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Conserved domains on  [gi|66932916|ref|NP_002736|]
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mitogen-activated protein kinase 1 [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
19-353 0e+00

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: 723.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  19 FDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQM 98
Cdd:cd07849   1 FDVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPTFESF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  99 KDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH 178
Cdd:cd07849  81 KDVYIVQELMETDLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 179 DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINL 258
Cdd:cd07849 161 DHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEDLNCIISL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 259 KARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMEL-DD 337
Cdd:cd07849 241 KARNYIKSLPFKPKVPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFDMELfDD 320
                       330
                ....*....|....*.
gi 66932916 338 LPKEKLKELIFEETAR 353
Cdd:cd07849 321 LPKEKLKELIFEEIMR 336
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-313 1.76e-89

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 272.10  E-value: 1.76e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916     25 YTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTieqmkDVYIV 104
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDED-----KLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916    105 QDLMET-DLYKLLKTQ-HLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPdhdhTG 182
Cdd:smart00220  76 MEYCEGgDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP----GE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916    183 FLTEYVATRWYRAPEImLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKhylDQLNHILGILGSPsqedlnciinlkarn 262
Cdd:smart00220 152 KLTTFVGTPEYMAPEV-LLGKGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKP--------------- 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 66932916    263 yllslphknKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYL 313
Cdd:smart00220 213 ---------KPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
 
Name Accession Description Interval E-value
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
19-353 0e+00

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: 723.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  19 FDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQM 98
Cdd:cd07849   1 FDVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPTFESF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  99 KDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH 178
Cdd:cd07849  81 KDVYIVQELMETDLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 179 DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINL 258
Cdd:cd07849 161 DHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEDLNCIISL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 259 KARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMEL-DD 337
Cdd:cd07849 241 KARNYIKSLPFKPKVPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFDMELfDD 320
                       330
                ....*....|....*.
gi 66932916 338 LPKEKLKELIFEETAR 353
Cdd:cd07849 321 LPKEKLKELIFEEIMR 336
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-313 1.76e-89

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 272.10  E-value: 1.76e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916     25 YTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTieqmkDVYIV 104
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDED-----KLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916    105 QDLMET-DLYKLLKTQ-HLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPdhdhTG 182
Cdd:smart00220  76 MEYCEGgDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDP----GE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916    183 FLTEYVATRWYRAPEImLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKhylDQLNHILGILGSPsqedlnciinlkarn 262
Cdd:smart00220 152 KLTTFVGTPEYMAPEV-LLGKGYGKAVDIWSLGVILYELLTGKPPFPGD---DQLLELFKKIGKP--------------- 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 66932916    263 yllslphknKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYL 313
Cdd:smart00220 213 ---------KPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
25-313 6.35e-75

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 234.41  E-value: 6.35e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916    25 YTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPfEHQT--YCQRTLREIKILLRFRHENIIGINDIIRAPtieqmKDVY 102
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAVKKIKK-EKIKkkKDKNVLREIKILKKLNHPNIVRLYDVFEDK-----DHLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916   103 IVQDLME-TDLYKLLKTQ-HLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDhdh 180
Cdd:pfam00069  75 LVLEYVEgGSLFDLLSEKgAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLAKQLSSG--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916   181 tGFLTEYVATRWYRAPEImLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILgilgspsqedlnciinlka 260
Cdd:pfam00069 152 -SKLTTFVGTPWYMAPEV-LRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGDTLYELII------------------- 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 66932916   261 RNYLLSLPHKNKVPwnrlfpnadSKALDLLDKMLTFNPHKRIEVEQALAHPYL 313
Cdd:pfam00069 211 DQLDLSSPRPSSIS---------EEAKDLLKKLLKKDPSKRLTATQALQHPWF 254
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
19-331 1.20e-68

