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Conserved domains on  [gi|21219970|ref|NP_625749.1|]
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Ser/Thr protein kinase [Streptomyces coelicolor A3(2)]

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
130-375 5.60e-36

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: 136.95  E-value: 5.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDTRvPGLHVVLKGLI--NTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEP 207
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL-LGRPVAIKVLRpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGED------DG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 208 TGYIVMEYVGGRSLSwirfapeEELARLfgtGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVID 286
Cdd:cd14014  74 RPYIVMEYVEGGSLA-------DLLRER---GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIlLTEDGRVKLTD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 287 LGAIRRIDD----RSSGLVHTHGYAPPKRERDRRgLDVDSDLYTVGRTL--------------------KVLAERAARPA 342
Cdd:cd14014 144 FGIARALGDsgltQTGSVLGTPAYMAPEQARGGP-VDPRSDIYSLGVVLyelltgrppfdgdspaavlaKHLQEAPPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21219970 343 GLAAR---SFEALIRRATHPEPAARFRSAAEMSRQL 375
Cdd:cd14014 223 PLNPDvppALDAIILRALAKDPEERPQSAAELLAAL 258
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
130-375 5.60e-36

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: 136.95  E-value: 5.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDTRvPGLHVVLKGLI--NTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEP 207
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL-LGRPVAIKVLRpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGED------DG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 208 TGYIVMEYVGGRSLSwirfapeEELARLfgtGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVID 286
Cdd:cd14014  74 RPYIVMEYVEGGSLA-------DLLRER---GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIlLTEDGRVKLTD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 287 LGAIRRIDD----RSSGLVHTHGYAPPKRERDRRgLDVDSDLYTVGRTL--------------------KVLAERAARPA 342
Cdd:cd14014 144 FGIARALGDsgltQTGSVLGTPAYMAPEQARGGP-VDPRSDIYSLGVVLyelltgrppfdgdspaavlaKHLQEAPPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21219970 343 GLAAR---SFEALIRRATHPEPAARFRSAAEMSRQL 375
Cdd:cd14014 223 PLNPDvppALDAIILRALAKDPEERPQSAAELLAAL 258
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
211-288 9.61e-03

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 36.81  E-value: 9.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21219970  211 IVMEYVGGRSLSWIRFAPEEELARLFGTGGfefghvitygcKILGALeylHDRGLLYCDMKPENVIHYGREIKVIDLG 288
Cdd:PRK14879  76 IVMEYIEGEPLKDLINSNGMEELELSREIG-----------RLVGKL---HSAGIIHGDLTTSNMILSGGKIYLIDFG 139
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
131-328 3.47e-22

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 96.83  E-value: 3.47e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970    131 YAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEPTGY 210
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARD-KKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFED------EDKLY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970    211 IVMEYVGGRSLSWIrfapeeelarLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLGA 289
Cdd:smart00220  74 LVMEYCEGGDLFDL----------LKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIlLDEDGHVKLADFGL 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 21219970    290 IRRIDD--RSSGLVHTHGYAPPkrER-DRRGLDVDSDLYTVG 328
Cdd:smart00220 144 ARQLDPgeKLTTFVGTPEYMAP--EVlLGKGYGKAVDIWSLG 183
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
130-331 1.51e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 96.35  E-value: 1.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDTRVPGLHVVLKGLINTGDAVARraAVEERRSLTTL-HHRDIVRIVTHVQHqvpgdaEPT 208
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDRKLVALKVLAKKLESKSKEVER--FLREIQILASLnHPPNIVKLYDFFQD------EGS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 209 GYIVMEYVGGRSLSWIrfapeeeLARLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGREIKVID 286
Cdd:COG0515  73 LYLVMEYVDGGSLEDL-------LKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILldRDGRVVKLID 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21219970 287 LGAIRRIDD---------RSSGLVHTHGYAPPKRERDRRGLDVD--SDLYTVGRTL 331
Cdd:COG0515 146 FGLAKLLPDpgstssipaLPSTSVGTPGYMAPEVLLGLSLAYASssSDIWSLGITL 201
Pkinase pfam00069
Protein kinase domain;
131-328 3.39e-19

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 87.69  E-value: 3.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970   131 YAVLGYLAVGGHGWVYLAEDTRVPGLhVVLKGLINTG-DAVARRAAVEERRSLTTLHHRDIVRIV-THVQHQVPgdaept 208
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGTGKI-VAVKILKKRSeKSKKDQTARREIRILRRLSHPNIVRLIdAFEDKDHL------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970   209 gYIVMEYVGGRSLSwirfapeeelARLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDL 287
Cdd:pfam00069  74 -YLVMEYCEGGDLF----------DYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENIlLDENGVVKIADF 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 21219970   288 GAIRRIDDRSS---GLVHTHGYAPPKRERDRRGLDVDSDLYTVG 328
Cdd:pfam00069 143 GLAKKLTKSSSsltTFVGTPEYMAPEVLLGGNGYGPKVDVWSLG 186
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
210-310 2.79e-08

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 54.82  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970  210 YIVMEYV-GGRSLSWIRFApeeelarlfgtGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVIHYGR-EIKVIDL 287
Cdd:PTZ00263  94 YFLLEFVvGGELFTHLRKA-----------GRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKgHVKVTDF 162
                         90       100
                 ....*....|....*....|...
gi 21219970  288 GAIRRIDDRSSGLVHTHGYAPPK 310
Cdd:PTZ00263 163 GFAKKVPDRTFTLCGTPEYLAPE 185
pknD PRK13184
serine/threonine-protein kinase; Reviewed
129-289 1.65e-07

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 53.62  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970  129 GHYAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKGLIN--TGDAVARRAAVEERRSLTTLHHRDIVRIVThvqhqVPGDAE 206
Cdd:PRK13184   2 QRYDIIRLIGKGGMGEVYLAYD-PVCSRRVALKKIREdlSENPLLKKRFLREAKIAADLIHPGIVPVYS-----ICSDGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970  207 PTgYIVMEYVGGRSLS------WIRFAPEEELARLFGTGGFefghvITYGCKILGALEYLHDRGLLYCDMKPENVI--HY 278
Cdd:PRK13184  76 PV-YYTMPYIEGYTLKsllksvWQKESLSKELAEKTSVGAF-----LSIFHKICATIEYVHSKGVLHRDLKPDNILlgLF 149
                        170
                 ....*....|.
gi 21219970  279 GrEIKVIDLGA 289
Cdd:PRK13184 150 G-EVVILDWGA 159
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
165-311 4.29e-05

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 45.20  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970  165 NTGDAVaRRAAVEERRSLTTLHHRDIVRivTHVQHQVPGDAEptgyIVMEYVGGRSLSWIRFAPEEELARLfgtggfefg 244
Cdd:PLN00034 110 NHEDTV-RRQICREIEILRDVNHPNVVK--CHDMFDHNGEIQ----VLLEFMDGGSLEGTHIADEQFLADV--------- 173
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21219970  245 hvityGCKILGALEYLHDRGLLYCDMKPEN-VIHYGREIKVIDLGAIRRID---DRSSGLVHTHGYAPPKR 311
Cdd:PLN00034 174 -----ARQILSGIAYLHRRHIVHRDIKPSNlLINSAKNVKIADFGVSRILAqtmDPCNSSVGTIAYMSPER 239
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
185-403 4.22e-03

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: 39.44  E-value: 4.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970    185 LHHRDIVRIVTHvqhqvpGDAEPTG-YIVMEYVGGRSLSwirfapeEELARLFGTGGFEFGHVITygcKILGALEYLHDR 263
Cdd:TIGR03903   35 LYHPNIVALLDS------GEAPPGLlFAVFEYVPGRTLR-------EVLAADGALPAGETGRLML---QVLDALACAHNQ 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970    264 GLLYCDMKPENVI----HYGREIKVIDLG----------AIRRIDDRSSGLVHTHGYAPPKRERDrRGLDVDSDLYTVG- 328
Cdd:TIGR03903   99 GIVHRDLKPQNIMvsqtGVRPHAKVLDFGigtllpgvrdADVATLTRTTEVLGTPTYCAPEQLRG-EPVTPNSDLYAWGl 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970    329 -----RTLKVLAERA---------------ARPAGLAARSFEALIRRATHPEPAARfrsaAEMSRQLWEVLREDQ--ALG 386
Cdd:TIGR03903  178 iflecLTGQRVVQGAsvaeilyqqlspvdvSLPPWIAGHPLGQVLRKALNKDPRQR----AASAPALAERFRALElcALV 253
                          250       260
                   ....*....|....*....|
gi 21219970    387 GREPYPER---STRFEPTAA 403
Cdd:TIGR03903  254 GILRMGEGagrEAIAAPLVA 273
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
130-375 5.60e-36

