWSILEELLEKDRQNRLGAKEDFLeiqnHPFFESL 422
Cdd:cd07880 248 aknyvKKLprfrkkdfrSLLPNANPLAVNVLEKMLVLDAESRITAAEALA----HPYFEEF 304
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
159-437 1.23e-21

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: 95.74  E-value: 1.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKLDGKfyavKVLQKKivLNRKEQKHIMAERN----VLLKNVKHPFLVGL------HY 228
Cdd:cd07879  14 PERYTSLKQVGSGAYGSVCSAIDKRTGE----KVAIKK--LSRPFQSEIFAKRAyrelTLLKHMQHENVIGLldvftsAV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 229 SFQTTEKLYFVLDFvnggeLFFHLQRERS--FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd07879  88 SGDEFQDFYLVMPY-----MQTDLQKIMGhpLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 LCKEGIAisdTTTTFCGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL----------- 374
Cdd:cd07879 163 LARHADA---EMTGYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILkvtgvpgpefv 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 375 -------------------HKPLS-LRPGVSLTAWSILEELLEKDRQNRLGAKEDFleiqNHPFFESLSWADlvQKKIPP 434
Cdd:cd07879 240 qkledkaaksyikslpkypRKDFStLFPKASPQAVDLLEKMLELDVDKRLTATEAL----EHPYFDSFRDAD--EETEQQ 313

                ...
gi 75813626 435 PFN 437
Cdd:cd07879 314 PYD 316
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
237-361 1.29e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 97.94  E-value: 1.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  237 YFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISD 316
Cdd:NF033483  83 YIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR---ALSS 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 75813626  317 TTTTFC----GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:NF033483 160 TTMTQTnsvlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF 208
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
167-361 1.48e-21

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: 94.22  E-value: 1.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKldGKFYAVKVLQKKIVLNRKEQKHIMAERNV-----------------LLKNVKHPFLVGLHYS 229
Cdd:cd14000   1 LLGDGGFGSVYRASYK--GEPVAVKIFNKHTSSNFANVPADTMLRHLratdamknfrllrqeltVLSHLHHPSIVYLLGI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 230 fqTTEKLYFVLDFVNGGELFFHLQRERSFPEHRARFY----AAEIASALGYLHSIKIVYRDLKPENILL-----DSVGHV 300
Cdd:cd14000  79 --GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLqqriALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIII 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 301 VLTDFGL----CKEGIaisdttTTFCGTPEYLAPEVIRKQ-PYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14000 157 KIADYGIsrqcCRMGA------KGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPM 216
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
162-361 1.77e-21

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: 94.29  E-value: 1.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd07848   3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDS--EENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT-TT 320
Cdd:cd07848  81 YVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANyTE 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07848 161 YVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLF 201
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
168-361 1.83e-21

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: 93.66  E-value: 1.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKldGKFYAVKvlqkkIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14058   1 VGRGSFGVVCKARWR--NQIVAVK-----IIESESEKKAFEVEVR-QLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEH---RARFYAAEIASALGYLHSIK---IVYRDLKPENILLDSVGHVV-LTDFGLCKEgiaISDTTTT 320
Cdd:cd14058  73 LYNVLHGKEPKPIYtaaHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVLkICDFGTACD---ISTHMTN 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75813626 321 FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14058 150 NKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
168-419 2.14e-21

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: 93.98  E-value: 2.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVlNRKEQKHI--MAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd07847   9 IGEGSYGVVFKCRNRETGQIVAIK----KFV-ESEDDPVIkkIALREIrMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd07847  84 HTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDDYTDYVAT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVI-RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCR-DVAEMY-------------------DNILH-------- 375
Cdd:cd07847 164 RWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKsDVDQLYlirktlgdliprhqqifstNQFFKglsipepe 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 376 --KPLSLR-PGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd07847 244 trEPLESKfPNISSPALSFLKGCLQMDPTERLSCE----ELLEHPYF 286
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
163-361 3.43e-21

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: 93.22  E-value: 3.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 163 DFLKVIGKGSFGKVLLAKRKldGKFYAVKVLQKKiVLNRKEQKHIMAERNVLlkNVKHPFLVGLHYSFQTTEKLYF---V 239
Cdd:cd13979   6 RLQEPLGSGGFGSVYKATYK--GETVAVKIVRRR-RKNRASRQSFWAELNAA--RLRHENIVRVLAAETGTDFASLgliI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFfHLQRERSFP---EHRARfYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG---LCKEGIA 313
Cdd:cd13979  81 MEYCGNGTLQ-QLIYEGSEPlplAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcsvKLGEGNE 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 314 ISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd13979 159 VGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPY 206
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
166-419 3.45e-21

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: 93.11  E-value: 3.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLaKRKLDGKFYAVKVLQKkivlnrkeQKHIMAERNV--LLKNVKHPFLVGLHYSFQTTEKLYFVL--- 240
Cdd:cd13982   7 KVLGYGSEGTIVF-RGTFDGRPVAVKRLLP--------EFFDFADREVqlLRESDEHPNVIRYFCTEKDRQFLYIALelc 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 -----DFVNGGELFFHLqrERSFPEHRARFYaaEIASALGYLHSIKIVYRDLKPENILLD---SVGHV--VLTDFGLCKE 310
Cdd:cd13982  78 aaslqDLVESPRESKLF--LRPGLEPVRLLR--QIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVraMISDFGLCKK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 311 giaISDTTTTF------CGTPEYLAPEVIRKQPYDNT---VDWWCLGAVLYEML-YGLPPF---YCRDVaemydNILHKP 377
Cdd:cd13982 154 ---LDVGRSSFsrrsgvAGTSGWIAPEMLSGSTKRRQtraVDIFSLGCVFYYVLsGGSHPFgdkLEREA-----NILKGK 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 378 LSLRPGVSLT-----AWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd13982 226 YSLDKLLSLGehgpeAQDLIERMIDFDPEKRPSAE----EVLNHPFF 268
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
161-363 4.28e-21

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: 92.80  E-value: 4.28e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDgkfYAVKVLQkkivLNRKEQKHIMAERNVLL--KNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHRGRWHGD---VAIKLLN----IDYLNEEQLEAFKEEVAayKNTRHDNLVLFMGACMDPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHL-QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVVLTDFGLCK-EGIAISD 316
Cdd:cd14063  74 VTSLCKGRTLYSLIhERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSlSGLLQPG 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 317 TTTTFCGTPE----YLAPEVIRK----------QPYDNTVDWWCLGAVLYEMLYGLPPFYC 363
Cdd:cd14063 153 RREDTLVIPNgwlcYLAPEIIRAlspdldfeesLPFTKASDVYAFGTVWYELLAGRWPFKE 213
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
168-361 4.35e-21

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: 93.44  E-value: 4.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLqkKIVLNRKEQKHIMAERNVLlKNVKHPFLVGL-----HYSFQTTEKLYFVLDF 242
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSC--RLELSVKNKDRWCHEIQIM-KKLNHPNVVKAcdvpeEMNFLVNDVPLLAMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERS---FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG----HVVLtDFGLCKEgIAIS 315
Cdd:cd14039  78 CSGGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkivHKII-DLGYAKD-LDQG 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14039 156 SLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
167-361 4.52e-21

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: 92.79  E-value: 4.52e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKldGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14146   1 IIGVGGFGKVYRATWK--GQEVAVKAARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHL---------QRERSFPEHRARFYAAEIASALGYLHS---IKIVYRDLKPENILL------DSVGHVVL--TDFG 306
Cdd:cd14146  79 TLNRALaaanaapgpRRARRIPPHILVNWAVQIARGMLYLHEeavVPILHRDLKSSNILLlekiehDDICNKTLkiTDFG 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 307 LCKEGIAISDTTTTfcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14146 159 LAREWHRTTKMSAA--GTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
162-422 5.40e-21

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: 93.74  E-value: 5.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKkIVLNRKEQKHIMAERnVLLKNVKHPFLVGLH---YSFQTTE--KL 236
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISN-VFDDLIDAKRILREI-KILRHLKHENIIGLLdilRPPSPEEfnDV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVnggELFFH--LQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAI 314
Cdd:cd07834  80 YIVTELM---ETDLHkvIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 SDTT--TTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILH---KP----------- 377
Cdd:cd07834 157 EDKGflTEYVVTRWYRAPELLLSSKkYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEvlgTPseedlkfisse 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 378 --------LSLRPGVSLT---------AWSILEELLEKDRQNRLGAKEDfLEiqnHPFFESL 422
Cdd:cd07834 237 karnylksLPKKPKKPLSevfpgaspeAIDLLEKMLVFNPKKRITADEA-LA---HPYLAQL 294
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
168-361 5.61e-21

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: 92.74  E-value: 5.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLN-RKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVALK----KIRLEtEDEGVPSTAIREIsLLKELNHPNIVRLLDVVHSENKLYLVFEFLDL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 gELFFHLQ--RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GIAISdTTTTFC 322
Cdd:cd07835  83 -DLKKYMDssPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAfGVPVR-TYTHEV 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07835 161 VTLWYRAPEILLGSKHYSTpVDIWSVGCIFAEMVTRRPLF 200
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
161-355 1.01e-20

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: 92.19  E-value: 1.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHiMAERNVLlKNVKHPFLVGLHYSFqtTEKLYFVL 240
Cdd:cd14049   7 EFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKV-LREVKVL-AGLQHPNIVGYHTAW--MEHVQLML 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 ------------DFVNGGELFFHLQRERSFPEHRARFYAA-----EIASALGYLHSIKIVYRDLKPENILLD-SVGHVVL 302
Cdd:cd14049  83 yiqmqlcelslwDWIVERNKRPCEEEFKSAPYTPVDVDVTtkilqQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRI 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 303 TDFGL-CKEGIAISD-----------TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd14049 163 GDFGLaCPDILQDGNdsttmsrlnglTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
161-426 1.02e-20

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: 92.22  E-value: 1.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlQKKIVLNRKEQKHIMAERNVLLKNVKhPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd06622   2 EIEVLDELGKGNYGSVYKVLHRPTGVTMAMK--EIRLELDESKFNQIIMELDILHKAVS-PYIVDFYGAFFIEGAVYMCM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGG---ELFFHLQRERSFPEHRARFYAAEIASALGYL-HSIKIVYRDLKPENILLDSVGHVVLTDFGLckEGIAISD 316
Cdd:cd06622  79 EYMDAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGV--SGNLVAS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQ-PYDN---TV--DWWCLGAVLYEMLYGLPPFycrdVAEMYDNILHK--------PLSLRP 382
Cdd:cd06622 157 LAKTNIGCQSYMAPERIKSGgPNQNptyTVqsDVWSLGLSILEMALGRYPY----PPETYANIFAQlsaivdgdPPTLPS 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 75813626 383 GVSLTAWSILEELLEKDRQNRlgakEDFLEIQNHPFFESLSWAD 426
Cdd:cd06622 233 GYSDDAQDFVAKCLNKIPNRR----PTYAQLLEHPWLVKYKNAD 272
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
165-422 1.08e-20

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: 92.37  E-value: 1.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd07873   7 LDKLGEGTYATVYKGRSKLTDNLVALK----EIRLEHEEGAPCTAIREVsLLKDLKHANIVTLHDIIHTEKSLTLVFEYL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCG 323
Cdd:cd07873  83 DKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 324 TPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEM---------------------------YDNILH 375
Cdd:cd07873 163 TLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQlhfifrilgtpteetwpgilsneefksYNYPKY 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 376 KPLSLR---PGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFFESL 422
Cdd:cd07873 243 RADALHnhaPRLDSDGADLLSKLLQFEGRKRISAE----EAMKHPYFHSL 288
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
168-355 1.30e-20

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 91.54  E-value: 1.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKfyaVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGK---VMVMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK-----EGIAISDTTT--- 319
Cdd:cd14222  77 LKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRliveeKKKPPPDKPTtkk 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 320 ------------TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd14222 157 rtlrkndrkkryTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
162-334 1.47e-20

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: 90.83  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14050   3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRF-RGEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVnGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDTTTTF 321
Cdd:cd14050  82 LC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE-LDKEDIHDAQ 159
                       170
                ....*....|...
gi 75813626 322 CGTPEYLAPEVIR 334
Cdd:cd14050 160 EGDPRYMAPELLQ 172
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
157-361 1.47e-20

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: 92.06  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 157 AKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEK 235
Cdd:cd07869   2 GKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIR----LQEEEGTPFTAIREAsLLKGLKHANIVLLHDIIHTKET 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAIS 315
Cdd:cd07869  78 LTLVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPS 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 316 DTTTTFCGTPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07869 158 HTYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAF 204
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
168-359 1.55e-20

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: 91.01  E-value: 1.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKfyavkVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGK-----VMVMKELKRFDEQRSFLKEVK-LMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFY-AAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLCKEgiaISDTTT---- 319
Cdd:cd14065  75 LEELLKSMDEQLPWSQRVSlAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLARE---MPDEKTkkpd 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75813626 320 -----TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLP 359
Cdd:cd14065 152 rkkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIGRVP 196
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
162-362 1.70e-20

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 91.86  E-value: 1.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLN-RKEQK---HIMAERNV-LLKNVKHPFLVGLHYSFQTTEKL 236
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIK----KIKLGeRKEAKdgiNFTALREIkLLQELKHPNIIGLLDVFGHKSNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVnGGELffhlqrERSFPEHRARFYAAEIAS-------ALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd07841  78 NLVFEFM-ETDL------EKVIKDKSIVLTPADIKSymlmtlrGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 310 EGIAISDTTTTFCGTPEYLAPEVI---RKqpYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd07841 151 SFGSPNRKMTHQVVTRWYRAPELLfgaRH--YGVGVDMWSVGCIFAELLLRVPFLP 204
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
162-365 2.49e-20

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: 91.45  E-value: 2.49e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnRKEQKHIMAERNvLLKNVKH------PFLVGLHYSFQ---- 231
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNK----KRFHQQALVEVK-ILKHLNDndpddkHNIVRYKDSFIfrgh 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 232 ---TTEKLyfvldfvnGGELFFHLQRE--RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH--VVLTD 304
Cdd:cd14210  90 lciVFELL--------SINLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVID 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 305 FGL-CKEGiaisDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD 365
Cdd:cd14210 162 FGSsCFEG----EKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGEN 219
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
215-418 2.72e-20

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: 90.11  E-value: 2.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 215 LKNVKHPFLVGLhYSFQTTE-------KLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDL 287
Cdd:cd14012  52 LKKLRHPNLVSY-LAFSIERrgrsdgwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 288 KPENILLDSVGH---VVLTDFGLCKE--GIAISDTTTTFCGTPeYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLppf 361
Cdd:cd14012 131 HAGNVLLDRDAGtgiVKLTDYSLGKTllDMCSRGSLDEFKQTY-WLPPELAQgSKSPTRKTDVWDLGLLFLQMLFGL--- 206
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 362 ycrDVAEMYD--NILHKPLSLrpgvSLTAWSILEELLEKDRQNRLGAkedfLEIQNHPF 418
Cdd:cd14012 207 ---DVLEKYTspNPVLVSLDL----SASLQDFLSKCLSLDPKKRPTA----LELLPHEF 254
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
158-388 4.35e-20

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: 90.88  E-value: 4.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhIMAERNVLlKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd06650   3 KDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQ--IIRELQVL-HECNSPYIVGFYGAFYSDGEIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSI-KIVYRDLKPENILLDSVGHVVLTDFGLckEGIAISD 316
Cdd:cd06650  80 ICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGV--SGQLIDS 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMyDNILHKPLSLRPGVSLTA 388
Cdd:cd06650 158 MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKEL-ELMFGCQVEGDAAETPPR 228
PX smart00312
PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function ...
23-118 4.63e-20

PhoX homologous domain, present in p47phox and p40phox; Eukaryotic domain of unknown function present in phox proteins, PLD isoforms, a PI3K isoform.


Pssm-ID: 214610  Cd Length: 105  Bit Score: 85.09  E-value: 4.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626     23 EHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMAL-KIPAKRIFG--DNFDPDFIKQRRAGLNEFIQ 99
Cdd:smart00312   6 KIGDGKHYYYVIEIETKTGLEEWTVSRRYSDFLELHSKLKKHFPRSILpPLPGKKLFGrlNNFSEEFIEKRRRGLEKYLQ 85
                           90       100
                   ....*....|....*....|
gi 75813626    100 NLVRYPELYNH-PDVRAFLQ 118
Cdd:smart00312  86 SLLNHPELINHsEVVLEFLE 105
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
168-355 1.17e-19

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 88.72  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKfyaVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFL---VGLHYSfqtTEKLYFVLDFVN 244
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGE---VMVMKELIRFDEEAQRNFLKEVKVM-RSLDHPNVlkfIGVLYK---DKKLNLITEYIP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGEL--FFHlQRERSFP-EHRARFyAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC-------KEGIAI 314
Cdd:cd14154  74 GGTLkdVLK-DMARPLPwAQRVRF-AKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerLPSGNM 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75813626 315 SDTTT-------------TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd14154 152 SPSETlrhlkspdrkkryTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
165-365 1.17e-19

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: 89.94  E-value: 1.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKI---VLNRKEQKHIMaernvLLKNVKHPFLVGLHYSF-QTTEKLYFVL 240
Cdd:cd07856  15 LQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFstpVLAKRTYRELK-----LLKHLRHENIISLSDIFiSPLEDIYFVT 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVngGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiaISDTTTT 320
Cdd:cd07856  90 ELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR----IQDPQMT 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 321 -FCGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFYCRD 365
Cdd:cd07856 164 gYVSTRYYRAPEIMLTwQKYDVEVDIWSAGCIFAEMLEGKPLFPGKD 210
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
168-361 1.18e-19

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: 88.96  E-value: 1.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVglhysfqtteKLYFVLdFVNGG- 246
Cdd:cd06616  14 IGRGAFGTVNKMLHKPSGTIMAVK--RIRSTVDEKEQKRLLMDLDVVMRSSDCPYIV----------KFYGAL-FREGDc 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ----EL----------FFHLQRERSFPEHRARFYAAEIASALGYL-HSIKIVYRDLKPENILLDSVGHVVLTDFGLC--- 308
Cdd:cd06616  81 wicmELmdisldkfykYVYEVLDSVIPEEILGKIAVATVKALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISgql 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 309 KEGIAisdtTTTFCGTPEYLAPEVI----RKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd06616 161 VDSIA----KTRDAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPY 213
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
163-362 1.34e-19

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 89.02  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 163 DFLKV--IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVL-NRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd07861   1 DYTKIekIGEGTYGVVYKGRNKKTGQIVAMK----KIRLeSEEEGVPSTAIREIsLLKELQHPNIVCLEDVLMQENRLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFvnggeLFFHLQR-------ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE- 310
Cdd:cd07861  77 VFEF-----LSMDLKKyldslpkGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAf 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75813626 311 GIAISDTTTTFCgTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd07861 152 GIPVRVYTHEVV-TLWYRAPEVLLGSPrYSTPVDIWSIGTIFAEMATKKPLFH 203
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
162-361 1.47e-19

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: 88.78  E-value: 1.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVL-NRKEQKHIMAERNV-LLKNVKHPFLVGLH------YSFQTT 233
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKTGELVALK----KIRMeNEKEGFPITAIREIkLLQKLDHPNVVRLKeivtskGSAKYK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFV----NGgelfFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd07840  77 GSIYMVFEYMdhdlTG----LLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75813626 310 egiaisdtTTTFCGTPE---------YLAPEVI--RKQpYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07840 153 --------PYTKENNADytnrvitlwYRPPELLlgATR-YGPEVDMWSVGCILAELFTGKPIF 206
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
168-408 1.73e-19

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 88.34  E-value: 1.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLnrkeqKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVK----KVRL-----EVFRAEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG-HVVLTDFGL--CKEGIAISDTTTT---F 321
Cdd:cd13991  85 LGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHaeCLDPDGLGKSLFTgdyI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR---PGVSLTAWSILEELLEK 398
Cdd:cd13991 165 PGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPLReipPSCAPLTAQAIQAGLRK 244
                       250
                ....*....|
gi 75813626 399 DRQNRLGAKE 408
Cdd:cd13991 245 EPVHRASAAE 254
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
168-359 1.75e-19

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: 87.96  E-value: 1.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvlnrkeQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDV------DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLCKEGIAI----SDTTT 319
Cdd:cd14156  75 LEELLAREELPLSWREKVeLACDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGREAVVTDFGLAREVGEMpandPERKL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLP 359
Cdd:cd14156 155 SLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIP 194
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
162-419 2.18e-19