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 221.17  E-value: 1.20e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916   19 FDVGPRYTNL-SYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQR-------------TLREIKILLRFRHENII 84
Cdd:PTZ00024   4 FSISERYIQKgAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKdrqlvgmcgihftTLRELKIMNEIKHENIM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916   85 GINDIIraptIEQmKDVYIVQDLMETDLYKLLKTQ-HLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDL 163
Cdd:PTZ00024  84 GLVDVY----VEG-DFINLVMDIMASDLKKVVDRKiRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGIC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  164 KICDFGLAR--VADPDHDHTGF---------LTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKH 232
Cdd:PTZ00024 159 KIADFGLARryGYPPYSDTLSKdetmqrreeMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGEN 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  233 YLDQLNHILGILGSPSQEDLNciinlKARNYLLSLP--HKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAH 310
Cdd:PTZ00024 239 EIDQLGRIFELLGTPNEDNWP-----QAKKLPLYTEftPRKPKDLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKH 313
                        330       340
                 ....*....|....*....|.
gi 66932916  311 PYLEQYYDPSDepIAEAPFKF 331
Cdd:PTZ00024 314 EYFKSDPLPCD--PSQLPFNF 332
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
25-360 3.88e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 165.69  E-value: 3.88e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  25 YTNLSYIGEGAYGMVCSAYDNVnkvRVAIKKISP--FEHQTYCQRTLREIKILLRFRHE-NIIGINDIIRaptiEQMKDV 101
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRK---LVALKVLAKklESKSKEVERFLREIQILASLNHPpNIVKLYDFFQ----DEGSLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 102 YIVQDLMETDLYKLLKTQH----LSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLN-TTCDLKICDFGLARVADP 176
Cdd:COG0515  75 LVMEYVDGGSLEDLLKKIGrkgpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAKLLPD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 177 DHDHTG---FLTEYVATRWYRAPEIMLNSKG--YTKSIDIWSVGCILAEMLSNRPIFPGKHyldqlnhilgilGSPSQED 251
Cdd:COG0515 155 PGSTSSipaLPSTSVGTPGYMAPEVLLGLSLayASSSSDIWSLGITLYELLTGLPPFEGEK------------NSSATSQ 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 252 LNCIInlkarnYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKF 331
Cdd:COG0515 223 TLKII------LELPTPSLASPLSPSNPELISKAASDLLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDD 296
                       330       340
                ....*....|....*....|....*....
gi 66932916 332 DMELDDLPKEKLKELIFEETARFQPGYRS 360
Cdd:COG0515 297 SAPLRLSLPPSLEALISSLNSLAISGSDL 325
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
50-230 3.66e-12

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 66.41  E-value: 3.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916     50 RVAIK--KISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTieqmKDVYIVQDLME-TDLYKLLKTQH-LSNDH 125
Cdd:TIGR03903    5 EVAIKllRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPP----GLLFAVFEYVPgRTLREVLAADGaLPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916    126 ICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCD---LKICDFGLAR----VADPDHDHTGFLTEYVATRWYRAPEi 198
Cdd:TIGR03903   81 TGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVrphAKVLDFGIGTllpgVRDADVATLTRTTEVLGTPTYCAPE- 159
                          170       180       190
                   ....*....|....*....|....*....|..
gi 66932916    199 MLNSKGYTKSIDIWSVGCILAEMLSNRPIFPG 230
Cdd:TIGR03903  160 QLRGEPVTPNSDLYAWGLIFLECLTGQRVVQG 191
 
Name Accession Description Interval E-value
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
19-353 0e+00

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: 723.32  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  19 FDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQM 98
Cdd:cd07849   1 FDVGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQRPPTFESF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  99 KDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH 178
Cdd:cd07849  81 KDVYIVQELMETDLYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEH 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 179 DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINL 258
Cdd:cd07849 161 DHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEDLNCIISL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 259 KARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMEL-DD 337
Cdd:cd07849 241 KARNYIKSLPFKPKVPWNKLFPNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFDMELfDD 320
                       330
                ....*....|....*.
gi 66932916 338 LPKEKLKELIFEETAR 353
Cdd:cd07849 321 LPKEKLKELIFEEIMR 336
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
24-350 0e+00