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: 136.95  E-value: 5.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDTRvPGLHVVLKGLI--NTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEP 207
Cdd:cd14014   1 RYRLVRLLGRGGMGEVYRARDTL-LGRPVAIKVLRpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGED------DG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 208 TGYIVMEYVGGRSLSwirfapeEELARLfgtGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVID 286
Cdd:cd14014  74 RPYIVMEYVEGGSLA-------DLLRER---GPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIlLTEDGRVKLTD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 287 LGAIRRIDD----RSSGLVHTHGYAPPKRERDRRgLDVDSDLYTVGRTL--------------------KVLAERAARPA 342
Cdd:cd14014 144 FGIARALGDsgltQTGSVLGTPAYMAPEQARGGP-VDPRSDIYSLGVVLyelltgrppfdgdspaavlaKHLQEAPPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21219970 343 GLAAR---SFEALIRRATHPEPAARFRSAAEMSRQL 375
Cdd:cd14014 223 PLNPDvppALDAIILRALAKDPEERPQSAAELLAAL 258
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
137-375 8.78e-23

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: 97.73  E-value: 8.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEDTRvPGLHVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIvthvqHQVpGDAEPTGYIVMEYV 216
Cdd:cd00180   1 LGKGSFGKVYKARDKE-TGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKL-----YDV-FETENFLYLVMEYC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 217 GGRSLswirfapEEELARLFGtgGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLGAIRRIDD 295
Cdd:cd00180  74 EGGSL-------KDLLKENKG--PLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENIlLDSDGTVKLADFGLAKDLDS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 296 RSSGLVHTHGYAPPKR----ERDRRGLDVDSDLYTVGRTLKVLAEraarpaglaarsFEALIRRATHPEPAARFrSAAEM 371
Cdd:cd00180 145 DDSLLKTTGGTTPPYYappeLLGGRYYGPKVDIWSLGVILYELEE------------LKDLIRRMLQYDPKKRP-SAKEL 211

                ....
gi 21219970 372 SRQL 375
Cdd:cd00180 212 LEHL 215
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
137-344 6.31e-14

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: 71.26  E-value: 6.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEdtrVPGLHVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHQVPGDAeptGYIVMEYV 216
Cdd:cd13979  11 LGSGGFGSVYKAT---YKGETVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAETGTDFASL---GLIIMEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 217 GGRSLSWIRFAPEEELArlfgtggfeFGHVITYGCKILGALEYLHDRGLLYCDMKPENVIHYGREI-KVIDLGAIRRIDD 295
Cdd:cd13979  85 GNGTLQQLIYEGSEPLP---------LAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVcKLCDFGCSVKLGE 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21219970 296 ------RSSGLVHTHGYAPPKRerdRRGLDVD--SDLYTVGRTLKVLAERAARPAGL 344
Cdd:cd13979 156 gnevgtPRSHIGGTYTYRAPEL---LKGERVTpkADIYSFGITLWQMLTRELPYAGL 209
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
131-309 1.83e-13

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: 69.96  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKGLINtgDAVARRAAVEERRSLTTL----HHRDIVRIVTHVQHQVPGDAe 206
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARD-KVTGEKVAIKKIKN--DFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEHRGGNHL- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 207 ptgYIVMEYVGgRSLswirfapeEELARLFGTGgFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGREIKV 284
Cdd:cd05118  77 ---CLVFELMG-MNL--------YELIKDYPRG-LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILinLELGQLKL 143
                       170       180
                ....*....|....*....|....*.
gi 21219970 285 IDLGAIRRIDDR-SSGLVHTHGYAPP 309
Cdd:cd05118 144 ADFGLARSFTSPpYTPYVATRWYRAP 169
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
136-295 3.74e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 69.09  E-value: 3.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 136 YLAVGGHGWVYLAEDTRVPGLHVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEPTGYIVMEY 215
Cdd:cd06606   7 LLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERT------ENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 216 VGGRSLSwirfapeeELARLFGtgGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGReIKVIDLGAIRRI 293
Cdd:cd06606  81 VPGGSLA--------SLLKKFG--KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILvdSDGV-VKLADFGCAKRL 149

                ..
gi 21219970 294 DD 295
Cdd:cd06606 150 AE 151
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
178-308 9.34e-12

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: 65.29  E-value: 9.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 178 ERRSLTTLHHRDIVRIVTHVQhqvpgDAEPTgYIVMEYV-GGRSLSWIRFApeeelarlfgtGGFEFGHVITYGCKILGA 256
Cdd:cd05580  51 EKRILSEVRHPFIVNLLGSFQ-----DDRNL-YMVMEYVpGGELFSLLRRS-----------GRFPNDVAKFYAAEVVLA 113
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21219970 257 LEYLHDRGLLYCDMKPENVI-----HygreIKVIDLGAIRRIDDRSSGLVHTHGY-AP 308
Cdd:cd05580 114 LEYLHSLDIVYRDLKPENLLldsdgH----IKITDFGFAKRVKDRTYTLCGTPEYlAP 167
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
210-309 1.96e-11

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: 64.35  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYV-GGRSLSWIRfapeeelarlfGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGReIKVID 286
Cdd:cd14209  77 YMVMEYVpGGEMFSHLR-----------RIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLidQQGY-IKVTD 144
                        90       100
                ....*....|....*....|...
gi 21219970 287 LGAIRRIDDRSSGLVHTHGYAPP 309
Cdd:cd14209 145 FGFAKRVKGRTWTLCGTPEYLAP 167
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
131-328 2.34e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 63.85  E-value: 2.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYlavGGHGWVYLAEDtRVPGLHVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIVTH-VQhqvpgdaEPTG 209
Cdd:cd13996  11 IELLGS---GGFGSVYKVRN-KVDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAwVE-------EPPL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYVGGRSL-SWIRfapeeelARLFGTGGFEFGHV-ITYgcKILGALEYLHDRGLLYCDMKPENV-IHYG-REIKVI 285
Cdd:cd13996  80 YIQMELCEGGTLrDWID-------RRNSSSKNDRKLALeLFK--QILKGVSYIHSKGIVHRDLKPSNIfLDNDdLQVKIG 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21219970 286 DLGAIRRIDD------------------RSSGlVHTHGYAPPKRErdrRGLDVD--SDLYTVG 328
Cdd:cd13996 151 DFGLATSIGNqkrelnnlnnnnngntsnNSVG-IGTPLYASPEQL---DGENYNekADIYSLG 209
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
140-310 1.31e-10

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: 61.68  E-value: 1.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 140 GGHGWVYLAEDtRVPGLHVVLKgLINTGDaVARRAAVE----ERRSLTTLHHRDIVRI--VTHVQHQVpgdaeptgYIVM 213
Cdd:cd05612  12 GTFGRVHLVRD-RISEHYYALK-VMAIPE-VIRLKQEQhvhnEKRVLKEVSHPFIIRLfwTEHDQRFL--------YMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 214 EYV-GGRSLSWIRFApeeelarlfgtGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVIhYGRE--IKVIDLGAI 290
Cdd:cd05612  81 EYVpGGELFSYLRNS-----------GRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL-LDKEghIKLTDFGFA 148
                       170       180
                ....*....|....*....|
gi 21219970 291 RRIDDRSSGLVHTHGYAPPK 310
Cdd:cd05612 149 KKLRDRTWTLCGTPEYLAPE 168
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
130-309 3.40e-10