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 88.31  E-value: 2.18e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVlqkkIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKE----IHLDAEEGTPSTAIREIsLMKELKHENIVRLHDVIHTENKLMLVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGgelffHLQR-------ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GI 312
Cdd:cd07836  78 EYMDK-----DLKKymdthgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAfGI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISdtttTFCG---TPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL-------------- 374
Cdd:cd07836 153 PVN----TFSNevvTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFrimgtptestwpgi 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 375 ------------HKPLSLR---PGVSLTAWSILEELLEKDRQNRLGAKEDFleiqNHPFF 419
Cdd:cd07836 229 sqlpeykptfprYPPQDLQqlfPHADPLGIDLLHRLLQLNPELRISAHDAL----QHPWF 284
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
165-365 2.33e-19

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: 87.76  E-value: 2.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDgkfYAVKVLqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVgLHYSFQTTEKLYFVLDFVN 244
Cdd:cd14150   5 LKRIGTGSFGTVFRGKWHGD---VAVKIL--KVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC--KEGIAISDTTTTF 321
Cdd:cd14150  79 GSSLYRHLHvTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQQVEQP 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVIRKQ---PYDNTVDWWCLGAVLYEMLYGLPPFY---CRD 365
Cdd:cd14150 159 SGSILWMAPEVIRMQdtnPYSFQSDVYAYGVVLYELMSGTLPYSninNRD 208
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
124-361 2.39e-19

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 90.48  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  124 HQSDPSEDEDERSSqklhsTSQNINLGPSgnphakpTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVK-VLQKKIVLNRK 202
Cdd:PTZ00036  42 HNNNAGEDEDEEKM-----IDNDINRSPN-------KSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKkVLQDPQYKNRE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  203 eqkhIMAERNvlLKNVKHPFLVGLHY--SFQTTEKLYF---VLDFVNG---GELFFHLQRERSFPEHRARFYAAEIASAL 274
Cdd:PTZ00036 110 ----LLIMKN--LNHINIIFLKDYYYteCFKKNEKNIFlnvVMEFIPQtvhKYMKHYARNNHALPLFLVKLYSYQLCRAL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  275 GYLHSIKIVYRDLKPENILLDSVGHVV-LTDFGLCKEGIAISDTTTTFCgTPEYLAPEV-IRKQPYDNTVDWWCLGAVLY 352
Cdd:PTZ00036 184 AYIHSKFICHRDLKPQNLLIDPNTHTLkLCDFGSAKNLLAGQRSVSYIC-SRFYRAPELmLGATNYTTHIDLWSLGCIIA 262

                 ....*....
gi 75813626  353 EMLYGLPPF 361
Cdd:PTZ00036 263 EMILGYPIF 271
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
162-418 2.96e-19

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: 87.12  E-value: 2.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQ----KHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd06607   3 FEDLREIGHGSFGAVYYARNKRTSEVVAIK----KMSYSGKQStekwQDIIKEVK-FLRQLRHPNTIEYKGCYLREHTAW 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGG-----ELffhlqrersfpeHRARFYAAEIAS-------ALGYLHSIKIVYRDLKPENILLDSVGHVVLTDF 305
Cdd:cd06607  78 LVMEYCLGSasdivEV------------HKKPLQEVEIAAichgalqGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 306 GlckeGIAISDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPP-FYCRDVAEMYDNILHKPLSLR 381
Cdd:cd06607 146 G----SASLVCPANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPlFNMNAMSALYHIAQNDSPTLS 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75813626 382 PGvsltAWS-----ILEELLEKDRQNRLGAkEDFLEiqnHPF 418
Cdd:cd06607 222 SG----EWSddfrnFVDSCLQKIPQDRPSA-EDLLK---HPF 255
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
166-419 3.61e-19

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: 86.80  E-value: 3.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHimaerNVLlknvKHPFLVGLHYSFQTTEKLYFVLDFVN- 244
Cdd:cd14109  10 EDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPFLMREVDIH-----NSL----DHPNIVQMHDAYDDEKLAVTVIDNLAs 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFH--LQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLdSVGHVVLTDFGLCKEgIAISDTTTTFC 322
Cdd:cd14109  81 TIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILL-QDDKLKLADFGQSRR-LLRGKLTTLIY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGV----SLTAWSILEELLEK 398
Cdd:cd14109 159 GSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPlgniSDDARDFIKKLLVY 238
                       250       260
                ....*....|....*....|.
gi 75813626 399 DRQNRLGAKEDFleiqNHPFF 419
Cdd:cd14109 239 IPESRLTVDEAL----NHPWF 255
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
160-360 4.29e-19

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: 87.88  E-value: 4.29e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAIRNQ--IIRELKVLHE-CNSPYIVGFYGAFYSDGEISIC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQRERSFPEHrarfYAAEIASA----LGYLHS-IKIVYRDLKPENILLDSVGHVVLTDFGLckEGIAI 314
Cdd:cd06615  78 MEHMDGGSLDQVLKKAGRIPEN----ILGKISIAvlrgLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGV--SGQLI 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 315 SDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPP 360
Cdd:cd06615 152 DSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYP 197
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
162-408 5.42e-19

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: 86.51  E-value: 5.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnrKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14110   5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYK-----PEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG----LCKEGIAISDT 317
Cdd:cd14110  80 LCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGnaqpFNQGKVLMTDK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCgtpEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCrDVAEMYDNILHKPL----SLRPGVSLTAWSILE 393
Cdd:cd14110 160 KGDYV---ETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSS-DLNWERDRNIRKGKvqlsRCYAGLSGGAVNFLK 235
                       250
                ....*....|....*
gi 75813626 394 ELLEKDRQNRLGAKE 408
Cdd:cd14110 236 STLCAKPWGRPTASE 250
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
162-355 6.23e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 88.01  E-value: 6.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLnrkeqkhIMAernVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQKGTTL-------IEA---MLLQNVNHPSVIRMKDTLVSGAITCMVLP 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  242 FVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDtTTTF 321
Cdd:PHA03209 138 HYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPA-FLGL 216
                        170       180       190
                 ....*....|....*....|....*....|....
gi 75813626  322 CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:PHA03209 217 AGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
158-361 7.95e-19

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: 85.87  E-value: 7.95e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKldGKFYAVKVLqkKIVLNRKEQkhIMAERNVLLKnVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd05039   4 NKKDLKLGELIGKGEFGDVMLGDYR--GQKVAVKCL--KDDSTAAQA--FLAEASVMTT-LRHPNLVQLLGVVLEGNGLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQ-RERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgiaiS 315
Cdd:cd05039  77 IVTEYMAKGSLVDYLRsRGRAVITRKDQLgFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKE----A 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 316 DTTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05039 153 SSNQDGGKLPiKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPY 200
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
165-434 8.74e-19

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: 87.01  E-value: 8.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd06633  26 LHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVK-FLQQLKHPNTIEYKGCYLKDHTAWLVMEYCL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGElffhlqrERSFPEHRARFYAAEIAS-------ALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGlckeGIAISDT 317
Cdd:cd06633 105 GSA-------SDLLEVHKKPLQEVEIAAithgalqGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG----SASIASP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPP-FYCRDVAEMYdnilHKPLSLRPGVSLTAWS--- 390
Cdd:cd06633 174 ANSFVGTPYWMAPEVIlamDEGQYDGKVDIWSLGITCIELAERKPPlFNMNAMSALY----HIAQNDSPTLQSNEWTdsf 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 391 --ILEELLEKDRQNRLGAkedfLEIQNHpffeslswaDLVQKKIPP 434
Cdd:cd06633 250 rgFVDYCLQKIPQERPSS----AELLRH---------DFVRRERPP 282
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
168-355 9.37e-19

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: 86.16  E-value: 9.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKfyaVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGE---VMVMKELIRFDEETQRTFLKEVKVM-RCLEHPNVLKFIGVLYKDKRLNFITEYIKGGT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAISDTTT------- 319
Cdd:cd14221  77 LRGIIKSMDShYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLAR--LMVDEKTQpeglrsl 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75813626 320 ---------TFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd14221 155 kkpdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
167-361 1.09e-18

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: 85.81  E-value: 1.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLlakrklDGKFYAVKVLQKKIVLNRKEQKHIMAErNV-----LLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14148   1 IIGVGGFGKVY------KGLWRGEEVAVKAARQDPDEDIAVTAE-NVrqearLFWMLQHPNIIALRGVCLNPPHLCLVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERsFPEHRARFYAAEIASALGYLHS---IKIVYRDLKPENILL------DSVGHVVL--TDFGLCKE 310
Cdd:cd14148  74 YARGGALNRALAGKK-VPPHVLVNWAVQIARGMNYLHNeaiVPIIHRDLKSSNILIlepienDDLSGKTLkiTDFGLARE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 311 GIaiSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14148 153 WH--KTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
165-361 1.24e-18

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: 86.58  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd07872  11 LEKLGEGTYATVFKGRSKLTENLVALK----EIRLEHEEGAPCTAIREVsLLKDLKHANIVTLHDIVHTDKSLTLVFEYL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCG 323
Cdd:cd07872  87 DKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSNEVV 166
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 324 TPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07872 167 TLWYRPPDVLLgSSEYSTQIDMWGVGCIFFEMASGRPLF 205
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
162-434 1.35e-18

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: 86.65  E-value: 1.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKfyavKVLQKKIVlnRKEQKHIMAERNV----LLKNVKHPFLVGLHYSFQTTEKL- 236
Cdd:cd07855   7 YEPIETIGSGAYGVVCSAIDTKSGQ----KVAIKKIP--NAFDVVTTAKRTLrelkILRHFKHDNIIAIRDILRPKVPYa 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 -----YFVLDFVNGgELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG----L 307
Cdd:cd07855  81 dfkdvYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGmargL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 308 CKEGIAISDTTTTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEML---------------------YGLPP----- 360
Cdd:cd07855 160 CTSPEEHKYFMTEYVATRWYRAPELMLSLPeYTQAIDMWSVGCIFAEMLgrrqlfpgknyvhqlqliltvLGTPSqavin 239
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 361 -FYCRDVAEMYDNILHKPL----SLRPGVSLTAWSILEELLEKDRQNRLGAKEDFLeiqnHPFFESLSWADLVQKKIPP 434
Cdd:cd07855 240 aIGADRVRRYIQNLPNKQPvpweTLYPKADQQALDLLSQMLRFDPSERITVAEALQ----HPFLAKYHDPDDEPDCAPP 314
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
167-385 1.79e-18

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: 84.90  E-value: 1.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERN--VLLKNV----KHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14101   7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLPGVNPVPNevALLQSVgggpGHRGVIRLLDWFEIPEGFLLVL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DF-VNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS-VGHVVLTDFGlckEGIAISDTT 318
Cdd:cd14101  87 ERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLrTGDIKLIDFG---SGATLKDSM 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 319 -TTFCGTPEYLAPEVIRKQPYDN---TVdwWCLGAVLYEMLYGLPPFycrdvaEMYDNILHKPLSLRPGVS 385
Cdd:cd14101 164 yTDFDGTRVYSPPEWILYHQYHAlpaTV--WSLGILLYDMVCGDIPF------ERDTDILKAKPSFNKRVS 226
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
167-406 1.93e-18

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: 85.57  E-value: 1.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLlaKRKLDGKFYAVKVLQKKIVLNRKEQKHIMaeRNVLLK--NVKHpFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd13998   2 VIGKGRFGEVW--KASLKNEPVAVKIFSSRDKQSWFREKEIY--RTPMLKheNILQ-FIAADERDTALRTELWLVTAFHP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPEHRARFyAAEIASALGYLHS---------IKIVYRDLKPENILLDSVGHVVLTDFGLC---KEGI 312
Cdd:cd13998  77 NGSL*DYLSLHTIDWVSLCRL-ALSVARGLAHLHSeipgctqgkPAIAHRDLKSKNILVKNDGTCCIADFGLAvrlSPST 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDTTTTF-CGTPEYLAPEV----IRKQPYDN--TVDWWCLGAVLYEM------LYGL-----PPFYCR-----DVAEM 369
Cdd:cd13998 156 GEEDNANNGqVGTKRYMAPEVlegaINLRDFESfkRVDIYAMGLVLWEMasrctdLFGIveeykPPFYSEvpnhpSFEDM 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 370 YDNILHKplSLRPGVSlTAW----------SILEELLEKDRQNRLGA 406
Cdd:cd13998 236 QEVVVRD--KQRPNIP-NRWlshpglqslaETIEECWDHDAEARLTA 279
PX pfam00787
PX domain; PX domains bind to phosphoinositides.
41-118 2.09e-18

PX domain; PX domains bind to phosphoinositides.


Pssm-ID: 459940  Cd Length: 84  Bit Score: 79.59  E-value: 2.09e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626    41 GRSEWFVFRRYAEFDKLYNTLKKQFPA-MALKIPAKRIFGdNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQ 118
Cdd:pfam00787   5 SLEEWSVRRRYSDFVELHKKLLRKFPSvIIPPLPPKRWLG-RYNEEFIEKRRKGLEQYLQRLLQHPELRNSEVLLEFLE 82
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
159-374 2.10e-18

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: 86.26  E-value: 2.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAkrkldgkfYAVKVLQKKIV--LNRKEQKHIMAERNV----LLKNVKHPFLVGL------ 226
Cdd:cd07878  14 PERYQNLTPVGSGAYGSVCSA--------YDTRLRQKVAVkkLSRPFQSLIHARRTYrelrLLKHMKHENVIGLldvftp 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 227 HYSFQTTEKLYFVLDFVnGGELFFHLQRERSFPEHrARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd07878  86 ATSIENFNEVYLVTNLM-GADLNNIVKCQKLSDEH-VQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFG 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 307 LCKEGiaiSDTTTTFCGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL 374
Cdd:cd07878 164 LARQA---DDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIM 229
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
166-361 2.11e-18

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: 85.08  E-value: 2.11e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKldGKFYAVKVLQKkivlNRKEQKHIMAErNV-----LLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd14147   9 EVIGIGGFGKVYRGSWR--GELVAVKAARQ----DPDEDISVTAE-SVrqearLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERsFPEHRARFYAAEIASALGYLHS---IKIVYRDLKPENILL------DSVGHVVL--TDFGLCK 309
Cdd:cd14147  82 EYAAGGPLSRALAGRR-VPPHVLVNWAVQIARGMHYLHCealVPVIHRDLKSNNILLlqpienDDMEHKTLkiTDFGLAR 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 310 EGIAISDTTTTfcGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14147 161 EWHKTTQMSAA--GTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
167-418 2.90e-18

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: 84.25  E-value: 2.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKH--IMAERNVLLKNVKHPF--LVGLHYSFQTTEKLYFVLDF 242
Cdd:cd14100   7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPNgtRVPMEIVLLKKVGSGFrgVIRLLDWFERPDSFVLVLER 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD-SVGHVVLTDFGlckEGIAISDTT-T 319
Cdd:cd14100  87 PEPVQDLFDFITERgALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFG---SGALLKDTVyT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQPYDN-TVDWWCLGAVLYEMLYGLPPFycrdvaEMYDNILHKPLSLRPGVS-----LTAWSIle 393
Cdd:cd14100 164 DFDGTRVYSPPEWIRFHRYHGrSAAVWSLGILLYDMVCGDIPF------EHDEEIIRGQVFFRQRVSsecqhLIKWCL-- 235
                       250       260
                ....*....|....*....|....*
gi 75813626 394 ELLEKDRQNrlgakedFLEIQNHPF 418
Cdd:cd14100 236 ALRPSDRPS-------FEDIQNHPW 253
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
166-361 3.25e-18

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: 84.71  E-value: 3.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKrkLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd14145  12 EIIGIGGFGKVYRAI--WIGDEVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERsFPEHRARFYAAEIASALGYLHS---IKIVYRDLKPENILL------DSVGHVVL--TDFGLCKEGIai 314
Cdd:cd14145  90 GPLNRVLSGKR-IPPDILVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILIlekvenGDLSNKILkiTDFGLAREWH-- 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 315 SDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14145 167 RTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
158-378 3.35e-18

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: 85.49  E-value: 3.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhIMAERNVLlKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd06649   3 KDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQ--IIRELQVL-HECNSPYIVGFYGAFYSDGEIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSI-KIVYRDLKPENILLDSVGHVVLTDFGLckEGIAISD 316
Cdd:cd06649  80 ICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGV--SGQLIDS 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMyDNILHKPL 378
Cdd:cd06649 158 MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKEL-EAIFGRPV 218
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
160-361 3.60e-18

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: 84.18  E-value: 3.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDF-DFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkkIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd14108   1 TDYyDIHKEIGRGAFSYLRRVKEKSSDLSFAAK-----FIPVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVII 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGgELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL--DSVGHVVLTDFGLCKEgiaISD 316
Cdd:cd14108  76 VTELCHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQE---LTP 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 317 TTTTFC--GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14108 152 NEPQYCkyGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPF 198
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
159-386 3.67e-18

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: 85.86  E-value: 3.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAkrkLDGKfYAVKVLQKKivLNRKEQKHIMAERNV----LLKNVKHPFLVGL------HY 228
Cdd:cd07877  16 PERYQNLSPVGSGAYGSVCAA---FDTK-TGLRVAVKK--LSRPFQSIIHAKRTYrelrLLKHMKHENVIGLldvftpAR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 229 SFQTTEKLYFVLDFVnGGELFFHLQRERSFPEHrARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd07877  90 SLEEFNDVYLVTHLM-GADLNNIVKCQKLTDDH-VQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 309 KEgiaISDTTTTFCGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHkpLSLRPGVSL 386
Cdd:cd07877 168 RH---TDDEMTGYVATRWYRAPEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILR--LVGTPGAEL 241
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
168-365 8.70e-18

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: 83.47  E-value: 8.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQkkiVLNRKEQKHIMAERNV-LLKNVK---HPFLVGLHYSFQTTE-----KLYF 238
Cdd:cd07863   8 IGVGAYGTVYKARDPHSGHFVALKSVR---VQTNEDGLPLSTVREVaLLKRLEafdHPNIVRLMDVCATSRtdretKVTL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGgELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK---EGIA 313
Cdd:cd07863  85 VFEHVDQ-DLRTYLDKvpPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARiysCQMA 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 314 ISDTTTTFCgtpeYLAPEVIRKQPYDNTVDWWCLGAVLYEMlYGLPPFYCRD 365
Cdd:cd07863 164 LTPVVVTLW----YRAPEVLLQSTYATPVDMWSVGCIFAEM-FRRKPLFCGN 210
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
167-382 1.02e-17

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 82.70  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERN-VLLKNVKHPF--LVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd14102   7 VLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEiVLLKKVGSGFrgVIKLLDWYERPDGFLIVMERP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 N-GGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD-SVGHVVLTDFGlckEGIAISDTT-TT 320
Cdd:cd14102  87 EpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFG---SGALLKDTVyTD 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 321 FCGTPEYLAPEVIRKQPYD-NTVDWWCLGAVLYEMLYGLPPF------------YCRDVAEMYDNILHKPLSLRP 382
Cdd:cd14102 164 FDGTRVYSPPEWIRYHRYHgRSATVWSLGVLLYDMVCGDIPFeqdeeilrgrlyFRRRVSPECQQLIKWCLSLRP 238
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
162-408 1.23e-17

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 83.56  E-value: 1.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06635  27 FSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVK-FLQRIKHPNSIEYKGCYLREHTAWLVME 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGElffhlqrERSFPEHRARFYAAEIAS-------ALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGlckeGIAI 314
Cdd:cd06635 106 YCLGSA-------SDLLEVHKKPLQEIEIAAithgalqGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG----SASI 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 315 SDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMydnILHKPLSLRPGVSLTAWS- 390
Cdd:cd06635 175 ASPANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSA---LYHIAQNESPTLQSNEWSd 251
                       250       260
                ....*....|....*....|..
gi 75813626 391 ----ILEELLEKDRQNRLGAKE 408
Cdd:cd06635 252 yfrnFVDSCLQKIPQDRPTSEE 273
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
167-357 1.24e-17

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: 82.31  E-value: 1.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKldGKFYAVKVLqkkivlNRKEQKHIMAERNVLLKNVKHPFLVGLHYSfqTTEKLYFVLDFVNGG 246
Cdd:cd14068   1 LLGDGGFGSVYRAVYR--GEDVAVKIF------NKHTSFRLLRQELVVLSHLHHPSLVALLAA--GTAPRMLVMELAPKG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRE-----RSFpEHRArfyAAEIASALGYLHSIKIVYRDLKPENILL-----DSVGHVVLTDFGL----CKEGI 312
Cdd:cd14068  71 SLDALLQQDnasltRTL-QHRI---ALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIaqycCRMGI 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 313 AISdttttfCGTPEYLAPEVIRKQ-PYDNTVDWWCLGAVLYEMLYG 357
Cdd:cd14068 147 KTS------EGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTC 186
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
154-419 1.76e-17