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: 562.92  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  24 RYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKIS-PFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVY 102
Cdd:cd07834   1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISnVFDDLIDAKRILREIKILRHLKHENIIGLLDILRPPSPEEFNDVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 103 IVQDLMETDLYKLLKT-QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDhT 181
Cdd:cd07834  81 IVTELMETDLHKVIKSpQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDED-K 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 182 GFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKAR 261
Cdd:cd07834 160 GFLTEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEDLKFISSEKAR 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 262 NYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKF-DMELDDLPK 340
Cdd:cd07834 240 NYLKSLPKKPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPEDEPVAKPPFDFpFFDDEELTI 319
                       330
                ....*....|
gi 66932916 341 EKLKELIFEE 350
Cdd:cd07834 320 EELKELIYEE 329
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
19-356 2.91e-170

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: 481.10  E-value: 2.91e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  19 FDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKIS-PFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQ 97
Cdd:cd07858   1 FEVDTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIAnAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHREA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  98 MKDVYIVQDLMETDLYKLLK-TQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADP 176
Cdd:cd07858  81 FNDVYIVYELMDTDLHQIIRsSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 177 DHDhtgFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCII 256
Cdd:cd07858 161 KGD---FMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDLGFIR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 257 NLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELD 336
Cdd:cd07858 238 NEKARRYIRSLPYTPRQSFARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVCQTPFSFDFEED 317
                       330       340
                ....*....|....*....|
gi 66932916 337 DLPKEKLKELIFEETARFQP 356
Cdd:cd07858 318 ALTEEDIKELIYNEMLAYHP 337
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
19-350 5.54e-161

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: 457.60  E-value: 5.54e-161
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  19 FDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKIS-PFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAP-TIE 96
Cdd:cd07855   1 FDVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPnAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKvPYA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  97 QMKDVYIVQDLMETDLYKLLKT-QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVAD 175
Cdd:cd07855  81 DFKDVYVVLDLMESDLHHIIHSdQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGLC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 176 PDH-DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNC 254
Cdd:cd07855 161 TSPeEHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVINA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 255 IINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDME 334
Cdd:cd07855 241 IGADRVRRYIQNLPNKQPVPWETLYPKADQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPDDEPDCAPPFDFDFD 320
                       330
                ....*....|....*.
gi 66932916 335 LDDLPKEKLKELIFEE 350
Cdd:cd07855 321 AEALTREALKEAIVNE 336
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
18-356 3.40e-149

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: 427.87  E-value: 3.40e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  18 VFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKIS-PFEHQTYCQRTLREIKILLRFRHENIIGINDII-RAPTI 95
Cdd:cd07851  10 VWEVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSrPFQSAIHAKRTYRELRLLKHMDHENVIGLLDVFtPASSL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  96 EQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVAD 175
Cdd:cd07851  90 EDFQDVYLVTHLMGADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNIAVNEDCELKILDFGLARHTD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 176 PDhdhtgfLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCI 255
Cdd:cd07851 170 DE------MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDEELLQKI 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 256 INLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEaPFKFDMEL 335
Cdd:cd07851 244 SSESARNYIQSLPQMPKKDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPEDEPVAP-PYDQSFES 322
                       330       340
                ....*....|....*....|.
gi 66932916 336 DDLPKEKLKELIFEETARFQP 356
Cdd:cd07851 323 RDLTVDEWKELVYKEIMNFKP 343
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
24-350 4.52e-139