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: 59.84  E-value: 3.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKgLINTGDAVARRAAVEER--RSLTTLHHRDIVRIVTHVQhqvpgdaep 207
Cdd:cd14003   1 NYELGKTLGEGSFGKVKLARH-KLTGEKVAIK-IIDKSKLKEEIEEKIKReiEIMKLLNHPNIIKLYEVIE--------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 208 TG---YIVMEYV-GGRSLSWI----RFaPEEELARLFGtggfefghvitygcKILGALEYLHDRGLLYCDMKPENV-IHY 278
Cdd:cd14003  70 TEnkiYLVMEYAsGGELFDYIvnngRL-SEDEARRFFQ--------------QLISAVDYCHSNGIVHRDLKLENIlLDK 134
                       170       180       190
                ....*....|....*....|....*....|...
gi 21219970 279 GREIKVIDLGAIRRI--DDRSSGLVHTHGYAPP 309
Cdd:cd14003 135 NGNLKIIDFGLSNEFrgGSLLKTFCGTPAYAAP 167
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
172-294 1.20e-09

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: 58.05  E-value: 1.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 172 RRAAVEERRSLTTLHHRDIVRIvthvqHQVPGDaePTGYI-VMEYVGGRSLsWIRFAPEEELARlfgtggfefGHVITYG 250
Cdd:cd14006  33 KEAVLREISILNQLQHPRIIQL-----HEAYES--PTELVlILELCSGGEL-LDRLAERGSLSE---------EEVRTYM 95
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21219970 251 CKILGALEYLHDRGLLYCDMKPENVIHYGR---EIKVIDLGAIRRID 294
Cdd:cd14006  96 RQLLEGLQYLHNHHILHLDLKPENILLADRpspQIKIIDFGLARKLN 142
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
140-372 1.46e-09

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: 57.98  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 140 GGHGWVYLAEDtRVPGLHVVLKgLINTGDAVARRAAVEERRSLTTLHHRDIVRIVThvQHQVPGDAeptgYIVMEYVGGR 219
Cdd:cd05122  11 GGFGVVYKARH-KKTGQIVAIK-KINLESKEKKESILNEIAILKKCKHPNIVKYYG--SYLKKDEL----WIVMEFCSGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 220 SLS-WIRFA----PEEELArlfgtggfefghvitYGCK-ILGALEYLHDRGLLYCDMKPENVI--HYGrEIKVIDLGAIR 291
Cdd:cd05122  83 SLKdLLKNTnktlTEQQIA---------------YVCKeVLKGLEYLHSHGIIHRDIKAANILltSDG-EVKLIDFGLSA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 292 RIDDRSSG--LVHTHGYAPPKRERDRRgLDVDSDLYTVGRTLKVLAERaaRPAGLAARSFEALIRRATHPEPaaRFRSAA 369
Cdd:cd05122 147 QLSDGKTRntFVGTPYWMAPEVIQGKP-YGFKADIWSLGITAIEMAEG--KPPYSELPPMKALFLIATNGPP--GLRNPK 221

                ...
gi 21219970 370 EMS 372
Cdd:cd05122 222 KWS 224
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
130-375 2.66e-09

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 57.49  E-value: 2.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDTRVPGLHVV-------LKGLINTGDAVARraaveERRSLTTLHHRDIVRIVTHVQhqvp 202
Cdd:cd14098   1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIkqivkrkVAGNDKNLQLFQR-----EINILKSLEHPGIVRLIDWYE---- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 203 gDAEPTgYIVMEYV-GGRSLSWIrfapeeelarlfgtggFEFGHVITYGCK-----ILGALEYLHDRGLLYCDMKPENVI 276
Cdd:cd14098  72 -DDQHI-YLVMEYVeGGDLMDFI----------------MAWGAIPEQHAReltkqILEAMAYTHSMGITHRDLKPENIL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 277 ---HYGREIKVIDLGAIRRIDDRS--SGLVHTHGYAPP-----KRERDRRGLDVDSDLYTVGRTLKVLAERAARPAGLAA 346
Cdd:cd14098 134 itqDDPVIVKISDFGLAKVIHTGTflVTFCGTMAYLAPeilmsKEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQ 213
                       250       260
                ....*....|....*....|....*....
gi 21219970 347 RSFEALIRRATHPEPAARFRSAAEMSRQL 375
Cdd:cd14098 214 LPVEKRIRKGRYTQPPLVDFNISEEAIDF 242
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
137-275 3.12e-09

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


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 57.23  E-value: 3.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEDTRVpGLHVVLKGLINTGDAVARRAAV-EERRSLTTLHHRDIVRIVTHVQHQVpgdaepTGYIVMEY 215
Cdd:cd06627   8 IGRGAFGSVYKGLNLNT-GEFVAIKQISLEKIPKSDLKSVmGEIDLLKKLNHPNIVKYIGSVKTKD------SLYIILEY 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21219970 216 VGGRSLSWI--RFA--PEEELARlfgtggfefghvitYGCKILGALEYLHDRGLLYCDMKPENV 275
Cdd:cd06627  81 VENGSLASIikKFGkfPESLVAV--------------YIYQVLEGLAYLHEQGVIHRDIKGANI 130
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
140-313 3.35e-09

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: 57.23  E-value: 3.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 140 GGHGWVYLAEDtrvpglhvvlkglINTGDAVA----------RRAAVE----ERRSLTTLHHRDIVRIVTHVQHqvpgda 205
Cdd:cd05579   4 GAYGRVYLAKK-------------KSTGDLYAikvikkrdmiRKNQVDsvlaERNILSQAQNPFVVKLYYSFQG------ 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 206 EPTGYIVMEYV-GGRSLSWIRF--APEEELARLfgtggfefghvitYGCKILGALEYLHDRGLLYCDMKPENVI--HYGR 280
Cdd:cd05579  65 KKNLYLVMEYLpGGDLYSLLENvgALDEDVARI-------------YIAEIVLALEYLHSHGIIHRDLKPDNILidANGH 131
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 21219970 281 eIKVID-----LGAIRRIDDRSSgLVHTHGYAPPKRER 313
Cdd:cd05579 132 -LKLTDfglskVGLVRRQIKLSI-QKKSNGAPEKEDRR 167
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
130-288 3.91e-09

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: 56.70  E-value: 3.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDTRvPGLHVVLKgLINTG--DAVARRAAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEP 207
Cdd:cd08215   1 KYEKIRVIGKGSFGSAYLVRRKS-DGKLYVLK-EIDLSnmSEKEREEALNEVKLLSKLKHPNIVKYYESFEE------NG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 208 TGYIVMEYVGGRSLS-WIR-------FAPEEELARLFgtggfefghvitygCKILGALEYLHDRGLLYCDMKPENV-IHY 278
Cdd:cd08215  73 KLCIVMEYADGGDLAqKIKkqkkkgqPFPEEQILDWF--------------VQICLALKYLHSRKILHRDLKTQNIfLTK 138
                       170
                ....*....|
gi 21219970 279 GREIKVIDLG 288
Cdd:cd08215 139 DGVVKLGDFG 148
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
130-309 4.45e-09

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: 56.72  E-value: 4.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDtrvpglhvvlkglINTGDAVA------RRAAVEERRSLTT-------LHHRDIVRIV-- 194
Cdd:cd05117   1 KYELGKVLGRGSFGVVRLAVH-------------KKTGEEYAvkiidkKKLKSEDEEMLRReieilkrLDHPNIVKLYev 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 195 ----THVqhqvpgdaeptgYIVMEYV-GGRSLSWI----RFaPEEElARlfgtggfefgHVITygcKILGALEYLHDRGL 265
Cdd:cd05117  68 feddKNL------------YLVMELCtGGELFDRIvkkgSF-SERE-AA----------KIMK---QILSAVAYLHSQGI 120
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 21219970 266 LYCDMKPENVIHYGRE----IKVIDLGAIRRIDDRS--SGLVHTHGYAPP 309
Cdd:cd05117 121 VHRDLKPENILLASKDpdspIKIIDFGLAKIFEEGEklKTVCGTPYYVAP 170
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
131-309 5.31e-09

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: 56.51  E-value: 5.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKGLINTGDAVarRAAVEERRSLTTLH------HRDIVRIVTHVQHQvpgd 204
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYD-LLTGEEVALKIIKNNKDYL--DQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFK---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 205 aEPTgYIVMEYVGgRSLswirfapeEELARLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGR-E 281
Cdd:cd14133  74 -NHL-CIVFELLS-QNL--------YEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILlaSYSRcQ 142
                       170       180
                ....*....|....*....|....*...
gi 21219970 282 IKVIDLGAIRRIDDRSSGLVHTHGYAPP 309
Cdd:cd14133 143 IKIIDFGSSCFLTQRLYSYIQSRYYRAP 170
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
210-376 5.94e-09