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: 82.46  E-value: 1.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 154 NPHAKPTDFDFlkVIGKGSFGKVLlakRKLDGKFYaVKV----LQKKIVLNRKEQKhiMAERNVLLKNVKHPFLVGLHYS 229
Cdd:cd14031   6 SPGGRFLKFDI--ELGRGAFKTVY---KGLDTETW-VEVawceLQDRKLTKAEQQR--FKEEAEMLKGLQHPNIVRFYDS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 230 FQTTEK----LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILLDS-VGHVVL 302
Cdd:cd14031  78 WESVLKgkkcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 303 TDFGLCKegIAISDTTTTFCGTPEYLAPEVIRKQpYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILH--KPLS 379
Cdd:cd14031 158 GDLGLAT--LMRTSFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSeCQNAAQIYRKVTSgiKPAS 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 75813626 380 LRPGVSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd14031 235 FNKVTDPEVKEIIEGCIRQNKSERLSIK----DLLNHAFF 270
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
168-361 2.02e-17

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: 82.01  E-value: 2.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKL-DGKFY--AVKVL-QKKIVLNRKEqkhIMAERNVLLKnVKHPFLVGLhYSFQTTEKLYFVLDFV 243
Cdd:cd05060   3 LGHGNFGSVRKGVYLMkSGKEVevAVKTLkQEHEKAGKKE---FLREASVMAQ-LDHPCIVRL-IGVCKGEPLMLVMELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISD--TTTTF 321
Cdd:cd05060  78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSDyyRATTA 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 75813626 322 CGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05060 158 GRWPlKWYAPECINYGKFSSKSDVWSYGVTLWEAFsYGAKPY 199
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
168-415 2.27e-17

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: 82.92  E-value: 2.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKhiMAERNVLlKNVKHPFLVGLHYSF--QTTEKLYFVLDFVNG 245
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKVFNNLSFMRPLDVQ--MREFEVL-KKLNHKNIVKLFAIEeeLTTRHKVLVMELCPC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQR-ERSF--PEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL--LDSVGHVV--LTDFGLCKEgIAISDTT 318
Cdd:cd13988  78 GSLYTVLEEpSNAYglPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQSVykLTDFGAARE-LEDDEQF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 319 TTFCGTPEYLAPE-----VIRK---QPYDNTVDWWCLGAVLYEMLYGLPPFYC-----RDVAEMYDNILHKPLSLRPGVS 385
Cdd:cd13988 157 VSLYGTEEYLHPDmyeraVLRKdhqKKYGATVDLWSIGVTFYHAATGSLPFRPfegprRNKEVMYKIITGKPSGAISGVQ 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 75813626 386 LTA-----WS-------------------ILEELLEKDRQNRLGAKEDFLEIQN 415
Cdd:cd13988 237 KSEngpieWSgelpvscslsqglqtlltpVLANILEADQEKCWGFDQFFAETSD 290
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
160-359 2.70e-17

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: 82.75  E-value: 2.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqKKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGL-----HYSFQTT 233
Cdd:cd07866   8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALK---KILMHNEKDGFPITALREIkILKKLKHPNVVPLidmavERPDKSK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKL---YFVLDFVNGgELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC- 308
Cdd:cd07866  85 RKRgsvYMVTPYMDH-DLSGLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLAr 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75813626 309 ---------KEGIAISDTTTTFC-GTPEYLAPEVI---RKqpYDNTVDWWCLGAVLYEMLYGLP 359
Cdd:cd07866 164 pydgpppnpKGGGGGGTRKYTNLvVTRWYRPPELLlgeRR--YTTAVDIWGIGCVFAEMFTRRP 225
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
168-361 6.19e-17

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: 81.23  E-value: 6.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKR-KLDGKFYAVKVLQkkiVLNRKEQKHIMAERNVL----LKNVKHPFLVGLHYSFQTTE-----KLY 237
Cdd:cd07862   9 IGEGAYGKVFKARDlKNGGRFVALKRVR---VQTGEEGMPLSTIREVAvlrhLETFEHPNVVRLFDVCTVSRtdretKLT 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGgELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAIS 315
Cdd:cd07862  86 LVFEHVDQ-DLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARI-YSFQ 163
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 316 DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07862 164 MALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLF 209
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
228-395 6.29e-17

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: 81.30  E-value: 6.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 228 YSFQTTEKLYFVLD-------------FVNggeLFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL 294
Cdd:cd13974  89 YTGRVRKRLCLVLDclcahdfsdktadLIN---LQHYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVL 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 295 DSVGH-VVLTDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQPY-DNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDN 372
Cdd:cd13974 166 NKRTRkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYlGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRK 245
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75813626 373 I--------------------LHKPLSLRPGVSLTAWSILEEL 395
Cdd:cd13974 246 IkaaeytipedgrvsentvclIRKLLVLNPQKRLTASEVLDSL 288
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
161-373 6.33e-17

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: 80.56  E-value: 6.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKlDGKFYAVKVLQKKIVLNRKE-QKHIMAernvlLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd05148   7 EFTLERKLGSGYFGEVWEGLWK-NRVRVAIKILKSDDLLKQQDfQKEVQA-----LKRLRHKHLISLFAVCSVGEPVYII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELFFHLQ--RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC---KEGIAI 314
Cdd:cd05148  81 TELMEKGSLLAFLRspEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliKEDVYL 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 315 SDTTTtfcgTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:cd05148 161 SSDKK----IPyKWTAPEAASHGTFSTKSDVWSFGILLYEMFtYGQVPYPGMNNHEVYDQI 217
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
160-420 8.74e-17

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 80.55  E-value: 8.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYS-FQT------ 232
Cdd:cd06617   1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRI--RATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGAlFREgdvwic 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 TEKLYFVLDfvnggELFFH-LQRERSFPEHRARFYAAEIASALGYLHS-IKIVYRDLKPENILLDSVGHVVLTDFGLckE 310
Cdd:cd06617  79 MEVMDTSLD-----KFYKKvYDKGLTIPEDILGKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFGI--S 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 311 GIAISDTTTTF-CGTPEYLAPEVI----RKQPYDNTVDWWCLGAVLYEMLYGLPPFYC-RDVAEMYDNILHKPLSLRP-- 382
Cdd:cd06617 152 GYLVDSVAKTIdAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIELATGRFPYDSwKTPFQQLKQVVEEPSPQLPae 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 75813626 383 GVSLTAWSILEELLEKDRQNRlgakEDFLEIQNHPFFE 420
Cdd:cd06617 232 KFSPEFQDFVNKCLKKNYKER----PNYPELLQHPFFE 265
pknD PRK13184
serine/threonine-protein kinase PknD;
162-382 1.22e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 83.28  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIA-ADLIHPGIVPVYSICSDGDPVYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  242 FVNGGELFFHL----QRERSFPEHRARFYAA-------EIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK- 309
Cdd:PRK13184  83 YIEGYTLKSLLksvwQKESLSKELAEKTSVGaflsifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIf 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  310 ------EGIAISDTTTTFC-----------GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEM-YD 371
Cdd:PRK13184 163 kkleeeDLLDIDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKIsYR 242
                        250
                 ....*....|.
gi 75813626  372 NILHKPLSLRP 382
Cdd:PRK13184 243 DVILSPIEVAP 253
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
161-419 1.36e-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: 79.19  E-value: 1.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLD-------GKFYAVKvlqkKIVLNrKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTT 233
Cdd:cd14019   2 KYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALK----HIYPT-SSPSRILNELECLERLGGSNNVSGLITAFRNE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGGElFFHLQRERSFPEHRARFYAaeIASALGYLHSIKIVYRDLKPENILLDS-VGHVVLTDFGLCKEGI 312
Cdd:cd14019  77 DQVVAVLPYIEHDD-FRDFYRKMSLTDIRIYLRN--LFKALKHVHSFGIIHRDVKPGNFLYNReTGKGVLVDFGLAQREE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDTTTTFCGTPEYLAPEVIRKQPYDNT-VDWWCLGAVLYEMLYGL-PPFYCRDVAEmydnilhkplSLRPGVSLTAWS 390
Cdd:cd14019 154 DRPEQRAPRAGTRGFRAPEVLFKCPHQTTaIDIWSAGVILLSILSGRfPFFFSSDDID----------ALAEIATIFGSD 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 75813626 391 ----ILEELLEKDRQNRLGAkEDFLeiqNHPFF 419
Cdd:cd14019 224 eaydLLDKLLELDPSKRITA-EEAL---KHPFF 252
PX_SNARE cd06897
The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain ...
15-119 1.37e-16

The phosphoinositide binding Phox Homology domain of SNARE proteins from fungi; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of fungal proteins similar to Saccharomyces cerevisiae Vam7p. They contain an N-terminal PX domain and a C-terminal SNARE domain. The SNARE (Soluble NSF attachment protein receptor) family of proteins are integral membrane proteins that serve as key factors for vesicular trafficking. Vam7p is anchored at the vacuolar membrane through the specific interaction of its PX domain with phosphatidylinositol-3-phosphate (PI3P) present in bilayers. It plays an essential role in vacuole fusion. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction.


Pssm-ID: 132807  Cd Length: 108  Bit Score: 75.39  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  15 SVSIPSSDEHRekkKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMAL-KIPAKRIFGDNF-DPDFIKQRRA 92
Cdd:cd06897   2 EISIPTTSVSP---KPYTVYNIQVRLPLRSYTVSRRYSEFVALHKQLESEVGIEPPyPLPPKSWFLSTSsNPKLVEERRV 78
                        90       100
                ....*....|....*....|....*....
gi 75813626  93 GLNEFIQNLV--RYPELYNHPDVRAFLQM 119
Cdd:cd06897  79 GLEAFLRALLndEDSRWRNSPAVKEFLNL 107
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
168-403 1.43e-16

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: 79.36  E-value: 1.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLlakrklDGKFY---AVKVLqkKIVLNRKEQkhIMAERN--VLLKNVKHPFLVgLHYSFQTTEKLYFVLDF 242
Cdd:cd14062   1 IGSGSFGTVY------KGRWHgdvAVKKL--NVTDPTPSQ--LQAFKNevAVLRKTRHVNIL-LFMGYMTKPQLAIVTQW 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC--KEGIAISDTTT 319
Cdd:cd14062  70 CEGSSLYKHLHvLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKTRWSGSQQFE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 320 TFCGTPEYLAPEVIRKQ---PYDNTVDWWCLGAVLYEMLYGLPPFY---CRD-VAEMYDNILHKP-LS-LRPGVSLTAWS 390
Cdd:cd14062 150 QPTGSILWMAPEVIRMQdenPYSFQSDVYAFGIVLYELLTGQLPYShinNRDqILFMVGRGYLRPdLSkVRSDTPKALRR 229
                       250
                ....*....|...
gi 75813626 391 ILEELLEKDRQNR 403
Cdd:cd14062 230 LMEDCIKFQRDER 242
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
164-355 1.66e-16

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: 79.94  E-value: 1.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKL----DGKFYAVKVLQKKIVlnrKEQKHIMAERNVLlKNVKHPFLV---GLHYSfQTTEKL 236
Cdd:cd05081   8 YISQLGKGNFGSVELCRYDPlgdnTGALVAVKQLQHSGP---DQQRDFQREIQIL-KALHSDFIVkyrGVSYG-PGRRSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQRERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAIS 315
Cdd:cd05081  83 RLVMEYLPSGCLRDFLQRHRARLDASRLLlYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAK--LLPL 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75813626 316 DTTTTFCGTPE-----YLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd05081 161 DKDYYVVREPGqspifWYAPESLSDNIFSRQSDVWSFGVVLYELF 205
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
158-408 1.86e-16

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: 79.28  E-value: 1.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFlkvIGKGSFGKVLLAKRKLDGKFYAVKVLqkkivlnrkEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd13995   5 RNIGSDF---IPRGAFGKVYLAQDTKTKKRMACKLI---------PVEQFKPSDVEIQACFRHENIAELYGALLWEETVH 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVgHVVLTDFGLCKEGIAISDT 317
Cdd:cd13995  73 LFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMST-KAVLVDFGLSVQMTEDVYV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF---YCRDVAEMYDNILHK---PLS-LRPGVSLTAWS 390
Cdd:cd13995 152 PKDLRGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWvrrYPRSAYPSYLYIIHKqapPLEdIAQDCSPAMRE 231
                       250
                ....*....|....*...
gi 75813626 391 ILEELLEKDRQNRLGAKE 408
Cdd:cd13995 232 LLEAALERNPNHRSSAAE 249
PX_SNX13 cd06873
The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a ...
24-120 2.19e-16

The phosphoinositide binding Phox Homology domain of Sorting Nexin 13; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX13, also called RGS-PX1, contains an N-terminal PXA domain, a regulator of G protein signaling (RGS) domain, a PX domain, and a C-terminal domain that is conserved in some SNXs. It specifically binds to the stimulatory subunit of the heterotrimeric G protein G(alpha)s, serving as its GTPase activating protein, through the RGS domain. It preferentially binds phosphatidylinositol-3-phosphate (PI3P) through the PX domain and is localized in early endosomes. SNX13 is involved in endosomal sorting of EGFR into multivesicular bodies (MVB) for delivery to the lysosome.


Pssm-ID: 132783  Cd Length: 120  Bit Score: 75.38  E-value: 2.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  24 HREKKKRFTVYKVLVSV----GRSE-WFVFRRYAEFDKLYNTLKKQFPAMA-LKIPAKRIFgDNFDPDFIKQRRAGLNEF 97
Cdd:cd06873  15 VKEHGKTYAVYAISVTRiypnGQEEsWHVYRRYSDFHDLHMRLKEKFPNLSkLSFPGKKTF-NNLDRAFLEKRRKMLNQY 93
                        90       100
                ....*....|....*....|....*..
gi 75813626  98 IQNLVRYPELYNHPD----VRAFLQMD 120
Cdd:cd06873  94 LQSLLNPEVLDANPGlqeiVLDFLEPG 120
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
164-419 3.06e-16

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: 78.51  E-value: 3.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKV---IGKGSFGKVLlakRKLDGKfYAVKV----LQKKIVLNRKEQKhiMAERNVLLKNVKHPFLVGLHYSFQTTEK- 235
Cdd:cd14033   2 FLKFnieIGRGSFKTVY---RGLDTE-TTVEVawceLQTRKLSKGERQR--FSEEVEMLKGLQHPNIVRFYDSWKSTVRg 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 ---LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHS--IKIVYRDLKPENILLDS-VGHVVLTDFGLCK 309
Cdd:cd14033  76 hkcIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSrcPPILHRDLKCDNIFITGpTGSVKIGDLGLAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 egIAISDTTTTFCGTPEYLAPEVIRKQpYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILH--KPLSLRPGVSL 386
Cdd:cd14033 156 --LKRASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSeCQNAAQIYRKVTSgiKPDSFYKVKVP 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 75813626 387 TAWSILEELLEKDRQNRLgAKEDFLEiqnHPFF 419
Cdd:cd14033 233 ELKEIIEGCIRTDKDERF-TIQDLLE---HRFF 261
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
161-365 3.21e-16

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: 79.66  E-value: 3.21e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGkfyaVKVLQKKIvlnRKEQKHIMAERNV----LLKNVKHPFLVGLH-----YSFQ 231
Cdd:cd07849   6 RYQNLSYIGEGAYGMVCSAVHKPTG----QKVAIKKI---SPFEHQTYCLRTLreikILLRFKHENIIGILdiqrpPTFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 232 TTEKLYFVLDFVnggELFFH-LQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE 310
Cdd:cd07849  79 SFKDVYIVQELM---ETDLYkLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARI 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 311 GIAISDTT---TTFCGTPEYLAPEV-IRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRD 365
Cdd:cd07849 156 ADPEHDHTgflTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKD 214
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
120-366 3.40e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 80.27  E-value: 3.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  120 DSPKHQSDPSEDEDERSSQKLHSTSQNINLGPSGNPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKfyAVKVLQKKIVL 199
Cdd:PHA03207  52 DDVTHATDYDADEESLSPQTDVCQEPCETTSSSDPASVVRMQYNILSSLTPGSEGEVFVCTKHGDEQ--RKKVIVKAVTG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  200 NRKEQKHIMaernvLLKNVKHPFLVGLHYSFQTTEKLYFVLDfVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHS 279
Cdd:PHA03207 130 GKTPGREID-----ILKTISHRAIINLIHAYRWKSTVCMVMP-KYKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHG 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  280 IKIVYRDLKPENILLDSVGHVVLTDFG-LCKEGIAIsDTTTTF--CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY 356
Cdd:PHA03207 204 RGIIHRDVKTENIFLDEPENAVLGDFGaACKLDAHP-DTPQCYgwSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSV 282
                        250
                 ....*....|
gi 75813626  357 GLPPFYCRDV 366
Cdd:PHA03207 283 KNVTLFGKQV 292
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
161-361 4.27e-16

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: 78.10  E-value: 4.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKldGKFYAVKVLQkkivlNRKEQKHIMAERNVLLKnVKHPFLVGLhYSFQTTEK--LYF 238
Cdd:cd05082   7 ELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCIK-----NDATAQAFLAEASVMTQ-LRHSNLVQL-LGVIVEEKggLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQ-RERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISD 316
Cdd:cd05082  78 VTEYMAKGSLVDYLRsRGRSVLGGDCLLkFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQD 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 317 TTTTfcgTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05082 158 TGKL---PVKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPY 200
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
165-357 5.88e-16

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: 79.00  E-value: 5.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkivlnRKEQKHIMAERN----VLLKNVKHPFLVGL------HYSFQTTE 234
Cdd:cd07850   5 LKPIGSGAQGIVCAAYDTVTGQNVAIKKLS------RPFQNVTHAKRAyrelVLMKLVNHKNIIGLlnvftpQKSLEEFQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGgELFFHLQRErsFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAI 314
Cdd:cd07850  79 DVYLVMELMDA-NLCQVIQMD--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAG 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75813626 315 SDTTTT-FCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG 357
Cdd:cd07850 154 TSFMMTpYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRG 197
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
162-426 6.31e-16

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: 79.05  E-value: 6.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHY-----SFQTTEKL 236
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIN-DVFEHVSDATRILREIK-LLRLLRHPDIVEIKHimlppSRREFKDI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVnGGELFFHLQRERSF-PEHRaRFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAIS 315
Cdd:cd07859  80 YVVFELM-ESDLHQVIKANDDLtPEHH-QFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLAR--VAFN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DTTTT-----FCGTPEYLAPEVIRK--QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDV---------------------- 366
Cdd:cd07859 156 DTPTAifwtdYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVvhqldlitdllgtpspetisrv 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 367 ----AEMYDNILHK----PLSLR-PGVSLTAWSILEELLEKDRQNRLGAKEDFleiqNHPFFESLSWAD 426
Cdd:cd07859 236 rnekARRYLSSMRKkqpvPFSQKfPNADPLALRLLERLLAFDPKDRPTAEEAL----ADPYFKGLAKVE 300
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
168-361 7.69e-16

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 77.76  E-value: 7.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDgkfYAVKVLqkKIVLNRKEQKHIMAERNVLLKNVKHPFLVgLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14149  20 IGSGSFGTVYKGKWHGD---VAVKIL--KVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSS 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC--KEGIAISDTTTTFCGT 324
Cdd:cd14149  94 LYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRWSGSQQVEQPTGS 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQ---PYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14149 174 ILWMAPEVIRMQdnnPFSFQSDVYSYGIVLYELMTGELPY 213
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
166-361 7.75e-16

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: 77.46  E-value: 7.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKV---LLAKRKLDGKFYAVKVLQKKIVLNRKEQkhIMAErNVLLKNVKHPFLVGLhYSFQTTEKLYFVLDF 242
Cdd:cd05056  12 RCIGEGQFGDVyqgVYMSPENEKIAVAVKTCKNCTSPSVREK--FLQE-AYIMRQFDHPHIVKL-IGVITENPVWIVMEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISDT---T 318
Cdd:cd05056  88 APLGELRSYLQVNKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSR---YMEDEsyyK 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 75813626 319 TTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05056 165 ASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILmLGVKPF 209
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
158-371 9.02e-16

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 77.45  E-value: 9.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKF----YAVKVLQKKIvlNRKEQKHIMAERNVLlKNVKHPFLVGLhYSFQTT 233
Cdd:cd05057   5 KETELEKGKVLGSGAFGTVYKGVWIPEGEKvkipVAIKVLREET--GPKANEEILDEAYVM-ASVDHPHLVRL-LGICLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGGELFFHLQrersfpEHRARF-------YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd05057  81 SQVQLITQLMPLGCLLDYVR------NHRDNIgsqlllnWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFG 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 307 LCKEgIAISDTTTTFCG--TP-EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPPFYCRDVAEMYD 371
Cdd:cd05057 155 LAKL-LDVDEKEYHAEGgkVPiKWMALESIQYRIYTHKSDVWSYGVTVWElMTFGAKPYEGIPAVEIPD 222
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
162-362 9.66e-16