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: 401.78  E-value: 4.52e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  24 RYTNLSYIGEGAYGMVCSAYD--NVNKVRVAIKKISP-FEHQTYCQRTLREIKILLRFR-HENIIGINDIiRAPTIEQMK 99
Cdd:cd07857   1 RYELIKELGQGAYGIVCSARNaeTSEEETVAIKKITNvFSKKILAKRALRELKLLRHFRgHKNITCLYDM-DIVFPGNFN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 100 DVYIVQDLMETDLYKLLKT-QHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDH 178
Cdd:cd07857  80 ELYLYEELMEADLHQIIRSgQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSENP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 179 -DHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIIN 257
Cdd:cd07857 160 gENAGFMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDEETLSRIGS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 258 LKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDD 337
Cdd:cd07857 240 PKAQNYIRSLPNIPKKPFESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDPDDEPVCQKPFDFSFESED 319
                       330
                ....*....|...
gi 66932916 338 lPKEKLKELIFEE 350
Cdd:cd07857 320 -SMEELRDMIIEE 331
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
24-350 9.02e-132

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: 383.06  E-value: 9.02e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  24 RYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKI-SPFEHQTYCQRTLREIKILLRFR-HENIIGINDIIRAptiEQMKDV 101
Cdd:cd07852   8 RYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfDAFRNATDAQRTFREIMFLQELNdHPNIIKLLNVIRA---ENDKDI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 102 YIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLAR--VADPDHD 179
Cdd:cd07852  85 YLVFEYMETDLHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARslSQLEEDD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 180 HTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLK 259
Cdd:cd07852 165 ENPVLTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIGRPSAEDIESIQSPF 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 260 ARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKfdMELDD-- 337
Cdd:cd07852 245 AATMLESLPPSRPKSLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQFHNPADEPSLPGPIV--IPLDDnk 322
                       330
                ....*....|....
gi 66932916 338 -LPKEKLKELIFEE 350
Cdd:cd07852 323 kLTVDEYRNRLYEE 336
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
18-356 4.82e-129

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: 376.69  E-value: 4.82e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  18 VFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKIS-PFEHQTYCQRTLREIKILLRFRHENIIGINDIIR-APTI 95
Cdd:cd07877  12 IWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSrPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTpARSL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  96 EQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVAD 175
Cdd:cd07877  92 EEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTD 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 176 PDhdhtgfLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCI 255
Cdd:cd07877 172 DE------MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 256 INLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEaPFKFDMEL 335
Cdd:cd07877 246 SSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVAD-PYDQSFES 324
                       330       340
                ....*....|....*....|.
gi 66932916 336 DDLPKEKLKELIFEETARFQP 356
Cdd:cd07877 325 RDLLIDEWKSLTYDEVISFVP 345
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
14-350 5.53e-129

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: 375.76  E-value: 5.53e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  14 VRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKI-SPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRA 92
Cdd:cd07856   1 IFGTVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKImKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFIS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  93 PtieqMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLAR 172
Cdd:cd07856  81 P----LEDIYFVTELLGTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLAR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 173 VADPDhdhtgfLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDL 252
Cdd:cd07856 157 IQDPQ------MTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 253 NCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFD 332
Cdd:cd07856 231 NTICSENTLRFVQSLPKRERVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHDPTDEPVADEKFDWS 310
                       330
                ....*....|....*...
gi 66932916 333 MELDDLPKEKLKELIFEE 350
Cdd:cd07856 311 FNDADLPVDTWKVMMYSE 328
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
18-356 6.71e-127

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: 370.92  E-value: 6.71e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  18 VFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKIS-PFEHQTYCQRTLREIKILLRFRHENIIGINDIIR-APTI 95
Cdd:cd07878  10 VWEVPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLSrPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTpATSI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916  96 EQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVAD 175
Cdd:cd07878  90 ENFNEVYLVTNLMGADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQAD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 176 PDhdhtgfLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCI 255
Cdd:cd07878 170 DE------MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKI 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66932916 256 INLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEaPFKFDMEL 335
Cdd:cd07878 244 SSEH</