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: 56.15  E-value: 5.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYV-GGRSLSWIR---FAPEEELARLFgtggfefghvitygCKILGALEYLHDRGLLYCDMKPENVIHYGRE-IKV 284
Cdd:cd14162  76 YIIMELAeNGDLLDYIRkngALPEPQARRWF--------------RQLVAGVEYCHSKGVVHRDLKCENLLLDKNNnLKI 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 285 IDLGAIRR---IDDRSSGLVHT----HGYAPPKRerdRRGLDVD---SD-------LYT--VGR------TLKVLAERAA 339
Cdd:cd14162 142 TDFGFARGvmkTKDGKPKLSETycgsYAYASPEI---LRGIPYDpflSDiwsmgvvLYTmvYGRlpfddsNLKVLLKQVQ 218
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 21219970 340 RPAGLAAR---SFEA--LIRRATHPEPaARFrSAAEMSRQLW 376
Cdd:cd14162 219 RRVVFPKNptvSEECkdLILRMLSPVK-KRI-TIEEIKRDPW 258
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
124-322 9.64e-09

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: 56.35  E-value: 9.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 124 GDRVAGHYAVLGYLAVGGHGWVYLAEDTrvpglhvvlkgliNTGDAVARR-------------AAVEERRSLTTLHHRDI 190
Cdd:cd07864   2 GKRCVDKFDIIGIIGEGTYGQVYKAKDK-------------DTGELVALKkvrldnekegfpiTAIREIKILRQLNHRSV 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 191 VR---IVTHVQHQVPGDAEPTG-YIVMEYVggrslswirfapEEELARLFGTGGFEFG--HVITYGCKILGALEYLHDRG 264
Cdd:cd07864  69 VNlkeIVTDKQDALDFKKDKGAfYLVFEYM------------DHDLMGLLESGLVHFSedHIKSFMKQLLEGLNYCHKKN 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21219970 265 LLYCDMKPENVIHYGR-EIKVIDLGAIRRIDDRSSGL----VHTHGYAPPK----RERDRRGLDVDS 322
Cdd:cd07864 137 FLHRDIKCSNILLNNKgQIKLADFGLARLYNSEESRPytnkVITLWYRPPElllgEERYGPAIDVWS 203
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
127-373 1.21e-08

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: 56.20  E-value: 1.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 127 VAGHYAVLGYLAVGGHGWVYLAEDTRVpGLHVVLKGLINTGDAV--ARRAaVEERRSLTTLHHRDIVRIVTHVQHQVPGD 204
Cdd:cd07877  15 VPERYQNLSPVGSGAYGSVCAAFDTKT-GLRVAVKKLSRPFQSIihAKRT-YRELRLLKHMKHENVIGLLDVFTPARSLE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 205 AEPTGYIVMEYVGGrslswirfapeeELARLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIK 283
Cdd:cd07877  93 EFNDVYLVTHLMGA------------DLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLaVNEDCELK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 284 VIDLGAIRRIDDRSSGLVHTHGYAPPKRERDRRGLDVDSDLYTVGRTL-KVLAERAARPAGLAARSFEALIRRATHPEPA 362
Cdd:cd07877 161 ILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMaELLTGRTLFPGTDHIDQLKLILRLVGTPGAE 240
                       250
                ....*....|.
gi 21219970 363 ARFRSAAEMSR 373
Cdd:cd07877 241 LLKKISSESAR 251
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
173-298 1.82e-08

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: 54.54  E-value: 1.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 173 RAAVE-ERRSLTTLHHRDIVRIVthvqhqvpgDAEPTGY---IVMEYVGGRSLsWIRFAPEE----ELArlfgtggfefg 244
Cdd:cd14103  34 REDVRnEIEIMNQLRHPRLLQLY---------DAFETPRemvLVMEYVAGGEL-FERVVDDDfeltERD----------- 92
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21219970 245 hVITYGCKILGALEYLHDRGLLYCDMKPENVI---HYGREIKVIDLGAIRRIDDRSS 298
Cdd:cd14103  93 -CILFMRQICEGVQYMHKQGILHLDLKPENILcvsRTGNQIKIIDFGLARKYDPDKK 148
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
137-288 2.06e-08

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: 54.87  E-value: 2.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEDT-----------------RVPGLHVVLKGLINTGDAVARRAAVeerrsLTTLHHRDIVRIvthvqH 199
Cdd:cd14008   1 LGRGSFGKVKLALDTetgqlyaikifnksrlrKRREGKNDRGKIKNALDDVRREIAI-----MKKLDHPNIVRL-----Y 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 200 QVPGDaePTG---YIVMEYV-GGRSLSWIRFAP----EEELARLfgtggfefghvitYGCKILGALEYLHDRGLLYCDMK 271
Cdd:cd14008  71 EVIDD--PESdklYLVLEYCeGGPVMELDSGDRvpplPEETARK-------------YFRDLVLGLEYLHENGIVHRDIK 135
                       170
                ....*....|....*....
gi 21219970 272 PENVI--HYGReIKVIDLG 288
Cdd:cd14008 136 PENLLltADGT-VKISDFG 153
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
237-338 2.59e-08

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 54.84  E-value: 2.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 237 GTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGrEIKVIDLGAIRRIDDRS--SGLVHTHGYAPPKRE 312
Cdd:cd05577  88 GTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILldDHG-HVRISDLGLAVEFKGGKkiKGRVGTHGYMAPEVL 166
                        90       100
                ....*....|....*....|....*..
gi 21219970 313 RDRRGLDVDSDLYTVGRTL-KVLAERA 338
Cdd:cd05577 167 QKEVAYDFSVDWFALGCMLyEMIAGRS 193
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
178-316 3.13e-08

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: 54.53  E-value: 3.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 178 ERRSLTTLHHRDIVRIVTHVQhqvpgDAEPTgYIVMEYV-GGRSLSWIRFApeeelarlfgtGGFEFgHVIT-YGCKILG 255
Cdd:cd05581  51 EKEVLSRLAHPGIVKLYYTFQ-----DESKL-YFVLEYApNGDLLEYIRKY-----------GSLDE-KCTRfYTAEIVL 112
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21219970 256 ALEYLHDRGLLYCDMKPENVI--HYGReIKVIDLGAIRRIDDRSSGLVHTHGYAPPKRERDRR 316
Cdd:cd05581 113 ALEYLHSKGIIHRDLKPENILldEDMH-IKITDFGTAKVLGPDSSPESTKGDADSQIAYNQAR 174
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
131-297 3.15e-08

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: 54.32  E-value: 3.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDTRVPGLHVVlkGLINTGD-AVARRAAVEERRSLTT-------LHHRDIVRIVTHVqhqvp 202
Cdd:cd14084   8 YIMSRTLGSGACGEVKLAYDKSTCKKVAI--KIINKRKfTIGSRREINKPRNIETeieilkkLSHPCIIKIEDFF----- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 203 gDAEPTGYIVMEYVGGRSLswirfapeeeLARLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVIHYGRE- 281
Cdd:cd14084  81 -DAEDDYYIVLELMEGGEL----------FDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEe 149
                       170
                ....*....|....*....
gi 21219970 282 ---IKVIDLGAIRRIDDRS 297
Cdd:cd14084 150 eclIKITDFGLSKILGETS 168
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
131-288 3.42e-08

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: 54.28  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDTRVpGLHVVLKGLI------NTGDAVARRAAVEERRSLTTLH-HRDIVRIVTHVQHQVpg 203
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDLRT-GRKYAIKCLYksgpnsKDGNDFQKLPQLREIDLHRRVSrHPNIITLHDVFETEV-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 204 daepTGYIVMEYVGGRSL-----SWIRFAPEEELARlfgtggfefgHVITygcKILGALEYLHDRGLLYCDMKPENVIHY 278
Cdd:cd13993  79 ----AIYIVLEYCPNGDLfeaitENRIYVGKTELIK----------NVFL---QLIDAVKHCHSLGIYHRDIKPENILLS 141
                       170
                ....*....|..
gi 21219970 279 GRE--IKVIDLG 288
Cdd:cd13993 142 QDEgtVKLCDFG 153
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
182-288 5.27e-08