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 77.76  E-value: 9.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd06634  17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQK-LRHPNTIEYRGCYLREHTAWLVME 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGElffhlqrERSFPEHRARFYAAEIAS-------ALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGlckeGIAI 314
Cdd:cd06634  96 YCLGSA-------SDLLEVHKKPLQEVEIAAithgalqGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFG----SASI 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 315 SDTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPFY 362
Cdd:cd06634 165 MAPANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIELAERKPPLF 215
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
162-420 1.04e-15

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: 78.21  E-value: 1.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRK--LDGKFYAVK----VLQKKIVLNR--KEQKhimaernvLLKNVK-HPFLVGLhysfqt 232
Cdd:cd07857   2 YELIKELGQGAYGIVCSARNAetSEEETVAIKkitnVFSKKILAKRalRELK--------LLRHFRgHKNITCL------ 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 teklyFVLDFVNGG---ELFFH-----------LQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG 298
Cdd:cd07857  68 -----YDMDIVFPGnfnELYLYeelmeadlhqiIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADC 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 299 HVVLTDFGLCKeGIAI-----SDTTTTFCGTPEYLAPEV-IRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDN 372
Cdd:cd07857 143 ELKICDFGLAR-GFSEnpgenAGFMTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQ 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 373 ILH------------------------------KPL-SLRPGVSLTAWSILEELLEKDRQNRLGAkEDFLEiqnHPFFE 420
Cdd:cd07857 222 ILQvlgtpdeetlsrigspkaqnyirslpnipkKPFeSIFPNANPLALDLLEKLLAFDPTKRISV-EEALE---HPYLA 296
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
168-361 1.48e-15

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: 76.64  E-value: 1.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDgkfYAVKVLQkkIVLNRKEQKHIMAERNVLLKNVKHPFLVgLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14151  16 IGSGSFGTVYKGKWHGD---VAVKMLN--VTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC--KEGIAISDTTTTFCGT 324
Cdd:cd14151  90 LYHHLHiIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSGS 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 75813626 325 PEYLAPEVIRKQ---PYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14151 170 ILWMAPEVIRMQdknPYSFQSDVYAFGIVLYELMTGQLPY 209
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
168-361 2.17e-15

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 76.03  E-value: 2.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLlaKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVG-LHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14064   1 IGSGSFGKVY--KGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCR-LNHPCVIQfVGACLDDPSQFAIVTQYVSGG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELF--FHLQRERSFPEHRARFyAAEIASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFG----LCKEGiaiSDTT 318
Cdd:cd14064  78 SLFslLHEQKRVIDLQSKLII-AVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGesrfLQSLD---EDNM 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75813626 319 TTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14064 154 TKQPGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
162-361 2.21e-15

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: 77.86  E-value: 2.21e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQK------HIMAERNVLLKNVKHpflVGLHYSFQTTEK 235
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRQAAEeirileHLKKQDKDNTMNVIH---MLESFTFRNHIC 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELffhLQRER--SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH--VVLTDFGL-CKE 310
Cdd:cd14224 144 MTFELLSMNLYEL---IKKNKfqGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSsCYE 220
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 311 GIAIsdttTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14224 221 HQRI----YTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLF 267
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
162-373 3.87e-15

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: 76.61  E-value: 3.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQGQIEVGILARLSNENADEFNFVRAYECFQHRNHTCLVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-DSVGH---VVLTDFGlckegiAISD 316
Cdd:cd14229  82 MLEQNLYDFLKQNKFSpLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvDPVRQpyrVKVIDFG------SASH 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 317 TTTTFCGT----PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycrDVAEMYDNI 373
Cdd:cd14229 156 VSKTVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY---PGALEYDQI 213
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
164-364 4.25e-15

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: 75.50  E-value: 4.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAK----RKLDGKFYAVKVLQKKivlnrKEQKHIMA-ERNV-LLKNVKHPFLV---GLHYSfQTTE 234
Cdd:cd05038   8 FIKQLGEGHFGSVELCRydplGDNTGEQVAVKSLQPS-----GEEQHMSDfKREIeILRTLDHEYIVkykGVCES-PGRR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFFHLQRERSFPEH-RARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIA 313
Cdd:cd05038  82 SLRLIMEYLPSGSLRDYLQRHRDQIDLkRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK--VL 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 314 ISDTTTTFCGTPE-----YLAPEVIRKQPYDNTVDWWCLGAVLYEMLYglppfYCR 364
Cdd:cd05038 160 PEDKEYYYVKEPGespifWYAPECLRESRFSSASDVWSFGVTLYELFT-----YGD 210
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
164-360 4.64e-15

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: 75.51  E-value: 4.64e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKLDGKFY----AVKVLQKKIVLN-RKEQKHIMAERNVLLKNVKHPFLVGLHySFQTTE--KL 236
Cdd:cd14001   3 FMKKLGYGTGVNVYLMKRSPRGGSSrspwAVKKINSKCDKGqRSLYQERLKEEAKILKSLNHPNIVGFR-AFTKSEdgSL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFvnGGELFFHLQRER------SFPEHRARFYAAEIASALGYLHSIK-IVYRDLKPENILLDSVGHVV-LTDFG-- 306
Cdd:cd14001  82 CLAMEY--GGKSLNDLIEERyeaglgPFPAATILKVALSIARALEYLHNEKkILHGDIKSGNVLIKGDFESVkLCDFGvs 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 307 --LCKEGIAISDTTTTFCGTPEYLAPEVI-RKQPYDNTVDWWCLGAVLYEMLYGLPP 360
Cdd:cd14001 160 lpLTENLEVDSDPKAQYVGTEPWKAKEALeEGGVITDKADIFAYGLVLWEMMTLSVP 216
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
168-354 4.69e-15

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: 75.87  E-value: 4.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKvlqKKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYfvldfvNGG 246
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALK---KVLMENEKEGFPITALREIkILQLLKHENVVNLIEICRTKATPY------NRY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRErsFPEH---------RARFYAAEIA-------SALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE 310
Cdd:cd07865  91 KGSIYLVFE--FCEHdlagllsnkNVKFTLSEIKkvmkmllNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARA 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75813626 311 -GIAISDTTTTFCG---TPEYLAPEV-IRKQPYDNTVDWWCLGAVLYEM 354
Cdd:cd07865 169 fSLAKNSQPNRYTNrvvTLWYRPPELlLGERDYGPPIDMWGAGCIMAEM 217
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
169-361 5.42e-15

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: 74.61  E-value: 5.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 169 GKGSFGKVLLAKRKLDGKFYAVKVLQKkivlnrkeqkhIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGEL 248
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLK-----------IEKEAEIL-SVLSHRNIIQFYGAILEAPNYGIVTEYASYGSL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 249 FFHLQRERS--FPEHRARFYAAEIASALGYLHS---IKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISDTT-TTFC 322
Cdd:cd14060  70 FDYLNSNESeeMDMDQIMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASR---FHSHTThMSLV 146
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14060 147 GTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
161-420 6.28e-15

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: 75.09  E-value: 6.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKV---IGKGSFGKVLlakRKLDGKfYAVKV----LQKKiVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTT 233
Cdd:cd14030  23 DGRFLKFdieIGRGSFKTVY---KGLDTE-TTVEVawceLQDR-KLSKSERQRFKEEAG-MLKGLQHPNIVRFYDSWEST 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EK----LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILLDS-VGHVVLTDFG 306
Cdd:cd14030  97 VKgkkcIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 LCKegIAISDTTTTFCGTPEYLAPEVIRKQpYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILH--KPLSLRPG 383
Cdd:cd14030 177 LAT--LKRASFAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSeCQNAAQIYRRVTSgvKPASFDKV 253
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 75813626 384 VSLTAWSILEELLEKDRQNRLGAKedflEIQNHPFFE 420
Cdd:cd14030 254 AIPEVKEIIEGCIRQNKDERYAIK----DLLNHAFFQ 286
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
261-361 9.31e-15

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: 75.29  E-value: 9.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 261 HRaRFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTT-----TTFCGTPEYLAPEVIRK 335
Cdd:cd07852 108 HK-QYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDenpvlTDYVATRWYRAPEILLG 186
                        90       100
                ....*....|....*....|....*..
gi 75813626 336 QP-YDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07852 187 STrYTKGVDMWSVGCILGEMLLGKPLF 213
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
165-376 1.63e-14

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 75.08  E-value: 1.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvLNRKEQKHIMAERnVLLKNVKHPFLVGL------HYSFQTTEKLYF 238
Cdd:cd07875  29 LKPIGSGAQGIVCAAYDAILERNVAIKKLSRPF-QNQTHAKRAYREL-VLMKCVNHKNIIGLlnvftpQKSLEEFQDVYI 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGgELFFHLQRErsFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGiaisdtT 318
Cdd:cd07875 107 VMELMDA-NLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA------G 177
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75813626 319 TTFCGTPE-----YLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK 376
Cdd:cd07875 178 TSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQ 240
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
162-364 1.71e-14

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 74.24  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRK--LDGKFYAVKvlqkKIVLNRKEQKHI--MAERNV-LLKNVKHPFLVGLHYSF--QTTE 234
Cdd:cd07842   2 YEIEGCIGRGTYGRVYKAKRKngKDGKEYAIK----KFKGDKEQYTGIsqSACREIaLLRELKHENVVSLVEVFleHADK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVN---GGELFFHLQ-RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFG 306
Cdd:cd07842  78 SVYLLFDYAEhdlWQIIKFHRQaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75813626 307 LCKegIAISDTTTTFCGTPE-----YLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCR 364
Cdd:cd07842 158 LAR--LFNAPLKPLADLDPVvvtiwYRAPELLLgARHYTKAIDIWAIGCIFAELLTLEPIFKGR 219
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
164-355 1.80e-14

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: 73.90  E-value: 1.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAK----RKLDGKFYAVKVLQkkivlnRKEQKHIMA-ERNV-LLKNVKHPFLV---GLHYSfQTTE 234
Cdd:cd14205   8 FLQQLGKGNFGSVEMCRydplQDNTGEVVAVKKLQ------HSTEEHLRDfEREIeILKSLQHDNIVkykGVCYS-AGRR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFFHLQRERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIA 313
Cdd:cd14205  81 NLRLIMEYLPYGSLRDYLQKHKERIDHIKLLqYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTK--VL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 314 ISDTTTTFCGTPE-----YLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd14205 159 PQDKEYYKVKEPGespifWYAPESLTESKFSVASDVWSFGVVLYELF 205
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
160-361 2.04e-14

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: 73.94  E-value: 2.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNR-KEQKHIMAERNV-LLKNVKHPFLVGLHYSF--QTTEK 235
Cdd:cd07845   7 TEFEKLNRIGEGTYGIVYRARDTTSGEIVALK----KVRMDNeRDGIPISSLREItLLLNLRHPNIVELKEVVvgKHLDS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNG--GELFFHLQRerSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GI 312
Cdd:cd07845  83 IFLVMEYCEQdlASLLDNMPT--PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTyGL 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISDTTTTFCgTPEYLAPEVI-RKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07845 161 PAKPMTPKVV-TLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLL 209
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
168-354 2.91e-14

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: 73.08  E-value: 2.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAK---------RKLDGKFYAVKVLQKKIVLNRKEQKHimaeRNVLL--KNVKHPFLVGLHYSFQTTEKL 236
Cdd:cd14152   8 IGQGRWGKVHRGRwhgevairlLEIDGNNQDHLKLFKKEVMNYRQTRH----ENVVLfmGACMHPPHLAIITSFCKGRTL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 Y-FVLDfvnggelffhlqRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVVLTDFGLCK-EGIAI 314
Cdd:cd14152  84 YsFVRD------------PKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDN-GKVVITDFGLFGiSGVVQ 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 75813626 315 SDTTTTFCGTPE----YLAPEVIRKQ---------PYDNTVDWWCLGAVLYEM 354
Cdd:cd14152 151 EGRRENELKLPHdwlcYLAPEIVREMtpgkdedclPFSKAADVYAFGTIWYEL 203
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
166-361 2.92e-14

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 73.09  E-value: 2.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNVLLKNVK-HPFLVGL--HYSFQTTEKLYFVL-- 240
Cdd:cd14037   9 KYLAEGGFAHVYLVKTSNGGNRAALK----RVYVNDEHDLNVCKREIEIMKRLSgHKNIVGYidSSANRSGNGVYEVLll 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 -DFVNGGELF-FHLQRERSfpehraRFYAAEI-------ASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd14037  85 mEYCKGGGVIdLMNQRLQT------GLTESEIlkifcdvCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGSAT 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75813626 310 EGIAISDTTTTFC---------GTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14037 159 TKILPPQTKQGVTyveedikkyTTLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYTTPF 222
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
167-379 3.38e-14

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: 72.77  E-value: 3.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd05047   2 VIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRER----------------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK- 309
Cdd:cd05047  82 NLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRg 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 310 EGIAISDTTTTFcgTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI-----LHKPLS 379
Cdd:cd05047 162 QEVYVKKTMGRL--PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLpqgyrLEKPLN 235
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
198-365 4.07e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 73.88  E-value: 4.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  198 VLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGgELFFHLQRERSFPEHRARFYAAEIASALGYL 277
Cdd:PHA03212 120 VVIKAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  278 HSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAIS-DTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY 356
Cdd:PHA03212 199 HENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINaNKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMAT 278

                 ....*....
gi 75813626  357 GLPPFYCRD 365
Cdd:PHA03212 279 CHDSLFEKD 287
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
165-361 4.12e-14

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: 73.44  E-value: 4.12e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKK-----------IVLNRKEQKHIMAERNVLLKNVKHpFLVGLHYSfqtt 233
Cdd:cd14212   4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKpayfrqamleiAILTLLNTKYDPEDKHHIVRLLDH-FMHHGHLC---- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 ekLYFVLDFVNGGELFfHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSV--GHVVLTDFG-LCKE 310
Cdd:cd14212  79 --IVFELLGVNLYELL-KQNQFRGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFGsACFE 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 311 GiaisDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14212 156 N----YTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLF 202
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
162-361 4.30e-14

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 73.20  E-value: 4.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnRKEQKHIMAERNVL----------LKNVKHpflVGLHYSFQ 231
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNK----KRFHHQALVEVKILdalrrkdrdnSHNVIH---MKEYFYFR 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 232 TTEKLYFVLDFVNGGELffhLQRE--RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH--VVLTDFGL 307
Cdd:cd14225 118 NHLCITFELLGMNLYEL---IKKNnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDFGS 194
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 308 -CKEGIAIsdttTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14225 195 sCYEHQRV----YTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLF 245
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
164-419 4.54e-14

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: 72.42  E-value: 4.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKV---IGKGSFGKVLlakRKLDGKFYaVKV----LQKKIVLNRKEQKhiMAERNVLLKNVKHPFLVGLHYSFQTTEK- 235
Cdd:cd14032   2 FLKFdieLGRGSFKTVY---KGLDTETW-VEVawceLQDRKLTKVERQR--FKEEAEMLKGLQHPNIVRFYDFWESCAKg 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 ---LYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIK--IVYRDLKPENILLDS-VGHVVLTDFGLCK 309
Cdd:cd14032  76 krcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 310 egIAISDTTTTFCGTPEYLAPEVIRKQpYDNTVDWWCLGAVLYEMLYGLPPFY-CRDVAEMYDNILH--KPLSLRPGVSL 386
Cdd:cd14032 156 --LKRASFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSeCQNAAQIYRKVTCgiKPASFEKVTDP 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 75813626 387 TAWSILEELLEKDRQNRLGAKedflEIQNHPFF 419
Cdd:cd14032 233 EIKEIIGECICKNKEERYEIK----DLLSHAFF 261
PX_IRAS cd06875
The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor ...
15-104 4.62e-14

The phosphoinositide binding Phox Homology domain of the Imidazoline Receptor Antisera-Selected; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Imidazoline Receptor Antisera-Selected (IRAS), also called nischarin, contains an N-terminal PX domain, leucine rich repeats, and a predicted coiled coil domain. The PX domain of IRAS binds to phosphatidylinositol-3-phosphate in membranes. Together with the coiled coil domain, it is essential for the localization of IRAS to endosomes. IRAS has been shown to interact with integrin and inhibit cell migration. Its interaction with alpha5 integrin causes a redistribution of the receptor from the cell surface to endosomal structures, suggesting that IRAS may function as a sorting nexin (SNX) which regulates the endosomal trafficking of integrin. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132785  Cd Length: 116  Bit Score: 68.46  E-value: 4.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  15 SVSIPSSdehrEKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMALKIPAKRIFGdNFDPDFIKQRRAGL 94
Cdd:cd06875   5 KIRIPSA----ETVEGYTVYIIEVKVGSVEWTVKHRYSDFAELHDKLVAEHKVDKDLLPPKKLIG-NKSPSFVEKRRKEL 79
                        90
                ....*....|
gi 75813626  95 NEFIQNLVRY 104
Cdd:cd06875  80 EIYLQTLLSF 89
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
165-435 7.32e-14

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 72.75  E-value: 7.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvLNRKEQKHIMAERnVLLKNVKHPFLVGL------HYSFQTTEKLYF 238
Cdd:cd07876  26 LKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPF-QNQTHAKRAYREL-VLLKCVNHKNIISLlnvftpQKSLEEFQDVYL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGEL-FFHLQRErsfpEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGiAISDT 317
Cdd:cd07876 104 VMELMDANLCqVIHMELD----HERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA-CTNFM 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL----------------------- 374
Cdd:cd07876 179 MTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIeqlgtpsaefmnrlqptvrnyve 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 375 HKPlsLRPGVSLT---------------------AWSILEELLEKDRQNRLGAKEDFleiqNHPFFEslSWADLVQKKIP 433
Cdd:cd07876 259 NRP--QYPGISFEelfpdwifpseserdklktsqARDLLSKMLVIDPDKRISVDEAL----RHPYIT--VWYDPAEAEAP 330

                ..
gi 75813626 434 PP 435
Cdd:cd07876 331 PP 332
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
159-377 8.01e-14

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: 71.52  E-value: 8.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKLDGKFyAVKVLQKKIVlnrkEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd05112   3 PSELTFVQEIGSGQFGLVHLGYWLNKDKV-AIKTIREGAM----SEEDFIEEAEVMMK-LSHPKLVQLYGVCLEQAPICL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAISDT 317
Cdd:cd05112  77 VFEFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTR--FVLDDQ 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 318 TTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY-GLPPFYCRDVAEMYDNI-----LHKP 377
Cdd:cd05112 155 YTSSTGTKfpvKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDInagfrLYKP 223
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
162-373 8.30e-14

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: 71.70  E-value: 8.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQkkiVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd07839   2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVR---LDDDDEGVPSSALREIcLLKELKHKNIVRLYDVLHSDKKLTLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGgELFFHLQRERSFPEHR-ARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE-GIAISdtt 318
Cdd:cd07839  79 EYCDQ-DLKKYFDSCNGDIDPEiVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAfGIPVR--- 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 319 ttfCGTPE-----YLAPEVI-RKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:cd07839 155 ---CYSAEvvtlwYRPPDVLfGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRI 213
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
166-403 9.78e-14

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 71.44  E-value: 9.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGK---FYAVKVLqkKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd05066  10 KVIGAGEFGEVCSGRLKLPGKreiPVAIKTL--KAGYTEKQRRDFLSEASIM-GQFDHPNIIHLEGVVTRSKPVMIVTEY 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRersfpeHRARFYAAE-------IASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGIA 313
Cdd:cd05066  87 MENGSLDAFLRK------HDGQFTVIQlvgmlrgIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvlEDDP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 314 ISDTTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPPFY---CRDVAEMYDNILHKPLSLRPGVSLta 388
Cdd:cd05066 161 EAAYTTRGGKIPiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYWemsNQDVIKAIEEGYRLPAPMDCPAAL-- 238
                       250
                ....*....|....*
gi 75813626 389 WSILEELLEKDRQNR 403
Cdd:cd05066 239 HQLMLDCWQKDRNER 253
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
158-354 1.09e-13

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: 71.06  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKldGKF-YAVKVLQKkivlNRKEQKHIMAERNVLLkNVKHPFLVGLHYSFQTTEKL 236
Cdd:cd05113   2 DPKDLTFLKELGTGQFGVVKYGKWR--GQYdVAIKMIKE----GSMSEDEFIEEAKVMM-NLSHEKLVQLYGVCTKQRPI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQrersfpEHRARFYAAE-------IASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd05113  75 FIITEYMANGCLLNYLR------EMRKRFQTQQllemckdVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSR 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 310 egIAISDTTTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEM 354
Cdd:cd05113 149 --YVLDDEYTSSVGSKfpvRWSPPEVLMYSKFSSKSDVWAFGVLMWEV 194
PX_MDM1p cd06876
The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a ...
16-117 1.17e-13

The phosphoinositide binding Phox Homology domain of yeast MDM1p; The PX domain is a phosphoinositide binding (PI) module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. Yeast MDM1p is a filament-like protein localized in punctate structures distributed throughout the cytoplasm. It plays an important role in nuclear and mitochondrial transmission to daughter buds. Members of this subfamily show similar domain architectures as some sorting nexins (SNXs). Some members are similar to SNX19 in that they contain an N-terminal PXA domain, a central PX domain, and a C-terminal domain that is conserved in some SNXs. Others are similar to SNX13 and SNX14, which also harbor these three domains as well as a regulator of G protein signaling (RGS) domain in between the PXA and PX domains. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132786  Cd Length: 133  Bit Score: 67.72  E-value: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  16 VSIPSSDEHREK-KKRFTVYkvLVSVGR-------SEWFVFRRYAEFDKLYNTLKKQFPAMA-LKIPAKRIFGDNFDP-D 85
Cdd:cd06876  22 VSIQSYISDVEEeGKEFVVY--LIEVQRlnnddqsSGWVVARRYSEFLELHKYLKKRYPGVLkLDFPQKRKISLKYSKtL 99
                        90       100       110
                ....*....|....*....|....*....|..
gi 75813626  86 FIKQRRAGLNEFIQNLVRYPELYNHPDVRAFL 117
Cdd:cd06876 100 LVEERRKALEKYLQELLKIPEVCEDEEFRKFL 131
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
168-361 1.20e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 71.39  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  168 IGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRK-EQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:PLN00009  10 IGEGTYGVVYKARDRVTNETIALK----KIRLEQEdEGVPSTAIREIsLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  246 gELFFHLQRERSFPE--HRARFYAAEIASALGYLHSIKIVYRDLKPENILLD-SVGHVVLTDFGLCKE-GIAISdTTTTF 321
Cdd:PLN00009  86 -DLKKHMDSSPDFAKnpRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLARAfGIPVR-TFTHE 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 75813626  322 CGTPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:PLN00009 164 VVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLF 204
PX_RUN cd07277
The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX ...
15-102 1.26e-13

The phosphoinositide binding Phox Homology domain of uncharacterized proteins containing PX and RUN domains; The PX domain is a phosphoinositide (PI) binding module involved in targeting proteins to PI-enriched membranes. Members in this subfamily are uncharacterized proteins containing an N-terminal RUN domain and a C-terminal PX domain. PX domain harboring proteins have been implicated in highly diverse functions such as cell signaling, vesicular trafficking, protein sorting, lipid modification, cell polarity and division, activation of T and B cells, and cell survival. In addition to protein-lipid interaction, the PX domain may also be involved in protein-protein interaction. The RUN domain is found in GTPases in the Rap and Rab families and may play a role in Ras-like signaling pathways.