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: 53.46  E-value: 5.27e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 182 LTTLHHRDIVRIVTHVQhqvpgDAEPTGYIVMEYVGGRSLswirfapeeeLARLFGTGGFEFGHVITYGCKILGALEYLH 261
Cdd:cd13994  51 SSKLHHPNIVKVLDLCQ-----DLHGKWCLVMEYCPGGDL----------FTLIEKADSLSLEEKDCFFKQILRGVAYLH 115
                        90       100
                ....*....|....*....|....*....
gi 21219970 262 DRGLLYCDMKPENVI--HYGrEIKVIDLG 288
Cdd:cd13994 116 SHGIAHRDLKPENILldEDG-VLKLTDFG 143
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
120-288 6.29e-08

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: 53.70  E-value: 6.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 120 KLRPGDRVAGHYAVLGYLAVGGHGWVYLAEDTRVPGlHVVLKGLINTgdavaRR---AAVEERRSLTTLHHRD------I 190
Cdd:cd14210   4 KVVLGDHIAYRYEVLSVLGKGSFGQVVKCLDHKTGQ-LVAIKIIRNK-----KRfhqQALVEVKILKHLNDNDpddkhnI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 191 VRIVTHVQ---HQVpgdaeptgyIVMEYVG-------------GRSLSWIRfapeeelarlfgtggfefghviTYGCKIL 254
Cdd:cd14210  78 VRYKDSFIfrgHLC---------IVFELLSinlyellksnnfqGLSLSLIR----------------------KFAKQIL 126
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21219970 255 GALEYLHDRGLLYCDMKPENV--IHYGR-EIKVIDLG 288
Cdd:cd14210 127 QALQFLHKLNIIHCDLKPENIllKQPSKsSIKVIDFG 163
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
127-294 6.91e-08

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: 54.01  E-value: 6.91e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 127 VAGHYAVLGYLAVGGHGWVYLAEDTRVpGLHVVLKGLINTgDAVARRAAVEERRSLTTLHHRDIVRiVTHV----QHQVP 202
Cdd:cd07854   3 LGSRYMDLRPLGCGSNGLVFSAVDSDC-DKRVAVKKIVLT-DPQSVKHALREIKIIRRLDHDNIVK-VYEVlgpsGSDLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 203 GD-AEPTG----YIVMEYVggrslswirfapEEELARLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVIH 277
Cdd:cd07854  80 EDvGSLTElnsvYIVQEYM------------ETDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFI 147
                       170
                ....*....|....*....
gi 21219970 278 YGRE--IKVIDLGAIRRID 294
Cdd:cd07854 148 NTEDlvLKIGDFGLARIVD 166
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
173-302 6.95e-08

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: 53.08  E-value: 6.95e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 173 RAAVEERRSLTTLHHRDIVR---IVTHvQHQVpgdaeptgYIVMEYVGGRSLswirfapeEELARLfgtGGFEFGHVI-T 248
Cdd:cd06626  44 KEIADEMKVLEGLDHPNLVRyygVEVH-REEV--------YIFMEYCQEGTL--------EELLRH---GRILDEAVIrV 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21219970 249 YGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLGAIRRIDDRSSGLVH 302
Cdd:cd06626 104 YTLQLLEGLAYLHENGIVHRDIKPANIfLDSNGLIKLGDFGSAVKLKNNTTTMAP 158
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
137-309 9.21e-08

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 52.61  E-value: 9.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEDTRvPGLHVVLKGLINtgDAVARRAAVE----ERRSLTTLHHRDIVRivthvQHQVPGDAEPTgYIV 212
Cdd:cd05572   1 LGVGGFGRVELVQLKS-KGRTFALKCVKK--RHIVQTRQQEhifsEKEILEECNSPFIVK-----LYRTFKDKKYL-YML 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 213 MEYVGGRSLSWI---RFAPEEELARlFGTGgfefghvitygCKILgALEYLHDRGLLYCDMKPENVI--HYGReIKVIDL 287
Cdd:cd05572  72 MEYCLGGELWTIlrdRGLFDEYTAR-FYTA-----------CVVL-AFEYLHSRGIIYRDLKPENLLldSNGY-VKLVDF 137
                       170       180
                ....*....|....*....|....
gi 21219970 288 GAIRRIDDRSSG--LVHTHGYAPP 309
Cdd:cd05572 138 GFAKKLGSGRKTwtFCGTPEYVAP 161
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
137-288 9.51e-08

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: 52.52  E-value: 9.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLA---EDTRVPGLHVVLKGLINTGDAVARraAVEERRSLTTLHHRDIVRivTHVQHQVPGDAeptgYIVM 213
Cdd:cd05123   1 LGKGSFGKVLLVrkkDTGKLYAMKVLRKKEIIKRKEVEH--TLNERNILERVNHPFIVK--LHYAFQTEEKL----YLVL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 214 EYVGGRSL-SWI----RFapEEELARLfgtggfefghvitYGCKILGALEYLHDRGLLYCDMKPENVI-----HygreIK 283
Cdd:cd05123  73 DYVPGGELfSHLskegRF--PEERARF-------------YAAEIVLALEYLHSLGIIYRDLKPENILldsdgH----IK 133

                ....*
gi 21219970 284 VIDLG 288
Cdd:cd05123 134 LTDFG 138
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
252-328 1.18e-07

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: 52.41  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 252 KILGALEYLHDRGLLYCDMKPENVIHYGRE----IKVIDLGAIRRIDDRS--SGLVHTHGYAPPKRERdRRGLDVDSDLY 325
Cdd:cd14082 111 QILVALRYLHSKNIVHCDLKPENVLLASAEpfpqVKLCDFGFARIIGEKSfrRSVVGTPAYLAPEVLR-NKGYNRSLDMW 189

                ...
gi 21219970 326 TVG 328
Cdd:cd14082 190 SVG 192
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
237-316 1.47e-07

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 52.67  E-value: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 237 GTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGrEIKVIDLGAIRRIDDRSS--GLVHTHGYAPPKRE 312
Cdd:cd05632  97 GNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILldDYG-HIRISDLGLAVKIPEGESirGRVGTVGYMAPEVL 175

                ....
gi 21219970 313 RDRR 316
Cdd:cd05632 176 NNQR 179
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
164-309 1.63e-07

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: 51.87  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 164 INTGDAVARRaaveERRSLTTLHHRDIVRIVTHVQhqvpGDAEPTGYIVMEYVGGRSLSWIRFAPEEELARlfgtggFEf 243
Cdd:cd14119  34 IPNGEANVKR----EIQILRRLNHRNVIKLVDVLY----NEEKQKLYMVMEYCVGGLQEMLDSAPDKRLPI------WQ- 98
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21219970 244 GHviTYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLG---AIRRIDD-----RSSGlvhTHGYAPP 309
Cdd:cd14119  99 AH--GYFVQLIDGLEYLHSQGIIHKDIKPGNLlLTTDGTLKISDFGvaeALDLFAEddtctTSQG---SPAFQPP 168
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
131-298 1.74e-07

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: 52.32  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKG-LINTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEPTG 209
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRN-KATGEIVAIKKfKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRR------KGRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYVGGRSLSWIRFAPeeelarlfgtGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLG 288
Cdd:cd07833  76 YLVFEYVERTLLELLEASP----------GGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENIlVSESGVLKLCDFG 145
                       170
                ....*....|
gi 21219970 289 AIRRIDDRSS 298
Cdd:cd07833 146 FARALTARPA 155
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
174-331 1.88e-07

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: 52.19  E-value: 1.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 174 AAVEERRSLTTLHHRDIVRIVTHVQhqvpgdAEPTGYIVMEYVGGRSLSWIRFAPEEElarlfgTGGFEFGHVITYGCKI 253
Cdd:cd05608  47 GAMVEKRILAKVHSRFIVSLAYAFQ------TKTDLCLVMTIMNGGDLRYHIYNVDEE------NPGFQEPRACFYTAQI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 254 LGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLGAIRRIDD---RSSGLVHTHGYAPPKRERDRRgLDVDSDLYTVGR 329
Cdd:cd05608 115 ISGLEHLHQRRIIYRDLKPENVlLDDDGNVRISDLGLAVELKDgqtKTKGYAGTPGFMAPELLLGEE-YDYSVDYFTLGV 193