Pssm-ID: 132810  Cd Length: 118  Bit Score: 67.37  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  15 SVSIPS-------SDEHRekkkrftVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAM-ALKIPAKRIFGdNFDPDF 86
Cdd:cd07277   2 NVWIPSvflrgkgSDAHH-------VYQVYIRIRDDEWNVYRRYSEFYELHKKLKKKFPVVrSFDFPPKKAIG-NKDAKF 73
                        90
                ....*....|....*.
gi 75813626  87 IKQRRAGLNEFIQNLV 102
Cdd:cd07277  74 VEERRKRLQVYLRRVV 89
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
168-353 1.28e-13

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 70.73  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEqKHIMAERnvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd05084   4 IGRGNFGEVFSGRLRADNTPVAVKSCRETLPPDLKA-KFLQEAR--ILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFPEHRARFYAAE-IASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK-EGIAISDTTTTFCGTP 325
Cdd:cd05084  81 FLTFLRTEGPRLKVKELIRMVEnAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSReEEDGVYAATGGMKQIP 160
                       170       180
                ....*....|....*....|....*....
gi 75813626 326 -EYLAPEVIRKQPYDNTVDWWCLGAVLYE 353
Cdd:cd05084 161 vKWTAPEALNYGRYSSESDVWSFGILLWE 189
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
166-361 1.94e-13

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: 70.29  E-value: 1.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLlakrklDGKFYAVKVLQKKIVLNRKEQKHImaERNVLLKNVKHPFLVGLhYSFQTTEKLYFVLDFVNG 245
Cdd:cd05083  12 EIIGEGEFGAVL------QGEYMGQKVAVKNIKCDVTAQAFL--EETAVMTKLQHKNLVRL-LGVILHNGLYIVMELMSK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQ-RERSF-PEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTfcg 323
Cdd:cd05083  83 GNLVNFLRsRGRALvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDNSRL--- 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 324 TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05083 160 PVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFsYGRAPY 198
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
168-360 2.00e-13

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: 70.38  E-value: 2.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRkLDGKFYAVKVLQKKIVLNRKEQ------KHIMA-----------ERNVLLKNVKHP---FLVGLh 227
Cdd:cd14067   1 LGQGGSGTVIYRAR-YQGQPVAVKRFHIKKCKKRTDGsadtmlKHLRAadamknfsefrQEASMLHSLQHPcivYLIGI- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 228 ysfqTTEKLYFVLDFVNGGELFFHLQ---RERSFPE--HRARFYAA-EIASALGYLHSIKIVYRDLKPENIL---LDSVG 298
Cdd:cd14067  79 ----SIHPLCFALELAPLGSLNTVLEenhKGSSFMPlgHMLTFKIAyQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQE 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75813626 299 HV--VLTDFGLCKEgiAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPP 360
Cdd:cd14067 155 HIniKLSDYGISRQ--SFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRP 216
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
168-306 2.04e-13

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: 67.08  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQkkiVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEK-LYFVLDFVNGG 246
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGD---DVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDVDGpNILLMELVKGG 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQrERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd13968  78 TLIAYTQ-EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
168-355 2.41e-13

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: 70.45  E-value: 2.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVL--LAKRKLDGKFY---AVKVLQKKIvlNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd05032  14 LGQGSFGMVYegLAKGVVKGEPEtrvAIKTVNENA--SMRERIEFLNEASVM-KEFNCHHVVRLLGVVSTGQPTLVVMEL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERS--------FPEHRARFY--AAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC---- 308
Cdd:cd05032  91 MAKGDLKSYLRSRRPeaennpglGPPTLQKFIqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTrdiy 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75813626 309 ------KEGIAIsdttttfcgTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd05032 171 etdyyrKGGKGL---------LPvRWMAPESLKDGVFTTKSDVWSFGVVLWEMA 215
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
158-408 3.14e-13

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 70.05  E-value: 3.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKF----YAVKVLQKKIvlNRKEQKHIMAERNVLlKNVKHPFLVGLhYSFQTT 233
Cdd:cd05109   5 KETELKKVKVLGSGAFGTVYKGIWIPDGENvkipVAIKVLRENT--SPKANKEILDEAYVM-AGVGSPYVCRL-LGICLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 234 EKLYFVLDFVNGGELFFHLQrersfpEHRARF-------YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd05109  81 STVQLVTQLMPYGCLLDYVR------ENKDRIgsqdllnWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 LCKEgIAISDTTTTFCG--TP-EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPP---FYCRDVAEMYDNilHKPLS 379
Cdd:cd05109 155 LARL-LDIDETEYHADGgkVPiKWMALESILHRRFTHQSDVWSYGVTVWElMTFGAKPydgIPAREIPDLLEK--GERLP 231
                       250       260
                ....*....|....*....|....*....
gi 75813626 380 LRPGVSLTAWSILEELLEKDRQNRLGAKE 408
Cdd:cd05109 232 QPPICTIDVYMIMVKCWMIDSECRPRFRE 260
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
165-376 3.40e-13

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 70.89  E-value: 3.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIvLNRKEQKHIMAERnVLLKNVKHPFLVGL------HYSFQTTEKLYF 238
Cdd:cd07874  22 LKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPF-QNQTHAKRAYREL-VLMKCVNHKNIISLlnvftpQKSLEEFQDVYL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGgELFFHLQRErsFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGiAISDTT 318
Cdd:cd07874 100 VMELMDA-NLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA-GTSFMM 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 319 TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHK 376
Cdd:cd07874 176 TPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQ 233
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
159-361 3.46e-13

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 69.51  E-value: 3.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKLDgkfyaVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLhYSFQTTEK-LY 237
Cdd:cd05114   3 PSELTFMKELGSGLFGVVRLGKWRAQ-----YKVAIKAIREGAMSEEDFIEEAKVMMK-LTHPKLVQL-YGVCTQQKpIY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHL-QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAISD 316
Cdd:cd05114  76 IVTEFMENGCLLNYLrQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTR--YVLDD 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75813626 317 TTTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY-GLPPF 361
Cdd:cd05114 154 QYTSSSGAKfpvKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPF 202
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
161-373 4.45e-13

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: 69.64  E-value: 4.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05089   3 DIKFEDVIGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIAI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRER----------------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTD 304
Cdd:cd05089  83 EYAPYGNLLDFLRKSRvletdpafakehgtasTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIAD 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 305 FGLCK-EGIAISDTTTTFcgTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:cd05089 163 FGLSRgEEVYVKKTMGRL--PVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVsLGGTPYCGMTCAELYEKL 231
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
168-361 4.80e-13

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: 69.01  E-value: 4.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKeQKHIMAERnvLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETLPPDLK-RKFLQEAR--ILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKE---GI-AISDTTTTFc 322
Cdd:cd05041  80 LLTFLRKKGArLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREeedGEyTVSDGLKQI- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 75813626 323 gtP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05041 159 --PiKWTAPEALNYGRYTSESDVWSFGILLWEIFsLGATPY 197
PX_SNX22 cd06880
The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a ...
16-130 5.08e-13

The phosphoinositide binding Phox Homology domain of Sorting Nexin 22; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX22 may be involved in recruiting other proteins to the membrane via protein-protein and protein-ligand interaction. The biological function of SNX22 is not yet known.


Pssm-ID: 132790  Cd Length: 110  Bit Score: 65.37  E-value: 5.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  16 VSIPS-SDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMalKIPAKRIfgDNFDPDFIKQRRAGL 94
Cdd:cd06880   3 VSIPSyRLEVDESEKPYTVFTIEVLVNGRRHTVEKRYSEFHALHKKLKKSIKTP--DFPPKRV--RNWNPKVLEQRRQGL 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 75813626  95 NEFIQNLVRYPELYNHpdVRAFLQMDSPkhQSDPSE 130
Cdd:cd06880  79 EAYLQGLLKINELPKQ--LLDFLGVRHF--PSLPKS 110
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
155-379 5.15e-13

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (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. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. 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. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 69.64  E-value: 5.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 155 PHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTE 234
Cdd:cd05088   2 PVLEWNDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 235 KLYFVLDFVNGGELFFHLQRER----------------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVG 298
Cdd:cd05088  82 YLYLAIEYAPHGNLLDFLRKSRvletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENY 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 299 HVVLTDFGLCKeGIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI---- 373
Cdd:cd05088 162 VAKIADFGLSR-GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLpqgy 240

                ....*..
gi 75813626 374 -LHKPLS 379
Cdd:cd05088 241 rLEKPLN 247
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
162-373 6.35e-13

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: 70.12  E-value: 6.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14228  17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-DSVGH---VVLTDFGLCKEgiAISD 316
Cdd:cd14228  97 MLEQNLYDFLKQNKFSpLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvDPVRQpyrVKVIDFGSASH--VSKA 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycrDVAEMYDNI 373
Cdd:cd14228 175 VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY---PGASEYDQI 228
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
421-487 8.01e-13

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 63.15  E-value: 8.01e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626    421 SLSWADLVQKKIPPPFNPNVAGPDDIRNFDTAFTEETVPYSVCvssDYSIVNASvleADDAFVGFSY 487
Cdd:smart00133   2 GIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPV---DSPLSGGI---QQEPFRGFSY 62
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
168-361 8.25e-13

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: 68.68  E-value: 8.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAkRKLDGKFYAVKvlqkKIVLNRKEQKHIMAERNV-LLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14664   1 IGRGGAGTVYKG-VMPNGTLVAVK----RLKGEGTQGGDHGFQAEIqTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 EL--FFHLQRERSFP---EHRARFyAAEIASALGYLH---SIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISDT- 317
Cdd:cd14664  76 SLgeLLHSRPESQPPldwETRQRI-ALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAK---LMDDKd 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 318 ---TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14664 152 shvMSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
164-361 8.39e-13

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 68.53  E-value: 8.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAkrkldgkFY--AVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd05072  11 LVKKLGAGQFGEVWMG-------YYnnSTKVAVKTLKPGTMSVQAFLEEAN-LMKTLQHDKLVRLYAVVTKEEPIYIITE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERSFPEHRARF--YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISDTTT 319
Cdd:cd05072  83 YMAKGSLLDFLKSDEGGKVLLPKLidFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLAR---VIEDNEY 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 320 TF---CGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05072 160 TAregAKFPiKWTAPEAINFGSFTIKSDVWSFGILLYEIVtYGKIPY 206
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
164-424 1.08e-12

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: 68.20  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLlakrklDGKF-----YAVKVLqKKIVLNRKEqkhIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYF 238
Cdd:cd05068  12 LLRKLGSGQFGEVW------EGLWnnttpVAVKTL-KPGTMDPED---FLREAQIM-KKLRHPKLIQLYAVCTLEEPIYI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRE-RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgIAISDT 317
Cdd:cd05068  81 ITELMKHGSLLEYLQGKgRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARV-IKVEDE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNILH-----KPlslrPGVSLTA 388
Cdd:cd05068 160 YEAREGAKfpiKWTAPEAANYNRFSIKSDVWSFGILLTEIVtYGRIPYPGMTNAEVLQQVERgyrmpCP----PNCPPQL 235
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 75813626 389 WSILEELLEKDRQNRlgakedfleiqnhPFFESLSW 424
Cdd:cd05068 236 YDIMLECWKADPMER-------------PTFETLQW 258
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
165-356 1.23e-12

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: 68.75  E-value: 1.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLqkkivlnRKEQKHIMA---ERNVLLK-NVKHPF----LVGLHYSFQ----- 231
Cdd:cd14134  17 LRLLGEGTFGKVLECWDRKRKRYVAVKII-------RNVEKYREAakiEIDVLETlAEKDPNgkshCVQLRDWFDyrghm 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 232 --TTEKL-YFVLDFVNGgelffhlQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDS------------ 296
Cdd:cd14134  90 ciVFELLgPSLYDFLKK-------NNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynpkkk 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75813626 297 --VGHVVLTDFGLCKEGIAISDTT--TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEmLY 356
Cdd:cd14134 163 rqIRVPKSTDIKLIDFGSATFDDEyhSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVE-LY 225
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
166-355 1.36e-12

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 68.07  E-value: 1.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKldGKFYAVKVLqkkivlNRKEQKHIMAER----NVLLKnvkHPFLVGL----HYSFQTTEKLY 237
Cdd:cd14056   1 KTIGKGRYGEVWLGKYR--GEKVAVKIF------SSRDEDSWFRETeiyqTVMLR---HENILGFiaadIKSTGSWTQLW 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSFPEHRARFyAAEIASALGYLHS--------IKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd14056  70 LITEYHEHGSLYDYLQRNTLDTEEALRL-AYSAASGLAHLHTeivgtqgkPAIAHRDLKSKNILVKRDGTCCIADLGLAV 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 310 EGIAISDTT----TTFCGTPEYLAPEVIRKQPYDN------TVDWWCLGAVLYEML 355
Cdd:cd14056 149 RYDSDTNTIdippNPRVGTKRYMAPEVLDDSINPKsfesfkMADIYSFGLVLWEIA 204
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
159-362 1.37e-12

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: 67.78  E-value: 1.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKLDGK---FYAVKVLqkKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEK 235
Cdd:cd05033   3 ASYVTIEKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTL--KSGYSDKQRLDFLTEASIM-GQFDHPNVIRLEGVVTKSRP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQrersfpEHRARFYAAE-------IASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd05033  80 VMIVTEYMENGSLDKFLR------ENDGKFTVTQlvgmlrgIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLS 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 309 KEGIAISDTTTTFCG-TP-EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPPFY 362
Cdd:cd05033 154 RRLEDSEATYTTKGGkIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSYGERPYW 210
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
166-362 1.38e-12

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 67.97  E-value: 1.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGK---FYAVKVLqkKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd05065  10 EVIGAGEFGEVCRGRLKLPGKreiFVAIKTL--KSGYTEKQRRDFLSEASIM-GQFDHPNIIHLEGVVTKSRPVMIITEF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGEL-FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGIAISDTTT 319
Cdd:cd05065  87 MENGALdSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRflEDDTSDPTYT 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 320 TFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPPFY 362
Cdd:cd05065 167 SSLGGKipiRWTAPEAIAYRKFTSASDVWSYGIVMWEvMSYGERPYW 213
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
269-375 1.57e-12

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 67.52  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 269 EIASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFGLCK-EGIAISD--TTTTFCGTPEYLAPEVIRK--QPYDNT 341
Cdd:cd14025 100 ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwNGLSHSHdlSRDGLRGTIAYLPPERFKEknRCPDTK 179
                        90       100       110
                ....*....|....*....|....*....|....
gi 75813626 342 VDWWCLGAVLYEMLYGLPPFycrdvaEMYDNILH 375
Cdd:cd14025 180 HDVYSFAIVIWGILTQKKPF------AGENNILH 207
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
166-400 1.68e-12

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 67.73  E-value: 1.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVL-NRKEQKHIMAERnVLLKNVKHPFLVGL-HYSFQTTEKLYF----- 238
Cdd:cd05075   6 KTLGEGEFGSVMEGQLNQDDSVLKVAVKTMKIAIcTRSEMEDFLSEA-VCMKEFDHPNVMRLiGVCLQNTESEGYpspvv 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 239 VLDFVNGGELFFHLQRER------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEgI 312
Cdd:cd05075  85 ILPFMKHGDLHSFLLYSRlgdcpvYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSKK-I 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 313 AISD--TTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEM-LYGLPPFYCRDVAEMYD-----NILHKPLSLRPG 383
Cdd:cd05075 164 YNGDyyRQGRISKMPvKWIAIESLADRVYTTKSDVWSFGVTMWEIaTRGQTPYPGVENSEIYDylrqgNRLKQPPDCLDG 243
                       250       260
                ....*....|....*....|
gi 75813626 384 V---SLTAWsileELLEKDR 400
Cdd:cd05075 244 LyelMSSCW----LLNPKDR 259
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
164-369 1.84e-12

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 67.73  E-value: 1.84e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLLAKRKLDG----KFYAVKVLQKkivLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd05090   9 FMEELGECAFGKIYKGHLYLPGmdhaQLVAIKTLKD---YNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCML 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 240 LDFVNGGELF-FHLQRE---------------RSFPEHRARFYAA-EIASALGYLHSIKIVYRDLKPENILLDSVGHVVL 302
Cdd:cd05090  86 FEFMNQGDLHeFLIMRSphsdvgcssdedgtvKSSLDHGDFLHIAiQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKI 165
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 303 TDFGLCKEgIAISDtttTFCGTPE------YLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYC---RDVAEM 369
Cdd:cd05090 166 SDLGLSRE-IYSSD---YYRVQNKsllpirWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGfsnQEVIEM 238
PX_SNX20_21_like cd07279
The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain ...
18-120 2.13e-12

The phosphoinositide binding Phox Homology domain of Sorting Nexins 20 and 21; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX20, SNX21, and similar proteins. SNX20 interacts with P-Selectin glycoprotein ligand-1 (PSGL-1), a surface-expressed mucin that acts as a ligand for the selectin family of adhesion proteins. It may function in the sorting and cycling of PSGL-1 into endosomes. SNX21, also called SNX-L, is distinctly and highly-expressed in fetal liver and may be involved in protein sorting and degradation during embryonic liver development.


Pssm-ID: 132812  Cd Length: 112  Bit Score: 63.50  E-value: 2.13e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  18 IPSSDEHREKKKRFTVYKVLV----SVGRSEWFVFRRYAEFDKLYNTLKKQFPAMALKI--PAKRIFGdNFDPDFIKQRR 91
Cdd:cd07279   5 IVSARTVKEGEKKYVVYQLAVvqtgDPDTQPAFIERRYSDFLKLYKALRKQHPQLMAKVsfPRKVLMG-NFSSELIAERS 83
                        90       100
                ....*....|....*....|....*....
gi 75813626  92 AGLNEFIQNLVRYPELYNHPDVRAFLQMD 120
Cdd:cd07279  84 RAFEQFLGHILSIPNLRDSKAFLDFLQGP 112
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
165-373 2.23e-12

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 67.22  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFyAVKVLQKKIVlnrkEQKHIMAERNvLLKNVKHPFLVGLHySFQTTEKLYFVLDFVN 244
Cdd:cd05067  12 VERLGAGQFGEVWMGYYNGHTKV-AIKSLKQGSM----SPDAFLAEAN-LMKQLQHQRLVRLY-AVVTQEPIYIITEYME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGEL--FFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAISDTTTTFC 322
Cdd:cd05067  85 NGSLvdFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLAR--LIEDNEYTARE 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 323 GTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNI 373
Cdd:cd05067 163 GAKfpiKWTAPEAINYGTFTIKSDVWSFGILLTEIVtHGRIPYPGMTNPEVIQNL 217
PX_SNX4 cd06864
The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a ...
47-119 2.24e-12

The phosphoinositide binding Phox Homology domain of Sorting Nexin 4; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX4 is involved in recycling traffic from the sorting endosome (post-Golgi endosome) back to the late Golgi. It shows a similar domain architecture as SNX1-2, among others, containing a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. SNX4 is implicated in the regulation of plasma membrane receptor trafficking and interacts with receptors for EGF, insulin, platelet-derived growth factor and the long form of the leptin receptor.