                ..
gi 21219970 330 TL 331
Cdd:cd05608 194 TL 195
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
123-289 2.15e-07

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: 52.44  E-value: 2.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 123 PGDRVAGHYAVLGYLAVGGHGWVYLAEDTRVpGLHVVLKGLINtgDAVARRAAVEErrslttlhhrdiVRIVTHVQHQvp 202
Cdd:cd14224  59 PHDHIAYRYEVLKVIGKGSFGQVVKAYDHKT-HQHVALKMVRN--EKRFHRQAAEE------------IRILEHLKKQ-- 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 203 gDAEPTGYIV--MEYVGGRSLSWIRFAPEE----ELARLFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI 276
Cdd:cd14224 122 -DKDNTMNVIhmLESFTFRNHICMTFELLSmnlyELIKKNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENIL 200
                       170
                ....*....|....*.
gi 21219970 277 --HYGRE-IKVIDLGA 289
Cdd:cd14224 201 lkQQGRSgIKVIDFGS 216
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
134-303 2.21e-07

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: 52.02  E-value: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 134 LGYLAVGGHGWVYLAEDT------RVPGLHVVLKGLI--NTGDAVARRAaveERRSLTTLHHRDIVRIvtHVQHQVPGDA 205
Cdd:cd05584   1 LKVLGKGGYGKVFQVRKTtgsdkgKIFAMKVLKKASIvrNQKDTAHTKA---ERNILEAVKHPFIVDL--HYAFQTGGKL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 206 eptgYIVMEYVGGRSLswirFAP-EEELARLFGTGGFefghvitYGCKILGALEYLHDRGLLYCDMKPENVI--HYGrEI 282
Cdd:cd05584  76 ----YLILEYLSGGEL----FMHlEREGIFMEDTACF-------YLAEITLALGHLHSLGIIYRDLKPENILldAQG-HV 139
                       170       180
                ....*....|....*....|..
gi 21219970 283 KVIDLGAIR-RIDDrsSGLVHT 303
Cdd:cd05584 140 KLTDFGLCKeSIHD--GTVTHT 159
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
130-292 2.82e-07

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: 51.53  E-value: 2.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 130 HYAVLGYLAVGGHGWVYLAEDTRVPGLHVVLKGLINTGDAVArrAAVEERRSLTTLHHRDIVRIVTHVQHQVpGDAEPTG 209
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVK--EAMREIENYRLFNHPNILRLLDSQIVKE-AGGKKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYVGGRSL-SWIR-------FAPEEELARLFgtggfefgHVItygCKILGALEYLHDRGLLYCDMKPENV-IHYGR 280
Cdd:cd13986  78 YLLLPYYKRGSLqDEIErrlvkgtFFPEDRILHIF--------LGI---CRGLKAMHEPELVPYAHRDIKPGNVlLSEDD 146
                       170
                ....*....|..
gi 21219970 281 EIKVIDLGAIRR 292
Cdd:cd13986 147 EPILMDLGSMNP 158
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
131-365 2.90e-07

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: 51.24  E-value: 2.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAE---DTRVPGLHVVLKGLINTGDavaRRAAVEERRSLTTLHHRDIVRIvthvqhqvpGDAEP 207
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKrlsDNQVYALKEVNLGSLSQKE---REDSVNEIRLLASVNHPNIIRY---------KEAFL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 208 TG---YIVMEYVGGRSLSWI--------RFAPEEELARLFgtggfefghvitygCKILGALEYLHDRGLLYCDMKPENVI 276
Cdd:cd08530  70 DGnrlCIVMEYAPFGDLSKLiskrkkkrRLFPEDDIWRIF--------------IQMLRGLKALHDQKILHRDLKSANIL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 277 HY-GREIKVIDLGaIRRIddRSSGLVHTH-G---YAPPKRERDrRGLDVDSDLYTVGrtlKVLAERAARPAGLAARSFEA 351
Cdd:cd08530 136 LSaGDLVKIGDLG-ISKV--LKKNLAKTQiGtplYAAPEVWKG-RPYDYKSDIWSLG---CLLYEMATFRPPFEARTMQE 208
                       250
                ....*....|....*..
gi 21219970 352 L---IRRATHPEPAARF 365
Cdd:cd08530 209 LrykVCRGKFPPIPPVY 225
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
252-379 2.98e-07

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: 51.97  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 252 KILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLGAIRRIDDRSSGLVHTHGYAPPKRERDRRGLDVDSDLYTVGRT 330
Cdd:cd07878 126 QLLRGLKYIHSAGIIHRDLKPSNVaVNEDCELRILDFGLARQADDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCI 205
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21219970 331 L-KVLAERAARPAGLAARSFEALIRRATHPEPAARFRSAAEMSRQLWEVL 379
Cdd:cd07878 206 MaELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISSEHARKYIQSL 255
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
133-309 3.06e-07

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: 50.94  E-value: 3.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 133 VLGYLAVGGHGWVYLAEDtRVPGLHVVLKgLINTgdAVARRAAVEE--RRSL---TTLHHRDIVRIVTHVQHQ--Vpgda 205
Cdd:cd14007   4 IGKPLGKGKFGNVYLARE-KKSGFIVALK-VISK--SQLQKSGLEHqlRREIeiqSHLRHPNILRLYGYFEDKkrI---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 206 eptgYIVMEYVGGRSL-----SWIRFaPEEELArlfgtggfefghviTYGCKILGALEYLHDRGLLYCDMKPENV-IHYG 279
Cdd:cd14007  76 ----YLILEYAPNGELykelkKQKRF-DEKEAA--------------KYIYQLALALDYLHSKNIIHRDIKPENIlLGSN 136
                       170       180       190
                ....*....|....*....|....*....|.
gi 21219970 280 REIKVIDLG-AIRRIDDRSSGLVHTHGYAPP 309
Cdd:cd14007 137 GELKLADFGwSVHAPSNRRKTFCGTLDYLPP 167
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
166-363 3.75e-07

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: 51.34  E-value: 3.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 166 TGDAVA----------RRAAVEERR--SLTTLHHRDIVRIV-----THVQHQVpgdaeptgyIVMEYVGGRSLswirFAP 228
Cdd:cd13988  17 TGDLYAvkvfnnlsfmRPLDVQMREfeVLKKLNHKNIVKLFaieeeLTTRHKV---------LVMELCPCGSL----YTV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 229 EEELARLFGTGGFEFGHVITYgckILGALEYLHDRGLLYCDMKPENVIHYGRE-----IKVIDLGAIRRI--DDRSSGLV 301
Cdd:cd13988  84 LEEPSNAYGLPESEFLIVLRD---VVAGMNHLRENGIVHRDIKPGNIMRVIGEdgqsvYKLTDFGAARELedDEQFVSLY 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21219970 302 HTHGYAPPK-------RERDRRGLDVDSDLYTVGRTLKVLAERAA--RPAGLAARSFEALIRRATHPEPAA 363
Cdd:cd13988 161 GTEEYLHPDmyeravlRKDHQKKYGATVDLWSIGVTFYHAATGSLpfRPFEGPRRNKEVMYKIITGKPSGA 231
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
253-309 4.89e-07

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: 50.40  E-value: 4.89e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 253 ILGALEYLHDRGLLYCDMKPENVIHYGRE---IKVIDLGAIRRIDDRSSGLVHTHGYAPP 309
Cdd:cd13987 100 LASALDFMHSKNLVHRDIKPENVLLFDKDcrrVKLCDFGLTRRVGSTVKRVSGTIPYTAP 159
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
127-310 5.21e-07

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: 51.11  E-value: 5.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 127 VAGHYAVLGYLAVGGHGWVYLAEDTRVpGLHVVLKGLIN--TGDAVARRAaVEERRSLTTLHHRDIVRIVTHVQHQVPGD 204
Cdd:cd07880  13 VPDRYRDLKQVGSGAYGTVCSALDRRT-GAKVAIKKLYRpfQSELFAKRA-YRELRLLKHMKHENVIGLLDVFTPDLSLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 205 AEPTGYIVMEYVG---GRSLSWIRFApEEELARLfgtggfefghviTYgcKILGALEYLHDRGLLYCDMKPENV-IHYGR 280
Cdd:cd07880  91 RFHDFYLVMPFMGtdlGKLMKHEKLS-EDRIQFL------------VY--QMLKGLKYIHAAGIIHRDLKPGNLaVNEDC 155
                       170       180       190
                ....*....|....*....|....*....|
gi 21219970 281 EIKVIDLGAIRRIDDRSSGLVHTHGYAPPK 310
Cdd:cd07880 156 ELKILDFGLARQTDSEMTGYVVTRWYRAPE 185
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
140-309 5.76e-07