Pssm-ID: 132774  Cd Length: 129  Bit Score: 63.93  E-value: 2.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  47 VFRRYAEFDKLYNTLKKQFPAMALK-IPAKRI-FG------DNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQ 118
Cdd:cd06864  48 LWRRYSEFELLRNYLVVTYPYVIVPpLPEKRAmFMwqklssDTFDPDFVERRRAGLENFLLRVAGHPELCQDKIFLEFLT 127

                .
gi 75813626 119 M 119
Cdd:cd06864 128 H 128
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
162-373 2.63e-12

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 68.19  E-value: 2.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14227  17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILARLSTESADDYNFVRAYECFQHKNHTCLVFE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQRERS-FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH----VVLTDFGLCKEgiAISD 316
Cdd:cd14227  97 MLEQNLYDFLKQNKFSpLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRqpyrVKVIDFGSASH--VSKA 174
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 317 TTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFycrDVAEMYDNI 373
Cdd:cd14227 175 VCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLY---PGASEYDQI 228
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
160-361 3.14e-12

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: 67.14  E-value: 3.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVL-NRKEQKHIMAERNV-LLKNVKHPFLVGLH---------Y 228
Cdd:cd07864   7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALK----KVRLdNEKEGFPITAIREIkILRQLNHRSVVNLKeivtdkqdaL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 229 SF-QTTEKLYFVLDFVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGL 307
Cdd:cd07864  83 DFkKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGL 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 308 CKegIAISDTTTTFCG---TPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd07864 163 AR--LYNSEESRPYTNkviTLWYRPPELLLgEERYGPAIDVWSCGCILGELFTKKPIF 218
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
267-357 3.42e-12

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 66.75  E-value: 3.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 267 AAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTtfcGTPEYLAPEVIRKQpYDNTVDWWC 346
Cdd:cd13975 108 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIV---GTPIHMAPELFSGK-YDNSVDVYA 183
                        90
                ....*....|.
gi 75813626 347 LGAVLYEMLYG 357
Cdd:cd13975 184 FGILFWYLCAG 194
PX_SNX1_2_like cd06859
The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is ...
31-120 3.52e-12

The phosphoinositide binding Phox Homology domain of Sorting Nexins 1 and 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. This subfamily consists of SNX1, SNX2, and similar proteins. They harbor a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. Both domains have been shown to determine the specific membrane-targeting of SNX1. SNX1 and SNX2 are components of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures effcient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex.


Pssm-ID: 132769 [Multi-domain]  Cd Length: 114  Bit Score: 62.98  E-value: 3.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  31 FTVYKV-----LVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMAL-KIPAKRIFG-DNFDPDFIKQRRAGLNEFIQNLVR 103
Cdd:cd06859  18 YVVYRVttktnLPDFKKSEFSVLRRYSDFLWLYERLVEKYPGRIVpPPPEKQAVGrFKVKFEFIEKRRAALERFLRRIAA 97
                        90
                ....*....|....*..
gi 75813626 104 YPELYNHPDVRAFLQMD 120
Cdd:cd06859  98 HPVLRKDPDFRLFLESD 114
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
158-361 3.61e-12

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 67.35  E-value: 3.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKI--VLNRKEQKHIMAERNVLlKNVKHPFLVGLhYSFQTTEK 235
Cdd:cd05108   5 KETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELreATSPKANKEILDEAYVM-ASVDNPHVCRL-LGICLTST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQrersfpEHRARF-------YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd05108  83 VQLITQLMPFGCLLDYVR------EHKDNIgsqyllnWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLA 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 309 KEGIAISDTTTTFCG-TP-EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPPF 361
Cdd:cd05108 157 KLLGAEEKEYHAEGGkVPiKWMALESILHRIYTHQSDVWSYGVTVWElMTFGSKPY 212
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
168-371 3.69e-12

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: 66.75  E-value: 3.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKldGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd14158  23 LGEGGFGVVFKGYIN--DKNVAVKKLAAMVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGS 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQRERSFP--EHRARFYAAE-IASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT--TTTFC 322
Cdd:cd14158 101 LLDRLACLNDTPplSWHMRCKIAQgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTimTERIV 180
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 323 GTPEYLAPEVIRKQPYDNTvDWWCLGAVLYEMLYGLPPF-YCRDVAEMYD 371
Cdd:cd14158 181 GTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGLPPVdENRDPQLLLD 229
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
162-310 3.73e-12

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: 66.33  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivlnrKEQKHIMAERNVL--LKNvkHPFLVGLHYSFQTTEKLYFV 239
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKD-----SKHPQLEYEAKVYklLQG--GPGIPRLYWFGQEGDYNVMV 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 240 LDFV--NGGELFfhLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL---DSVGHVVLTDFGLCKE 310
Cdd:cd14016  75 MDLLgpSLEDLF--NKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAKK 148
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
162-361 3.94e-12

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: 67.34  E-value: 3.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKivLNRKEQKHI-------MAERNVLLKNvkhpFLVGL--HYSFQT 232
Cdd:cd14226  15 YEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNK--KAFLNQAQIevrllelMNKHDTENKY----YIVRLkrHFMFRN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 233 TEKLYFVLDFVNGGELFFHlQRERSFPEHRARFYAAEIASALGYLHS--IKIVYRDLKPENILLDSV--GHVVLTDFG-L 307
Cdd:cd14226  89 HLCLVFELLSYNLYDLLRN-TNFRGVSLNLTRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLCNPkrSAIKIIDFGsS 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 75813626 308 CKEGIAISDttttFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14226 168 CQLGQRIYQ----YIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLF 217
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
162-355 4.07e-12

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: 67.20  E-value: 4.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLN---------------RKEQKHIMAERNVLLKN-VKHPFLVG 225
Cdd:cd13977   2 YSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRCNAPENvelalrefwalssiqRQHPNVIQLEECVLQRDgLAQRMSHG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 226 LHYS------FQTTEK------------LYFVLDFVNGGELFFHLQRERSFPEHRARFyAAEIASALGYLHSIKIVYRDL 287
Cdd:cd13977  82 SSKSdlylllVETSLKgercfdprsacyLWFVMEFCDGGDMNEYLLSRRPDRQTNTSF-MLQLSSALAFLHRNQIVHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 288 KPENILL-DSVGHVVL--TDFGLCK--EGIAISDTT---------TTFCGTPEYLAPEVIRKQpYDNTVDWWCLGAVLYE 353
Cdd:cd13977 161 KPDNILIsHKRGEPILkvADFGLSKvcSGSGLNPEEpanvnkhflSSACGSDFYMAPEVWEGH-YTAKADIFALGIIIWA 239

                ..
gi 75813626 354 ML 355
Cdd:cd13977 240 MV 241
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
166-361 4.16e-12

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 66.15  E-value: 4.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFyAVKVLQKKIVlnrkEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGTTKV-AVKTLKPGTM----SPEAFLQEAQIM-KKLRHDKLVQLYAVCSDEEPIYIVTELMSK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQ--RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVV-LTDFGLC---KEGIAISDTTT 319
Cdd:cd05034  75 GSLLDYLRtgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGE-NNVCkVADFGLArliEDDEYTAREGA 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 75813626 320 TFcgtP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05034 154 KF---PiKWTAPEAALYGRFTIKSDVWSFGILLYEIVtYGRVPY 194
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
166-376 5.43e-12

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: 65.83  E-value: 5.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVllakRKLD-----GKFY--AVKVLqKKIVLNRKEQ-KHIMAERNVLLKnVKHPFLVGLhYSFQTTEKLY 237
Cdd:cd05040   1 EKLGDGSFGVV----RRGEwttpsGKVIqvAVKCL-KSDVLSQPNAmDDFLKEVNAMHS-LDHPNLIRL-YGVVLSSPLM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRE-RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegiAISD 316
Cdd:cd05040  74 MVTELAPLGSLLDRLRKDqGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMR---ALPQ 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 317 TTTTFCGTPE------YLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEmydnILHK 376
Cdd:cd05040 151 NEDHYVMQEHrkvpfaWCAPESLKTRKFSHASDVWMFGVTLWEMFtYGEEPWLGLNGSQ----ILEK 213
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
166-361 5.57e-12

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: 65.80  E-value: 5.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKlDGKFYAVKVLQKKIvlnRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNG 245
Cdd:cd05085   2 ELLGKGNFGEVYKGTLK-DKTPVAVKTCKEDL---PQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTTFCGT 324
Cdd:cd05085  78 GDFLSFLRKKKdELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQI 157
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 325 P-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05085 158 PiKWTAPEALNYGRYSSESDVWSFGILLWETFsLGVCPY 196
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
166-360 6.44e-12

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: 66.14  E-value: 6.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLA-KRKLDGK----FYAVKVLQKKIvlNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05045   6 KTLGEGEFGKVVKAtAFRLKGRagytTVAVKMLKENA--SSSELRDLLSEFN-LLKQVNHPHVIKLYGACSQDGPLLLIV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRERSF------------------PEHRAR------FYAAEIASALGYLHSIKIVYRDLKPENILLDS 296
Cdd:cd05045  83 EYAKYGSLRSFLRESRKVgpsylgsdgnrnssyldnPDERALtmgdliSFAWQISRGMQYLAEMKLVHRDLAARNVLVAE 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75813626 297 VGHVVLTDFGLCKEGIAISDTTTTFCG-TP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY-------GLPP 360
Cdd:cd05045 163 GRKMKISDFGLSRDVYEEDSYVKRSKGrIPvKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlggnpypGIAP 235
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
163-370 6.46e-12

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 66.55  E-value: 6.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 163 DFLKVIGKGSFGK--VLLAKRKLDGKFYAVKvlqkKIVL---NRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd08216   1 ELLYEIGKCFKGGgvVHLAKHKPTNTLVAVK----KINLesdSKEDLKFLQQEIL-TSRQLQHPNILPYVTSFVVDNDLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAIS 315
Cdd:cd08216  76 VVTPLMAYGSCRDLLKThfPEGLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHG 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75813626 316 DTTTTFCGTPEY-------LAPEVIRK--QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMY 370
Cdd:cd08216 156 KRQRVVHDFPKSseknlpwLSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPFSDMPATQML 219
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
168-355 6.68e-12

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 65.57  E-value: 6.68e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVlqKKIVLNRKEqkhiMAERNVLLKNVKHP----FL-VGLHYSfqtteKLYFVLDF 242
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKM--NTLSSNRAN----MLREVQLMNRLSHPnilrFMgVCVHQG-----QLHALTEY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELFFHLQRERSFP-EHRARFyAAEIASALGYLHSIKIVYRDLKPENILL--DSVGH-VVLTDFGLCKEGIAISDTT 318
Cdd:cd14155  70 INGGNLEQLLDSNEPLSwTVRVKL-ALDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYtAVVGDFGLAEKIPDYSDGK 148
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 75813626 319 TTF--CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd14155 149 EKLavVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
168-371 6.71e-12

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 65.91  E-value: 6.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRKLDGKFYAVKVLqKKIVLNRKEqkhiMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLDFVNGGE 247
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTL-KEDTMEVEE----FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 248 LFFHLQR--ERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAISDTTTTFCGTP 325
Cdd:cd05052  89 LLDYLREcnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSR--LMTGDTYTAHAGAK 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 326 ---EYLAPEVIRKQPYDNTVDWWCLGAVLYEM-LYGLPPFYCRDVAEMYD 371
Cdd:cd05052 167 fpiKWTAPESLAYNKFSIKSDVWAFGVLLWEIaTYGMSPYPGIDLSQVYE 216
PX_MONaKA cd06871
The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain ...
45-121 7.04e-12

The phosphoinositide binding Phox Homology domain of Modulator of Na,K-ATPase; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. MONaKA (Modulator of Na,K-ATPase) binds the plasma membrane ion transporter, Na,K-ATPase, and modulates its enzymatic and ion pump activities. It modulates brain Na,K-ATPase and may be involved in regulating electrical excitability and synaptic transmission. MONaKA contains an N-terminal PX domain and a C-terminal catalytic kinase domain. The PX domain interacts with PIs and plays a role in targeting proteins to PI-enriched membranes.


Pssm-ID: 132781  Cd Length: 120  Bit Score: 62.38  E-value: 7.04e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626  45 WFVFRRYAEFDKLYNTLkkQFPAMALKIPAKRIFGdNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQMDS 121
Cdd:cd06871  38 WQVIRRYNDFDLLNASL--QISGISLPLPPKKLIG-NMDREFIAERQQGLQNYLNVILMNPILASCLPVKKFLDPNN 111
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
162-359 7.17e-12

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: 66.32  E-value: 7.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14211   1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQGQIEVSILSRLSQENADEFNFVRAYECFQHKNHTCLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNggELFFHLQRERSF---PEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-DSVGH---VVLTDFGlckegiAI 314
Cdd:cd14211  81 MLE--QNLYDFLKQNKFsplPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLvDPVRQpyrVKVIDFG------SA 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 75813626 315 SDTTTTFCGT----PEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLP 359
Cdd:cd14211 153 SHVSKAVCSTylqsRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWP 201
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
166-447 9.28e-12

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: 66.24  E-value: 9.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKfyavKVLQKKIV---LNRKEQKHIMAERNvLLKNVKHPFLVGLH-----YSFQTTEKLY 237
Cdd:cd07858  11 KPIGRGAYGIVCSAKNSETNE----KVAIKKIAnafDNRIDAKRTLREIK-LLRHLDHENVIAIKdimppPHREAFNDVY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGgELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDT 317
Cdd:cd07858  86 IVYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSEKGDF 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 318 TTTFCGTPEYLAPEVIRK-QPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVA------------------EMYDN------ 372
Cdd:cd07858 165 MTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVhqlklitellgspseedlGFIRNekarry 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 373 ILHKPLSLR-------PGVSLTAWSILEELLEKDRQNRLGAKEDFleiqNHPFFESLSwaDLVQKKI-PPPFNPNVA--- 441
Cdd:cd07858 245 IRSLPYTPRqsfarlfPHANPLAIDLLEKMLVFDPSKRITVEEAL----AHPYLASLH--DPSDEPVcQTPFSFDFEeda 318

                ....*..
gi 75813626 442 -GPDDIR 447
Cdd:cd07858 319 lTEEDIK 325
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
161-419 1.07e-11

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: 65.71  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 161 DFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNR-KEQKHIMAER--NVLLKnVKHP-------FLVGlhysf 230
Cdd:cd07843   6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALK----KLKMEKeKEGFPITSLReiNILLK-LQHPnivtvkeVVVG----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 231 QTTEKLYFVLDFVNGgELffhlqreRSFPEH-RARFYAAEIA-------SALGYLHSIKIVYRDLKPENILLDSVGHVVL 302
Cdd:cd07843  76 SNLDKIYMVMEYVEH-DL-------KSLMETmKQPFLQSEVKclmlqllSGVAHLHDNWILHRDLKTSNLLLNNRGILKI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 303 TDFGLCKEGIAISDTTTTFCGTPEYLAPEVIRKQP-YDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL------- 374
Cdd:cd07843 148 CDFGLAREYGSPLKPYTQLVVTLWYRAPELLLGAKeYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFkllgtpt 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 375 --------------------HKPLSLR---PGVSLTAW--SILEELLEKDRQNRLGAKEDFleiqNHPFF 419
Cdd:cd07843 228 ekiwpgfselpgakkktftkYPYNQLRkkfPALSLSDNgfDLLNRLLTYDPAKRISAEDAL----KHPYF 293
COG5391 COG5391
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ...
5-148 1.19e-11

Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];


Pssm-ID: 227680 [Multi-domain]  Cd Length: 524  Bit Score: 66.74  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626   5 HTMDYKESCPsVSIPSSDEHR-EKKKRFTVYKV-----LVSVGRSE---WFVFRRYAEFDKLYNTLKKQFPAMAL-KIPA 74
Cdd:COG5391 125 TILDYFISST-VSNPQSLTLLvDSRDKHTSYEIitvtnLPSFQLREsrpLVVRRRYSDFESLHSILIKLLPLCAIpPLPS 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  75 KR----IFGDNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDV------RAFLQM--DSPKHQSDPSEDEDERSSQKLHS 142
Cdd:COG5391 204 KKsnseYYGDRFSDEFIEERRQSLQNFLRRVSTHPLLSNYKNSksweshSTLLSSfiENRKSVPTPLSLDLTSTTQELDM 283

                ....*.
gi 75813626 143 TSQNIN 148
Cdd:COG5391 284 ERKELN 289
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
166-362 1.26e-11

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


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 65.00  E-value: 1.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGK---FYAVKVLqkKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTEKLYFVLDF 242
Cdd:cd05063  11 KVIGAGEFGEVFRGILKMPGRkevAVAIKTL--KPGYTEKQRQDFLSEASIM-GQFSHHNIIRLEGVVTKFKPAMIITEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGELffhlqrERSFPEHRARFYAAE-------IASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK--EGIA 313
Cdd:cd05063  88 MENGAL------DKYLRDHDGEFSSYQlvgmlrgIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRvlEDDP 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 314 ISDTTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPPFY 362
Cdd:cd05063 162 EGTYTTSGGKIPiRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSFGERPYW 212
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
162-378 1.62e-11

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 64.94  E-value: 1.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKL-DGKF--YAVKVLQKKIVLNRKEQKHImaERNVLLKNVKHPF---LVGLHYSFQTTEK 235
Cdd:cd05074  11 FTLGRMLGKGEFGSVREAQLKSeDGSFqkVAVKMLKADIFSSSDIEEFL--REAACMKEFDHPNvikLIGVSLRSRAKGR 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 L---YFVLDFVNGGELFFHLQRER------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG 306
Cdd:cd05074  89 LpipMVILPFMKHGDLHTFLLMSRigeepfTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 LCKEgIAISDTTTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYE-MLYGLPPFYCRDVAEMYD-----NILHKP 377
Cdd:cd05074 169 LSKK-IYSGDYYRQGCASKlpvKWLALESLADNVYTTHSDVWAFGVTMWEiMTRGQTPYAGVENSEIYNylikgNRLKQP 247

                .
gi 75813626 378 L 378
Cdd:cd05074 248 P 248
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
166-361 2.33e-11

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 64.28  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFyAVKVLQKKIVlnrkEQKHIMAERNvLLKNVKHPFLVGLHySFQTTEKLYFVLDFVNG 245
Cdd:cd05073  17 KKLGAGQFGEVWMATYNKHTKV-AVKTMKPGSM----SVEAFLAEAN-VMKTLQHDKLVKLH-AVVTKEPIYIITEFMAK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARF--YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAISDTTTTFCG 323
Cdd:cd05073  90 GSLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLAR--VIEDNEYTAREG 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 75813626 324 TP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05073 168 AKfpiKWTAPEAINFGSFTIKSDVWSFGILLMEIVtYGRIPY 209
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
160-294 2.95e-11

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 63.89  E-value: 2.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 160 TDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKhimAERNVLLKNV--KHPFLVGLHYSFQTTEKLY 237
Cdd:cd14138   5 TEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQN---ALREVYAHAVlgQHSHVVRYYSAWAEDDHML 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 238 FVLDFVNGGELF----FHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL 294
Cdd:cd14138  82 IQNEYCNGGSLAdaisENYRIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFI 142
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
168-414 2.98e-11

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: 64.08  E-value: 2.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKrkLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLH-YSFQTtEKLYFVLDFVNGG 246
Cdd:cd14159   1 IGEGGFGCVYQAV--MRNTEYAVKRLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAgYSAQQ-GNYCLIYVYLPNG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQRERSFP----EHRARFyAAEIASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFGLCK-----EGIAIS 315
Cdd:cd14159  78 SLEDRLHCQVSCPclswSQRLHV-LLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLARfsrrpKQPGMS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 316 DT---TTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG---------LPPFYCRDVAEMYDNILHKPLSLRPG 383
Cdd:cd14159 157 STlarTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGrramevdscSPTKYLKDLVKEEEEAQHTPTTMTHS 236
                       250       260       270
                ....*....|....*....|....*....|.
gi 75813626 384 VSLTAWSILEELLEKDRQNRLGAKEDFLEIQ 414
Cdd:cd14159 237 AEAQAAQLATSICQKHLDPQAGPCPPELGIE 267
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
244-418 3.19e-11

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 63.36  E-value: 3.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL--DSVGHVVLTDFGLCKEGIAISDTTTTF 321
Cdd:cd14024  67 HYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFtdELRTKLVLVNLEDSCPLNGDDDSLTDK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 322 CGTPEYLAPEVI--RKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKD 399
Cdd:cd14024 147 HGCPAYVGPEILssRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRS 226
                       170
                ....*....|....*....
gi 75813626 400 RQNRLGAKEDFLeiqnHPF 418
Cdd:cd14024 227 PAERLKASEILL----HPW 241
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
166-354 3.39e-11

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: 63.87  E-value: 3.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLlakrklDGKFYAvKVLQKKIVLNRKEQKHIMA-ERNVL-LKNVKHPFLVGLHYSFQTTEKLYFVLDFV 243
Cdd:cd14153   6 ELIGKGRFGQVY------HGRWHG-EVAIRLIDIERDNEEQLKAfKREVMaYRQTRHENVVLFMGACMSPPHLAIITSLC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 244 NGGELFFHLQRERSFPE-HRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVVLTDFGLCK-EGIAIS----DT 317
Cdd:cd14153  79 KGRTLYSVVRDAKVVLDvNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDN-GKVVITDFGLFTiSGVLQAgrreDK 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 318 TTTFCGTPEYLAPEVIR---------KQPYDNTVDWWCLGAVLYEM 354
Cdd:cd14153 158 LRIQSGWLCHLAPEIIRqlspeteedKLPFSKHSDVFAFGTIWYEL 203
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
159-354 3.47e-11

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 63.62  E-value: 3.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTDFDFLKVIGKGSFGKVLLAKRKldGKFY-AVKVLQKKIVlnrKEQKHImaERNVLLKNVKHPFLVGLhYSFQTTEK-L 236
Cdd:cd05059   3 PSELTFLKELGSGQFGVVHLGKWR--GKIDvAIKMIKEGSM---SEDDFI--EEAKVMMKLSHPKLVQL-YGVCTKQRpI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQrersfpEHRARFYAA-------EIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK 309
Cdd:cd05059  75 FIVTEYMANGCLLNYLR------ERRGKFQTEqllemckDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLAR 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 75813626 310 egIAISDTTTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEM 354
Cdd:cd05059 149 --YVLDDEYTSSVGTKfpvKWSPPEVFMYSKFSSKSDVWSFGVLMWEV 194
PX_KIF16B_SNX23 cd06874
The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The ...
16-103 3.49e-11

The phosphoinositide binding Phox Homology domain of KIF16B kinesin or Sorting Nexin 23; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. KIF16B, also called sorting nexin 23 (SNX23), is a family-3 kinesin which harbors an N-terminal kinesin motor domain containing ATP and microtubule binding sites, a ForkHead Associated (FHA) domain, and a C-terminal PX domain. The PX domain of KIF16B binds to phosphatidylinositol-3-phosphate (PI3P) in early endosomes and plays a role in the transport of early endosomes to the plus end of microtubules. By regulating early endosome plus end motility, KIF16B modulates the balance between recycling and degradation of receptors. SNXs make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway.


Pssm-ID: 132784  Cd Length: 127  Bit Score: 60.47  E-value: 3.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  16 VSIPSSDEHREKKKRFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAM-ALKIPAKRIFGdNFDPDFIKQRRAGL 94
Cdd:cd06874   3 ITIPRYVLRGQGKDEHFEFEVKITVLDETWTVFRRYSRFRELHKTMKLKYPEVaALEFPPKKLFG-NKSERVAKERRRQL 81

                ....*....
gi 75813626  95 NEFIQNLVR 103
Cdd:cd06874  82 ETYLRNFFS 90
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
166-361 3.61e-11

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 64.40  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLQ-KKIVLNRKEQK--------HIMAERNV-LLKNVKHPFLVGLHYSFQTTEK 235
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYDTLTGKIVAIKKVKiIEISNDVTKDRqlvgmcgiHFTTLRELkIMNEIKHENIMGLVDVYVEGDF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  236 LYFVLDFVNGgELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEGI--A 313
Cdd:PTZ00024  95 INLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRYGypP 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626  314 ISDTTTTFCG-------TPE-----YLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:PTZ00024 174 YSDTLSKDETmqrreemTSKvvtlwYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGKPLF 234
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
154-420 4.57e-11

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 63.71  E-value: 4.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 154 NPHAKPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVL----QKKIvlnRKEQKhimaernvLLKNVK-HPFLVGLHY 228
Cdd:cd14132  12 VEWGSQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkpvkKKKI---KREIK--------ILQNLRgGPNIVKLLD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 229 SFQTTEKLY--FVLDFVNGgELFFHLQRERSFPEhrARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH-VVLTDF 305
Cdd:cd14132  81 VVKDPQSKTpsLIFEYVNN-TDFKTLYPTLTDYD--IRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDW 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 306 GLC------KEgiaisdtTTTFCGTPEYLAPEV-IRKQPYDNTVDWWCLGAVLYEMLYGLPPFYC-RDVAEMYDNI---- 373
Cdd:cd14132 158 GLAefyhpgQE-------YNVRVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHgHDNYDQLVKIakvl 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 374 -------------------LHKPLSLRPGVSLT--------------AWSILEELLEKDRQNRLGAKedflEIQNHPFFE 420
Cdd:cd14132 231 gtddlyayldkygielpprLNDILGRHSKKPWErfvnsenqhlvtpeALDLLDKLLRYDHQERITAK----EAMQHPYFD 306
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
164-355 5.30e-11

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: 63.41  E-value: 5.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVI---GKGSFGKVLLAKRKLDG----KFYAVKVLQKKivlNRKEQKHIMAERNVLLKNVKHPFLVglHYSFQTTEK- 235
Cdd:cd05079   5 FLKRIrdlGEGHFGKVELCRYDPEGdntgEQVAVKSLKPE---SGGNHIADLKKEIEILRNLYHENIV--KYKGICTEDg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 ---LYFVLDFVNGGELFFHLQRERSFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKeg 311
Cdd:cd05079  80 gngIKLIMEFLPSGSLKEYLPRNKNKINLKQQLkYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 75813626 312 iAISD-----TTTTFCGTPEY-LAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:cd05079 158 -AIETdkeyyTVKDDLDSPVFwYAPECLIQSKFYIASDVWSFGVTLYELL 206
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
170-421 7.03e-11

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 63.11  E-value: 7.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 170 KGSFGKVLL-----AKRKLDGKFYAVKVLQKK-------------IVLNRKEQKHimaernvlLKNVKHP-FLVGLHYSF 230
Cdd:cd14011   1 VASAGPGLPwkiynGSKKSTKQEVSVFVFEKKqleeyskrdreqiLELLKRGVKQ--------LTRLRHPrILTVQHPLE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 231 QTTEKLYFVLDFVNGgELF--FHLQRERSFPEHRARFY---AAEI-------ASALGYLH-SIKIVYRDLKPENILLDSV 297
Cdd:cd14011  73 ESRESLAFATEPVFA-SLAnvLGERDNMPSPPPELQDYklyDVEIkygllqiSEALSFLHnDVKLVHGNICPESVVINSN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 298 GHVVLTDFGLCKEGIAISDTTTTFCG-----------TPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLY-GLPPFYCRD 365
Cdd:cd14011 152 GEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNkGKPLFDCVN 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75813626 366 V-------AEMYDNILHKPLSLRPGvSLTawSILEELLEKDRQNRLgakeDFLEIQNHPFFES 421
Cdd:cd14011 232 NllsykknSNQLRQLSLSLLEKVPE-ELR--DHVKTLLNVTPEVRP----DAEQLSKIPFFDD 287
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
168-372 8.15e-11

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 62.29  E-value: 8.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVL--LAKRKLDGKFYAVKVLqKKIVLNRKEQKHIMAERNVLlKNVKHPFLVGLhYSFQTTEKLYFVLDFVNG 245
Cdd:cd05116   3 LGSGNFGTVKkgYYQMKKVVKTVAVKIL-KNEANDPALKDELLREANVM-QQLDNPYIVRM-IGICEAESWMLVMEMAEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 246 GELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCK-----EGIAISDTTTT 320
Cdd:cd05116  80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKalradENYYKAQTHGK 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75813626 321 FcgtP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFY---CRDVAEMYDN 372
Cdd:cd05116 160 W---PvKWYAPECMNYYKFSSKSDVWSFGVLMWEAFsYGQKPYKgmkGNEVTQMIEK 213
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
168-364 8.36e-11

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: 63.16  E-value: 8.36e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRK--LDGKFYAVKVLQKKIVlnrkeqkHIMAERNV-LLKNVKHPFLVGLHYSF--QTTEKLYFVLDF 242
Cdd:cd07867  10 VGRGTYGHVYKAKRKdgKDEKEYALKQIEGTGI-------SMSACREIaLLRELKHPNVIALQKVFlsHSDRKVWLLFDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGGE---LFFHL-----QRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFGLCK- 309
Cdd:cd07867  83 AEHDLwhiIKFHRaskanKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARl 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 310 -----EGIAISDTTTTfcgTPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCR 364
Cdd:cd07867 163 fnsplKPLADLDPVVV---TFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHCR 220
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
165-423 1.03e-10

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: 63.26  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKvlqkKIVLNRKEQ-KHIMAERNVLLK----------------NVKHPFLVGLH 227
Cdd:cd07854  10 LRPLGCGSNGLVFSAVDSDCDKRVAVK----KIVLTDPQSvKHALREIKIIRRldhdnivkvyevlgpsGSDLTEDVGSL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 228 YSFQTtekLYFVLDFVNGgELFFHLQRERSFPEHrARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVV-LTDFG 306
Cdd:cd07854  86 TELNS---VYIVQEYMET-DLANVLEQGPLSEEH-ARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVLkIGDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 307 LCK--------EGIAISDTTTTFCGTPEYLapevIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNIL---- 374
Cdd:cd07854 161 LARivdphyshKGYLSEGLVTKWYRSPRLL----LSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILesvp 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 375 -------------------------HKPLS-LRPGVSLTAWSILEELLEKDRQNRLGAKEDFLeiqnHPFFESLS 423
Cdd:cd07854 237 vvreedrnellnvipsfvrndggepRRPLRdLLPGVNPEALDFLEQILTFNPMDRLTAEEALM----HPYMSCYS 307
PX_YPT35 cd07280
The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain ...
21-117 1.05e-10

The phosphoinositide binding Phox Homology domain of the fungal protein YPT35; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions such as cell signaling, vesicular trafficking, protein sorting, and lipid modification, among others. This subfamily is composed of YPT35 proteins from the fungal subkingdom Dikarya. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction. The PX domain of YPT35 binds to phosphatidylinositol 3-phosphate (PI3P). It also serves as a protein interaction domain, binding to members of the Yip1p protein family, which localize to the ER and Golgi. YPT35 is mainly associated with endosomes and together with Yip1p proteins, may be involved in a specific function in the endocytic pathway.


Pssm-ID: 132813  Cd Length: 120  Bit Score: 58.88  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  21 SDEHREKKkrFTVYKVLVSV---GRSEWFVFRRYAEFDKLYNTLKKQFPAMALK----IPAKRIFGD---NFDPDFIKQR 90
Cdd:cd07280  14 GGDTGGGA--YVVWKITIETkdlIGSSIVAYKRYSEFVQLREALLDEFPRHKRNeipqLPPKVPWYDsrvNLNKAWLEKR 91
                        90       100
                ....*....|....*....|....*..
gi 75813626  91 RAGLNEFIQNLVRYPELYNHPDVRAFL 117
Cdd:cd07280  92 RRGLQYFLNCVLLNPVFGGSPVVKEFL 118
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
156-408 1.09e-10

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: 62.48  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 156 HAKPTDFDFLKVIGKGSFGKVLLAK-RKL----DGKFYAVKVLQKKIVLNRKEQKHIMAErnvLLKNVKHPFLVGLHYSF 230
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGEcYNLepeqDKMLVAVKTLKDASSPDARKDFEREAE---LLTNLQHENIVKFYGVC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 231 QTTEKLYFVLDFVNGGEL------------FFHLQRERSFPEHRARFY--AAEIASALGYLHSIKIVYRDLKPENILLDS 296
Cdd:cd05049  78 TEGDPLLMVFEYMEHGDLnkflrshgpdaaFLASEDSAPGELTLSQLLhiAVQIASGMVYLASQHFVHRDLATRNCLVGT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 297 VGHVVLTDFGLCKegiaisDTTTT----FCGTP----EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVA 367
Cdd:cd05049 158 NLVVKIGDFGMSR------DIYSTdyyrVGGHTmlpiRWMPPESILYRKFTTESDVWSFGVVLWEIFtYGKQPWFQLSNT 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75813626 368 EMYDNILHKPLSLRP-GVSLTAWSILEELLEKDRQNRLGAKE 408
Cdd:cd05049 232 EVIECITQGRLLQRPrTCPSEVYAVMLGCWKREPQQRLNIKD 273
PX_SNX2 cd07282
The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a ...
30-118 1.12e-10

The phosphoinositide binding Phox Homology domain of Sorting Nexin 2; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX2 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. Similar to SNX1, SNX2 contains a Bin/Amphiphysin/Rvs (BAR) domain, which detects membrane curvature, C-terminal to the PX domain. The PX domain of SNX2 preferentially binds phosphatidylinositol-3-phosphate (PI3P), but not PI(3,4,5)P3. Studies on mice deficient with SNX1 and/or SNX2 suggest that they provide an essential function in embryogenesis and are functionally redundant.


Pssm-ID: 132815  Cd Length: 124  Bit Score: 58.91  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  30 RFTVYKVLVSVGRSEWFVFRRYAEFDKLYNTLKKQFPAMALKIPA---KRIFG---------DNFDPDFIKQRRAGLNEF 97
Cdd:cd07282  22 RVTTKTSLSMFSRSEFSVRRRFSDFLGLHSKLASKYLHVGYIVPPapeKSIVGmtkvkvgkeDSSSTEFVEKRRAALERY 101
                        90       100
                ....*....|....*....|.
gi 75813626  98 IQNLVRYPELYNHPDVRAFLQ 118
Cdd:cd07282 102 LQRTVKHPTLLQDPDLRQFLE 122
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
168-364 1.65e-10

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: 62.38  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAKRK--LDGKFYAVKVLQKKIVlnrkeqkHIMAERNV-LLKNVKHPFLVGLHYSF--QTTEKLYFVLDF 242
Cdd:cd07868  25 VGRGTYGHVYKAKRKdgKDDKDYALKQIEGTGI-------SMSACREIaLLRELKHPNVISLQKVFlsHADRKVWLLFDY 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 243 VNGgELFFHLQRERS---------FPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL----DSVGHVVLTDFGLCK 309
Cdd:cd07868  98 AEH-DLWHIIKFHRAskankkpvqLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 310 ------EGIAISDTTTTfcgTPEYLAPEVIR-KQPYDNTVDWWCLGAVLYEMLYGLPPFYCR 364
Cdd:cd07868 177 lfnsplKPLADLDPVVV---TFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHCR 235
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
231-419 1.72e-10

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 61.22  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 231 QTTEKLYFVLDFvngGELFFHLQ-RERSFPEHRARFYAaEIASALGYLHSIKIVYRDLKPENILLDSVGHV-----VLTD 304
Cdd:cd14023  57 DTKAYVFFEKDF---GDMHSYVRsCKRLREEEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTqlrleSLED 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 305 FGLCK-EGIAISDTTttfcGTPEYLAPEVIRKQ-PYD-NTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLR 381
Cdd:cd14023 133 THIMKgEDDALSDKH----GCPAYVSPEILNTTgTYSgKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP 208
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 75813626 382 PGVSLTAWSILEELLEKDRQNRLGAKEDFLeiqnHPFF 419
Cdd:cd14023 209 DHVSPKARCLIRSLLRREPSERLTAPEILL----HPWF 242
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
220-419 2.30e-10

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 60.90  E-value: 2.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 220 HPFLVGLHYSFQTTEKLYFVLDfVNGGELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGH 299
Cdd:cd13976  44 HPNISGVHEVIAGETKAYVFFE-RDHGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEER 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 300 VVLTDFGLckEGIAI----SDTTTTFCGTPEYLAPEVIR-KQPYD-NTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNI 373
Cdd:cd13976 123 TKLRLESL--EDAVIlegeDDSLSDKHGCPAYVSPEILNsGATYSgKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKI 200
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75813626 374 LHKPLSLRPGVSLTAWSILEELLEKDRQNRLGAKEDFLeiqnHPFF 419
Cdd:cd13976 201 RRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDILL----HPWL 242
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
168-357 2.70e-10

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 61.05  E-value: 2.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLlaKRKLDGKFYAVKVL-QKKIVLNRKEQKHIMAERNVLLKNvKHPFLVGLHYSFQTTEKLYFVLDFVNGG 246
Cdd:cd14160   1 IGEGEIFEVY--RVRIGNRSYAVKLFkQEKKMQWKKHWKRFLSELEVLLLF-QHPNILELAAYFTETEKFCLVYPYMQNG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 247 ELFFHLQR---ERSFPEHRARFYAAEIASALGYLHSIK---IVYRDLKPENILLDSVGHVVLTDFGLCKEGIAISDTTTT 320
Cdd:cd14160  78 TLFDRLQChgvTKPLSWHERINILIGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFALAHFRPHLEDQSCT 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 75813626 321 FCGTPE------YLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG 357
Cdd:cd14160 158 INMTTAlhkhlwYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTG 200
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
164-372 2.90e-10

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 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: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 61.19  E-value: 2.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVLlaKRKLDG-------KFYAVKVLQKKIVLN-RKEQKHIMAERNVLlknvKHPFLVGLHYSFQTTEK 235
Cdd:cd05091  10 FMEELGEDRFGKVY--KGHLFGtapgeqtQAVAIKTLKDKAEGPlREEFRHEAMLRSRL----QHPNIVCLLGVVTKEQP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELF-FHLQRE--------------RSFPEHRARFY-AAEIASALGYLHSIKIVYRDLKPENILLDSVGH 299
Cdd:cd05091  84 MSMIFSYCSHGDLHeFLVMRSphsdvgstdddktvKSTLEPADFLHiVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLN 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 300 VVLTDFGLCKEGIAiSDTTTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPfYC----RDVAEMYD 371
Cdd:cd05091 164 VKISDLGLFREVYA-ADYYKLMGNSLlpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFsYGLQP-YCgysnQDVIEMIR 241

                .
gi 75813626 372 N 372
Cdd:cd05091 242 N 242
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
166-357 2.91e-10

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: 61.22  E-value: 2.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAK---RKLDGKFYAVKV--------------LQKKIVlNRKEQKHIMAERNvLLKNVKHPFLVGLHY 228
Cdd:cd13981   6 KELGEGGYASVYLAKdddEQSDGSLVALKVekppsiwefyicdqLHSRLK-NSRLRESISGAHS-AHLFQDESILVMDYS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 229 SFQTteklyfVLDFVNGgelfFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL-------------- 294
Cdd:cd13981  84 SQGT------LLDVVNK----MKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicadwpgegen 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75813626 295 --DSVGhVVLTDFGlckEGIaisDTT-----TTF---CGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYG 357
Cdd:cd13981 154 gwLSKG-LKLIDFG---RSI---DMSlfpknQSFkadWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFG 219
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
166-370 2.99e-10

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 61.18  E-value: 2.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAK-----RKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLYFVL 240
Cdd:cd05098  19 KPLGEGCFGQVVLAEaigldKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHLQRER-----------SFPEHRARFY-----AAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTD 304
Cdd:cd05098  99 EYASKGNLREYLQARRppgmeycynpsHNPEEQLSSKdlvscAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIAD 178
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 305 FGLCKE--GIAISDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMY 370
Cdd:cd05098 179 FGLARDihHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSPYPGVPVEELF 247
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
156-408 3.01e-10

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: 61.14  E-value: 3.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 156 HAKPTDFDFLKVIGKGSFGKVLLAK-----RKLDGKFYAVKVLqKKIVLNRKEQKHIMAErnvLLKNVKHPFLVGLHYSF 230
Cdd:cd05092   1 HIKRRDIVLKWELGEGAFGKVFLAEchnllPEQDKMLVAVKAL-KEATESARQDFQREAE---LLTVLQHQHIVRFYGVC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 231 QTTEKLYFVLDFVNGGEL--FF--HLQRERSFPEHRARFY-----------AAEIASALGYLHSIKIVYRDLKPENILld 295
Cdd:cd05092  77 TEGEPLIMVFEYMRHGDLnrFLrsHGPDAKILDGGEGQAPgqltlgqmlqiASQIASGMVYLASLHFVHRDLATRNCL-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 296 sVGH---VVLTDFGLCKEgiaISDTTTTFCG----TP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDV 366
Cdd:cd05092 155 -VGQglvVKIGDFGMSRD---IYSTDYYRVGgrtmLPiRWMPPESILYRKFTTESDIWSFGVVLWEIFtYGKQPWYQLSN 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 75813626 367 AEMYDNI-----LHKPLSLRPGVsltaWSILEELLEKDRQNRLGAKE 408
Cdd:cd05092 231 TEAIECItqgreLERPRTCPPEV----YAIMQGCWQREPQQRHSIKD 273
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
166-361 3.22e-10