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: 50.64  E-value: 5.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 140 GGHGWVYLAEDtRVPGLHVVLKGLI----NTGDAVArraAVEERRSLTTLHHRDIVRIVTHVQHQVPGDAEPTGYIVMEY 215
Cdd:cd07840  10 GTYGQVYKARN-KKTGELVALKKIRmeneKEGFPIT---AIREIKLLQKLDHPNVVRLKEIVTSKGSAKYKGSIYMVFEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 216 VggrslswirfapEEELARLFGTGGFEF--GHVITYGCKILGALEYLHDRGLLYCDMKPENV-IHYGREIKVIDLGAIRR 292
Cdd:cd07840  86 M------------DHDLTGLLDNPEVKFteSQIKCYMKQLLEGLQYLHSNGILHRDIKGSNIlINNDGVLKLADFGLARP 153
                       170       180
                ....*....|....*....|.
gi 21219970 293 IDDRSSG----LVHTHGYAPP 309
Cdd:cd07840 154 YTKENNAdytnRVITLWYRPP 174
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
168-292 6.00e-07

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: 50.21  E-value: 6.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 168 DAVARRAAVEERRSLTTLHHRDIVRIvtHVQHQVPGdaeptgYIVM--EYVGGRSL--SWI-RFAPEEElarlfgtggfe 242
Cdd:cd14111  39 QAEEKQGVLQEYEILKSLHHERIMAL--HEAYITPR------YLVLiaEFCSGKELlhSLIdRFRYSED----------- 99
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 21219970 243 fgHVITYGCKILGALEYLHDRGLLYCDMKPENVIHYG-REIKVIDLGAIRR 292
Cdd:cd14111 100 --DVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNlNAIKIVDFGSAQS 148
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
140-309 6.11e-07

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: 50.69  E-value: 6.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 140 GGHGWVYLAEDTRvpglhvvlkglinTGDAVA-RRAAVEERRS------------LTTLHHRDIVrivtHVQHQVPGDAE 206
Cdd:cd07843  16 GTYGVVYRARDKK-------------TGEIVAlKKLKMEKEKEgfpitslreiniLLKLQHPNIV----TVKEVVVGSNL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 207 PTGYIVMEYVggrslswirfapEEELARLFGT--GGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVIHYGR-EIK 283
Cdd:cd07843  79 DKIYMVMEYV------------EHDLKSLMETmkQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRgILK 146
                       170       180
                ....*....|....*....|....*....
gi 21219970 284 VIDLGAIRRIDD---RSSGLVHTHGYAPP 309
Cdd:cd07843 147 ICDFGLAREYGSplkPYTQLVVTLWYRAP 175
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
134-331 6.25e-07

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: 50.58  E-value: 6.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 134 LGYLAVGGHGWVYLAEDTRVPGLHVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIVT----HVQHQVpgdaeptg 209
Cdd:cd14049  11 IARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTawmeHVQLML-------- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEyVGGRSL-SWI----RFAPEEElarlFGTGGFEFGHV-----ITYgcKILGALEYLHDRGLLYCDMKPENVIHYG 279
Cdd:cd14049  83 YIQMQ-LCELSLwDWIvernKRPCEEE----FKSAPYTPVDVdvttkILQ--QLLEGVTYIHSMGIVHRDLKPRNIFLHG 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21219970 280 RE--IKVIDLG-AIRRI---------DDRSSGLVHTHG-----YAPPKRERDRRgLDVDSDLYTVGRTL 331
Cdd:cd14049 156 SDihVRIGDFGlACPDIlqdgndsttMSRLNGLTHTSGvgtclYAAPEQLEGSH-YDFKSDMYSIGVIL 223
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
170-291 9.55e-07

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: 49.99  E-value: 9.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 170 VARRA-AVEERRSLTTLH-HRDIVRIvthvqHQVPGDAEPTgYIVMEYV-GGRSLSWIRFAP---EEELARLFGtggfef 243
Cdd:cd14092  39 VSRRLdTSREVQLLRLCQgHPNIVKL-----HEVFQDELHT-YLVMELLrGGELLERIRKKKrftESEASRIMR------ 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21219970 244 ghvitygcKILGALEYLHDRGLLYCDMKPENVIHY----GREIKVIDLGAIR 291
Cdd:cd14092 107 --------QLVSAVSFMHSKGVVHRDLKPENLLFTdeddDAEIKIVDFGFAR 150
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
126-311 9.82e-07

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: 49.87  E-value: 9.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 126 RVAGHYAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIVTHVQHQVPG-- 203
Cdd:cd14048   3 RFLTDFEPIQCLGRGGFGVVFEAKN-KVDDCNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERPPEgw 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 204 ---DAEPTGYIVMEYVGGRSL-SWIRFAPEEElARlfgtggfEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI-HY 278
Cdd:cd14048  82 qekMDEVYLYIQMQLCRKENLkDWMNRRCTME-SR-------ELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFfSL 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 21219970 279 GREIKVIDLGAIRRID---------------DRSSGLVHTHGYAPPKR 311
Cdd:cd14048 154 DDVVKVGDFGLVTAMDqgepeqtvltpmpayAKHTGQVGTRLYMSPEQ 201
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
137-310 1.05e-06

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: 49.64  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEDTRVPGLhVVLKGLINTGDAVARRAAVEERRSLTTLHHRDIVRIvthvqhqvpGDAEPTG---YIVM 213
Cdd:cd14167  11 LGTGAFSEVVLAEEKRTQKL-VAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVAL---------DDIYESGghlYLIM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 214 EYVGGRSLsWIR-----FAPEEELARLFgtggfefghvitygCKILGALEYLHDRGLLYCDMKPENVIHYGRE----IKV 284
Cdd:cd14167  81 QLVSGGEL-FDRivekgFYTERDASKLI--------------FQILDAVKYLHDMGIVHRDLKPENLLYYSLDedskIMI 145
                       170       180
                ....*....|....*....|....*....
gi 21219970 285 IDLGaIRRIDDRSSGL---VHTHGYAPPK 310
Cdd:cd14167 146 SDFG-LSKIEGSGSVMstaCGTPGYVAPE 173
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
172-379 1.05e-06

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: 49.60  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 172 RRAAV-EERRSLTTLHHRDIVRIV------THVqhqvpgdaeptgYIVMEYVGGRSLSWI----RFAPEEElarlfgtgg 240
Cdd:cd14010  37 KRPEVlNEVRLTHELKHPNVLKFYewyetsNHL------------WLVVEYCTGGDLETLlrqdGNLPESS--------- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 241 fefghVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGReIKVIDLGAIRR---IDDRSSGLVHTHG-YAPPKRERD 314
Cdd:cd14010  96 -----VRKFGRDLVRGLHYIHSKGIIYCDLKPSNILldGNGT-LKLSDFGLARRegeILKELFGQFSDEGnVNKVSKKQA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 315 RRG--------------LDVDSDLYTVGRTLKVLAerAARPAgLAARSFEALIRRA-THPEPAARFRSAAEMSRQLWEVL 379
Cdd:cd14010 170 KRGtpyymapelfqggvHSFASDLWALGCVLYEMF--TGKPP-FVAESFTELVEKIlNEDPPPPPPKVSSKPSPDFKSLL 246
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
237-316 1.06e-06

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: 49.64  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 237 GTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGrEIKVIDLG-AIRRIDDRS-SGLVHTHGYAPPKRE 312
Cdd:cd05630  95 GQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILldDHG-HIRISDLGlAVHVPEGQTiKGRVGTVGYMAPEVV 173

                ....
gi 21219970 313 RDRR 316
Cdd:cd05630 174 KNER 177
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
131-309 1.18e-06