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: 60.99  E-value: 3.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLDGKFYAVKVLqkkivLNRKEQKH--IMAERNVLLKNVKHPFLVGLHYSFQTTEKL------- 236
Cdd:cd14036   6 RVIAEGGFAFVYEAQDVGTGKEYALKRL-----LSNEEEKNkaIIQEINFMKKLSGHPNIVQFCSAASIGKEEsdqgqae 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQRERS----FPEHRAR-FYaaEIASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFGLC- 308
Cdd:cd14036  81 YLLLTELCKGQLVDFVKKVEApgpfSPDTVLKiFY--QTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSAt 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 309 -------------KEGIAISDTTTTfcGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14036 159 teahypdyswsaqKRSLVEDEITRN--TTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPF 225
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
166-375 3.59e-10

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 60.63  E-value: 3.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKL-DGKFYAVKVLQKKI-VLNRKEQKHIMAErNVLLKNVKHPF---LVGLHYSFQTTEKL---Y 237
Cdd:cd05035   5 KILGEGEFGSVMEAQLKQdDGSQLKVAVKTMKVdIHTYSEIEEFLSE-AACMKDFDHPNvmrLIGVCFTASDLNKPpspM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRER------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEg 311
Cdd:cd05035  84 VILPFMKHGDLHSYLLYSRlgglpeKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRK- 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 312 IAISDTTTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYDNILH 375
Cdd:cd05035 163 IYSGDYYRQGRISKmpvKWIALESLADNVYTSKSDVWSFGVTMWEIAtRGQTPYPGVENHEIYDYLRN 230
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
156-408 3.84e-10

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 60.79  E-value: 3.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 156 HAKPTDFDFLKVIGKGSFGKVLLAK-----RKLDGKFYAVKVLQKKIVLNRKEqkhiMAERNVLLKNVKHPFLVGLHYSF 230
Cdd:cd05094   1 HIKRRDIVLKRELGEGAFGKVFLAEcynlsPTKDKMLVAVKTLKDPTLAARKD----FQREAELLTNLQHDHIVKFYGVC 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 231 QTTEKLYFVLDFVNGGEL--FFH--------------LQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILL 294
Cdd:cd05094  77 GDGDPLIMVFEYMKHGDLnkFLRahgpdamilvdgqpRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 295 DSVGHVVLTDFGLCKEgIAISDTTTTFCGTP---EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMY 370
Cdd:cd05094 157 GANLLVKIGDFGMSRD-VYSTDYYRVGGHTMlpiRWMPPESIMYRKFTTESDVWSFGVILWEIFtYGKQPWFQLSNTEVI 235
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 75813626 371 DNILHKPLSLRPGV-SLTAWSILEELLEKDRQNRLGAKE 408
Cdd:cd05094 236 ECITQGRVLERPRVcPKEVYDIMLGCWQREPQQRLNIKE 274
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
165-362 4.33e-10

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 60.56  E-value: 4.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRK-----LDGKFYAVKVLQKkivlnRKEQKHIMAERNVL--LKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd05046  10 ITTLGRGEFGEVFLAKAKgieeeGGETLVLVKALQK-----TKDENLQSEFRRELdmFRKLSHKNVVRLLGLCREAEPHY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRERSF----------PEHRARFyAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGL 307
Cdd:cd05046  85 MILEYTDLGDLKQFLRATKSKdeklkppplsTKQKVAL-CTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSL 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 308 CKEgiAISDTTTTFCGT--P-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFY 362
Cdd:cd05046 164 SKD--VYNSEYYKLRNAliPlRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFtQGELPFY 220
PX_SNX8_Mvp1p_like cd06866
The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX ...
26-117 4.88e-10

The phosphoinositide binding Phox Homology domain of Sorting Nexin 8 and yeast Mvp1p; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX8 and the yeast counterpart Mvp1p are involved in sorting and delivery of late-Golgi proteins, such as carboxypeptidase Y, to vacuoles.


Pssm-ID: 132776  Cd Length: 105  Bit Score: 56.47  E-value: 4.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  26 EKKKRF---TVYKVLVSVGRSEwfVFRRYAEFDKLYNTLKKQFP-AMALKIPAKRIFGDNfDPDFIKQRRAGLNEFIQNL 101
Cdd:cd06866  10 EKKGLFlkhVEYEVSSKRFKST--VYRRYSDFVWLHEYLLKRYPyRMVPALPPKRIGGSA-DREFLEARRRGLSRFLNLV 86
                        90
                ....*....|....*.
gi 75813626 102 VRYPELYNHPDVRAFL 117
Cdd:cd06866  87 ARHPVLSEDELVRTFL 102
PX_SNX10 cd06898
The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a ...
25-118 5.48e-10

The phosphoinositide binding Phox Homology domain of Sorting Nexin 10; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. Some SNXs are localized in early endosome structures such as clathrin-coated pits, while others are located in late structures of the endocytic pathway. SNX10 may be involved in the regulation of endosome homeostasis. Its expression induces the formation of giant vacuoles in mammalian cells.


Pssm-ID: 132808  Cd Length: 113  Bit Score: 56.57  E-value: 5.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  25 REKKKRFTVYKVLV-----SVGRSEWFVFRRYAEFDKLYNTLKK-----QFPamalKIPAKRIFGDNFDPDFIKQRRAGL 94
Cdd:cd06898  12 EDDWGSYTDYEIFLhtnsmCFTLKTSCVRRRYSEFVWLRNRLQKnalliQLP----SLPPKNLFGRFNNEGFIEERQQGL 87
                        90       100
                ....*....|....*....|....
gi 75813626  95 NEFIQNLVRYPELYNHPDVRAFLQ 118
Cdd:cd06898  88 QDFLEKVLQTPLLLSDSRLHLFLQ 111
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
166-355 6.96e-10

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 60.08  E-value: 6.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKRKLD--GKF--YAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHpFLVGLHYSFQTTEKLYFVLD 241
Cdd:cd14055   1 KLVGKGRFAEVWKAKLKQNasGQYetVAVKIFPYEEYASWKNEKDIFTDASLKHENILQ-FLTAEERGVGLDRQYWLITA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 242 FVNGGELFFHLQReRSFPEHRARFYAAEIASALGYLHS---------IKIVYRDLKPENILLDSVGHVVLTDFGLckeGI 312
Cdd:cd14055  80 YHENGSLQDYLTR-HILSWEDLCKMAGSLARGLAHLHSdrtpcgrpkIPIAHRDLKSSNILVKNDGTCVLADFGL---AL 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 313 AISDTTTT-------FCGTPEYLAPEVIR-----------KQpydntVDWWCLGAVLYEML 355
Cdd:cd14055 156 RLDPSLSVdelansgQVGTARYMAPEALEsrvnledlesfKQ-----IDVYSMALVLWEMA 211
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
162-374 7.13e-10

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: 60.41  E-value: 7.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 162 FDFLKVIGKGSFGKVLLAKRKLDGKF-YAVKVLQKKIVLNRKEQKHIMAERNVLLKNVKHPFLVGLH---YSFQTTEKLY 237
Cdd:cd14214  15 YEIVGDLGEGTFGKVVECLDHARGKSqVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMsdwFNFHGHMCIA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDfvngGELFFHLQRERSF---PEHRARFYAAEIASALGYLHSIKIVYRDLKPENIL-LDSVGHVVLTDFGLCKE--- 310
Cdd:cd14214  95 FELL----GKNTFEFLKENNFqpyPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILfVNSEFDTLYNESKSCEEksv 170
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75813626 311 ----------GIAISDTT--TTFCGTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEMLYGLPPFYCRDVAE---MYDNIL 374
Cdd:cd14214 171 kntsirvadfGSATFDHEhhTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREhlvMMEKIL 249
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
163-295 7.49e-10

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 59.72  E-value: 7.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 163 DFLKV--IGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQkhiMAERNVLLKNV--KHPFLVGLHYSFQTTEKLYF 238
Cdd:cd14051   1 EFHEVekIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQ---NALNEVYAHAVlgKHPHVVRYYSAWAEDDHMII 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75813626 239 VLDFVNGGELFFHLQRE----RSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLD 295
Cdd:cd14051  78 QNEYCNGGSLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFIS 138
PX_SNX1 cd07281
The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a ...
15-120 7.76e-10

The phosphoinositide binding Phox Homology domain of Sorting Nexin 1; The PX domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds PIs and targets the protein to PI-enriched membranes. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway. SNX1 is both membrane associated and a cytosolic protein that exists as a tetramer in protein complexes. It can associate reversibly with membranes of the endosomal compartment, thereby coating these vesicles. SNX1 is a component of the retromer complex, a membrane coat multimeric complex required for endosomal retrieval of lysosomal hydrolase receptors to the Golgi. The retromer consists of a cargo-recognition subcomplex and a subcomplex formed by a dimer of sorting nexins (SNX1 and/or SNX2), which ensures efficient cargo sorting by facilitating proper membrane localization of the cargo-recognition subcomplex. SNX1 contains a Bin/Amphiphysin/Rvs (BAR) domain C-terminal to the PX domain. The PX domain of SNX1 specifically binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,5)P2, while the BAR domain detects membrane curvature. Both domains help determine the specific membrane-targeting of SNX1, which is localized to a microdomain in early endosomes where it regulates cation-independent mannose-6-phosphate receptor retrieval to the trans Golgi network.


Pssm-ID: 132814  Cd Length: 124  Bit Score: 56.61  E-value: 7.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  15 SVSIPSSDEHREKKKRFTVYKVL----VSVGRSEWF-VFRRYAEFDKLYNTLKKQFPAMALKI---PAKRIFG------- 79
Cdd:cd07281   2 KVSITDPEKIGDGMNAYVVYKVTtqtsLLMFRSKHFtVKRRFSDFLGLYEKLSEKHSQNGFIVpppPEKSLIGmtkvkvg 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 75813626  80 --DNFDPDFIKQRRAGLNEFIQNLVRYPELYNHPDVRAFLQMD 120
Cdd:cd07281  82 keDSSSAEFLERRRAALERYLQRIVSHPSLLQDPDVREFLEKE 124
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
165-361 8.37e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 59.93  E-value: 8.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 165 LKVIGKGSFGKVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTEKLYFVLDFVN 244
Cdd:cd14026   2 LRYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHK-ARFSYILPILGICNEPEFLGIVTEYMT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 245 GGELFFHLQRERSFPE----HRARFYAaEIASALGYLHSIK--IVYRDLKPENILLDSVGHVVLTDFGLCK-EGIAIS-- 315
Cdd:cd14026  81 NGSLNELLHEKDIYPDvawpLRLRILY-EIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwRQLSISqs 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75813626 316 --DTTTTFCGTPEYLAPEVI---RKQPYDNTVDWWCLGAVLYEMLYGLPPF 361
Cdd:cd14026 160 rsSKSAPEGGTIIYMPPEEYepsQKRRASVKHDIYSYAIIMWEVLSRKIPF 210
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
158-371 9.29e-10

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 59.58  E-value: 9.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 158 KPTDFDFLKVIGKGSFGKVLLAKRKLDGKFYAVKVlQKKIVLNRKEQK--HIMAERNVLLKNVKHPFLVGLhYSFQTTEK 235
Cdd:cd05111   5 KETELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPV-AIKVIQDRSGRQsfQAVTDHMLAIGSLDHAYIVRL-LGICPGAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 236 LYFVLDFVNGGELFFHLQRER-SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKegIAI 314
Cdd:cd05111  83 LQLVTQLLPLGSLLDHVRQHRgSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVAD--LLY 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75813626 315 SDTTTTF---CGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPFYCRDVAEMYD 371
Cdd:cd05111 161 PDDKKYFyseAKTPiKWMALESIHFGKYTHQSDVWSYGVTVWEMMtFGAEPYAGMRLAEVPD 222
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
168-357 1.00e-09

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 59.93  E-value: 1.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 168 IGKGSFGKVLLAK-RKLDGKFYAVKVL----------QKKIVLNRK-------EQKHIMA-ERNVLLKNvkHPFLV--GL 226
Cdd:cd14135   8 LGKGVFSNVVRARdLARGNQEVAIKIIrnnelmhkagLKELEILKKlndadpdDKKHCIRlLRHFEHKN--HLCLVfeSL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 227 HYSFQTTEKLYfvldfvnGGELFFHLQRERSfpehrarfYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVV-LTDF 305
Cdd:cd14135  86 SMNLREVLKKY-------GKNVGLNIKAVRS--------YAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTLkLCDF 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 306 GlckEGIAISDTTTTfcgtpEYL------APEVIRKQPYDNTVDWWCLGAVLYEMLYG 357
Cdd:cd14135 151 G---SASDIGENEIT-----PYLvsrfyrAPEIILGLPYDYPIDMWSVGCTLYELYTG 200
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
159-375 1.08e-09

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: 59.08  E-value: 1.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 159 PTD-FDFLKVIGKGSFGKVLLAkrkLDGKFYAVKVLQKKIVLNRKEQKHIMAERNvLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd14112   1 PTGrFSFGSEIFRGRFSVIVKA---VDSTTETDAHCAVKIFEVSDEASEAVREFE-SLRTLQHENVQRLIAAFKPSNFAY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGgELFFHLQRERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVV--LTDFG----LCKEG 311
Cdd:cd14112  77 LVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQvkLVDFGraqkVSKLG 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 312 IAISDTTTTFcGTPEYLAPEvirkQPYDNTVDWWCLGAVLYEMLYGLPPFY--CRDVAEMYDNILH 375
Cdd:cd14112 156 KVPVDGDTDW-ASPEFHNPE----TPITVQSDIWGLGVLTFCLLSGFHPFTseYDDEEETKENVIF 216
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
164-361 1.34e-09

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: 59.42  E-value: 1.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 164 FLKVIGKGSFGKVL------LAKRKLDGKFyAVKVLQKKIvlNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTEKLY 237
Cdd:cd05055  39 FGKTLGAGAFGKVVeataygLSKSDAVMKV-AVKMLKPTA--HSSEREALMSELKIMSHLGNHENIVNLLGACTIGGPIL 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRER-SFPEHRARF-YAAEIASALGYLHSIKIVYRDLKPENILLDSvGHVV-LTDFGLCKEgiAI 314
Cdd:cd05055 116 VITEYCCYGDLLNFLRRKReSFLTLEDLLsFSYQVAKGMAFLASKNCIHRDLAARNVLLTH-GKIVkICDFGLARD--IM 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75813626 315 SDTTTTFCGTP----EYLAPEVIRKQPYDNTVDWWCLGAVLYEML-YGLPPF 361
Cdd:cd05055 193 NDSNYVVKGNArlpvKWMAPESIFNCVYTFESDVWSYGILLWEIFsLGSNPY 244
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
247-353 1.35e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 60.29  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  247 ELFFHLQReRSFPEHRARFYAA--EIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFG-LC-KEGIAISDTTTTFC 322
Cdd:PHA03211 245 DLYTYLGA-RLRPLGLAQVTAVarQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGaACfARGSWSTPFHYGIA 323
                         90       100       110
                 ....*....|....*....|....*....|.
gi 75813626  323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYE 353
Cdd:PHA03211 324 GTVDTNAPEVLAGDPYTPSVDIWSAGLVIFE 354
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
166-355 1.36e-09

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: 59.26  E-value: 1.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAKrkLDGKFYAVKVLqkkivlNRKEQKHIMAERNVL-LKNVKHPFLVGLHYSFQTTEKLY----FVL 240
Cdd:cd14053   1 EIKARGRFGAVWKAQ--YLNRLVAVKIF------PLQEKQSWLTEREIYsLPGMKHENILQFIGAEKHGESLEaeywLIT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 241 DFVNGGELFFHL-QRERSFPEhrARFYAAEIASALGYLHS--------IK--IVYRDLKPENILLDSVGHVVLTDFGLC- 308
Cdd:cd14053  73 EFHERGSLCDYLkGNVISWNE--LCKIAESMARGLAYLHEdipatnggHKpsIAHRDFKSKNVLLKSDLTACIADFGLAl 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75813626 309 --KEGIAISDTTTTFcGTPEYLAPEVI------RKQPYdNTVDWWCLGAVLYEML 355
Cdd:cd14053 151 kfEPGKSCGDTHGQV-GTRRYMAPEVLegainfTRDAF-LRIDMYAMGLVLWELL 203
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
175-355 1.78e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 60.09  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  175 KVLLAKRKLDGKFYAVKVLQKKIVLNRKEQKHIMAERNVLlknvKHPflvglHYSFQTTEKLYFVL-DFVNGGELffhlQ 253
Cdd:PHA03210 193 ERLIAKRVKAGSRAAIQLENEILALGRLNHENILKIEEIL----RSE-----ANTYMITQKYDFDLySFMYDEAF----D 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626  254 RERSFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGlckegiaisdTTTTF-----------C 322
Cdd:PHA03210 260 WKDRPLLKQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFG----------TAMPFekereafdygwV 329
                        170       180       190
                 ....*....|....*....|....*....|...
gi 75813626  323 GTPEYLAPEVIRKQPYDNTVDWWCLGAVLYEML 355
Cdd:PHA03210 330 GTVATNSPEILAGDGYCEITDIWSCGLILLDML 362
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
167-354 2.04e-09

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 58.61  E-value: 2.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 167 VIGKGSFGKVLLAKRKldGKFYAVKvlqkkIVLNRKE----------QKHIMAERNVLlknvkhPFLVGLHYSFQTTEKL 236
Cdd:cd14143   2 SIGKGRFGEVWRGRWR--GEDVAVK-----IFSSREErswfreaeiyQTVMLRHENIL------GFIAADNKDNGTWTQL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 237 YFVLDFVNGGELFFHLQRERSFPEHRARFyAAEIASALGYLH--------SIKIVYRDLKPENILLDSVGHVVLTDFGLC 308
Cdd:cd14143  69 WLVSDYHEHGSLFDYLNRYTVTVEGMIKL-ALSIASGLAHLHmeivgtqgKPAIAHRDLKSKNILVKKNGTCCIADLGLA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75813626 309 KEGIAISDT----TTTFCGTPEYLAPEV----IRKQPYDN--TVDWWCLGAVLYEM 354
Cdd:cd14143 148 VRHDSATDTidiaPNHRVGTKRYMAPEVlddtINMKHFESfkRADIYALGLVFWEI 203
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
166-375 2.07e-09

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 58.41  E-value: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 166 KVIGKGSFGKVLLAK-RKLDGKFYAVKVlqKKIVLNRKEQKHI--MAERNVLLKNVKHPFL-----VGLHYSFQTTEKLY 237
Cdd:cd14204  13 KVLGEGEFGSVMEGElQQPDGTNHKVAV--KTMKLDNFSQREIeeFLSEAACMKDFNHPNVirllgVCLEVGSQRIPKPM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 238 FVLDFVNGGELFFHLQRER------SFPEHRARFYAAEIASALGYLHSIKIVYRDLKPENILLDSVGHVVLTDFGLCKEg 311
Cdd:cd14204  91 VILPFMKYGDLHSFLLRSRlgsgpqHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKK- 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75813626 312 IAISD--TTTTFCGTP-EYLAPEVIRKQPYDNTVDWWCLGAVLYEM-LYGLPPFYCRDVAEMYDNILH 375
Cdd:cd14204 170 IYSGDyyRQGRIAKMPvKWIAVESLADRVYTVKSDVWAFGVTMWEIaTRGMTPYPGVQNHEIYDYLLH 237
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
260-419 2.17e-09

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 58.12  E-value: 2.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 260 EHRAR-FYaaEIASALGYLHSIKIVYRDLKPENILLDS-----VGHVVLTD-FGLCKEGIAISDTTttfcGTPEYLAPEV 332
Cdd:cd14022  84 EEAARlFY--QIASAVAHCHDGGLVLRDLKLRKFVFKDeertrVKLESLEDaYILRGHDDSLSDKH----GCPAYVSPEI 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75813626 333 IRKQ-PYD-NTVDWWCLGAVLYEMLYGLPPFYCRDVAEMYDNILHKPLSLRPGVSLTAWSILEELLEKDRQNRLGAKedf 410
Cdd:cd14022 158 LNTSgSYSgKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSERLTSQ--- 234

                ....*....
gi 75813626 411 lEIQNHPFF 419
Cdd:cd14022 235 -EILDHPWF 242
 
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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