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: 49.49  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDTRVP-GLHVVLKgLINTgdavaRRAAVE--------ERRSLTTLHHRDIVRI--VTHVQH 199
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKSGlKEKVACK-IIDK-----KKAPKDflekflprELEILRKLRHPNIIQVysIFERGS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 200 QVpgdaeptgYIVMEY-VGGRSLSWIRF--APEEELARLFGTggfefghvitygcKILGALEYLHDRGLLYCDMKPENV- 275
Cdd:cd14080  76 KV--------FIFMEYaEHGDLLEYIQKrgALSESQARIWFR-------------QLALAVQYLHSLDIAHRDLKCENIl 134
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 21219970 276 IHYGREIKVIDLGAIRRI-DDRSSGLVHTH----GYAPP 309
Cdd:cd14080 135 LDSNNNVKLSDFGFARLCpDDDGDVLSKTFcgsaAYAAP 173
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
172-288 1.29e-06

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: 49.36  E-value: 1.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 172 RRAAVEERRSLTTLHHRDIVRIVTHVQHQVPgdaeptGYIVMEYVGGRSLSWIRFAPEEELArlfgtggFEFGHVITYGC 251
Cdd:cd14058  30 KKAFEVEVRQLSRVDHPNIIKLYGACSNQKP------VCLVMEYAEGGSLYNVLHGKEPKPI-------YTAAHAMSWAL 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 21219970 252 KILGALEYLH---DRGLLYCDMKPENVIHY--GREIKVIDLG 288
Cdd:cd14058  97 QCAKGVAYLHsmkPKALIHRDLKPPNLLLTngGTVLKICDFG 138
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
137-328 1.41e-06

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 49.19  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEDTR---VPGLHVVLKglintgdAVARRAAVEE--RRSL---TTLHHRDIVRIVTHVQhqvpgDAEPT 208
Cdd:cd14116  13 LGKGKFGNVYLAREKQskfILALKVLFK-------AQLEKAGVEHqlRREVeiqSHLRHPNILRLYGYFH-----DATRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 209 gYIVMEYvggrslswirfAPEEELAR-LFGTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPEN-VIHYGREIKVID 286
Cdd:cd14116  81 -YLILEY-----------APLGTVYReLQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENlLLGSAGELKIAD 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 21219970 287 LG-AIRRIDDRSSGLVHTHGYAPPKRERDRRGlDVDSDLYTVG 328
Cdd:cd14116 149 FGwSVHAPSSRRTTLCGTLDYLPPEMIEGRMH-DEKVDLWSLG 190
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
126-328 2.47e-06

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: 48.52  E-value: 2.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 126 RVAGHYAVLGYLAVGGHGWVYLAE---DTRvpgLHVVLKGLINTGDAVARRAaVEERRSLTTLHHRDIVR-----IVTHV 197
Cdd:cd14046   3 RYLTDFEELQVLGKGAFGQVVKVRnklDGR---YYAIKKIKLRSESKNNSRI-LREVMLLSRLNHQHVVRyyqawIERAN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 198 QhqvpgdaeptgYIVMEYVGGRSLSWI----RFAPEEELARLFGtggfefghvitygcKILGALEYLHDRGLLYCDMKPE 273
Cdd:cd14046  79 L-----------YIQMEYCEKSTLRDLidsgLFQDTDRLWRLFR--------------QILEGLAYIHSQGIIHRDLKPV 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21219970 274 NV-IHYGREIKVIDLG--------------AIRRIDDR-------SSGLVHTHGYAPPKRERDRRG-LDVDSDLYTVG 328
Cdd:cd14046 134 NIfLDSNGNVKIGDFGlatsnklnvelatqDINKSTSAalgssgdLTGNVGTALYVAPEVQSGTKStYNEKVDMYSLG 211
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
145-380 2.48e-06

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: 48.37  E-value: 2.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 145 VYLAEDTrVPGLHVVLKglintgdAVAR----RAAVE----ERRSLTTLHHRDIVRIVtHVQhqvpgDAEPTGYIVMEYV 216
Cdd:cd14009   9 VWKGRHK-QTGEVVAIK-------EISRkklnKKLQEnlesEIAILKSIKHPNIVRLY-DVQ-----KTEDFIYLVLEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 217 GGRSLS-WI--RFAPEEELARLFGTggfefghvitygcKILGALEYLHDRGLLYCDMKPENVIHYGR----EIKVIDLGA 289
Cdd:cd14009  75 AGGDLSqYIrkRGRLPEAVARHFMQ-------------QLASGLKFLRSKNIIHRDLKPQNLLLSTSgddpVLKIADFGF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 290 IRRIDDRSsgLVHT-HG---YAPPKRERDRRgLDVDSDLYTVGrtlKVLAERAARPAGLAARSFEALIRRATHPEPAARF 365
Cdd:cd14009 142 ARSLQPAS--MAETlCGsplYMAPEILQFQK-YDAKADLWSVG---AILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPF 215
                       250
                ....*....|....*
gi 21219970 366 RSAAEMSRQLWEVLR 380
Cdd:cd14009 216 PIAAQLSPDCKDLLR 230
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
137-309 2.60e-06

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: 48.52  E-value: 2.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 137 LAVGGHGWVYLAEDtRVPGLHVVLKgLINTGDAVARRAAVE-ERRSLTTLHHRDIVRIV------THVqhqvpgdaeptg 209
Cdd:cd14083  11 LGTGAFSEVVLAED-KATGKLVAIK-CIDKKALKGKEDSLEnEIAVLRKIKHPNIVQLLdiyeskSHL------------ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYVggrslswirfapeeelarlfgTGGFEFGHVITYGC-----------KILGALEYLHDRGLLYCDMKPENVIHY 278
Cdd:cd14083  77 YLVMELV---------------------TGGELFDRIVEKGSytekdashlirQVLEAVDYLHSLGIVHRDLKPENLLYY 135
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21219970 279 GRE----IKVIDLGaIRRIDDRS--SGLVHTHGYAPP 309
Cdd:cd14083 136 SPDedskIMISDFG-LSKMEDSGvmSTACGTPGYVAP 171
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
237-313 2.75e-06

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: 48.51  E-value: 2.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 237 GTGGFEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGrEIKVIDLGAIRRIDDRSS--GLVHTHGYAPP--- 309
Cdd:cd05605  95 GNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILldDHG-HVRISDLGLAVEIPEGETirGRVGTVGYMAPevv 173

                ....
gi 21219970 310 KRER 313
Cdd:cd05605 174 KNER 177
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
210-288 2.79e-06

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: 48.75  E-value: 2.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYVGGRSLSW-----IRFapEEELARLfgtggfefghvitYGCKILGALEYLHDRGLLYCDMKPENVI-----Hyg 279
Cdd:cd05570  72 YFVMEYVNGGDLMFhiqraRRF--TEERARF-------------YAAEICLALQFLHERGIIYRDLKLDNVLldaegH-- 134

                ....*....
gi 21219970 280 reIKVIDLG 288
Cdd:cd05570 135 --IKIADFG 141
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
131-334 2.98e-06

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: 48.17  E-value: 2.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDTrVPGLHVVLKgLINTgDAVARRAAVEE-RRSLTT---LHHRDIVRIvthvqHQVPGDAE 206
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNT-KTGESVAIK-IIDK-EQVAREGMVEQiKREIAImklLRHPNIVEL-----HEVMATKT 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 207 PTgYIVMEYV-GGRSLSWIRFAP--EEELARLFgtggfeFGHVITygckilgALEYLHDRGLLYCDMKPENVIHYGRE-I 282
Cdd:cd14663  74 KI-FFVMELVtGGELFSKIAKNGrlKEDKARKY------FQQLID-------AVDYCHSRGVFHRDLKPENLLLDEDGnL 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21219970 283 KVIDLG-AIRRIDDRSSGLVHTH----GYAPPKRERdRRGLD-VDSDLYTVGRTLKVL 334
Cdd:cd14663 140 KISDFGlSALSEQFRQDGLLHTTcgtpNYVAPEVLA-RRGYDgAKADIWSCGVILFVL 196
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
211-296 3.59e-06

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: 48.03  E-value: 3.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 211 IVMEYVGGRSLsWIRFAPEE-ELARLfgtggfefgHVITYGCKILGALEYLHDRGLLYCDMKPENVI---HYGREIKVID 286
Cdd:cd14192  78 LIMEYVDGGEL-FDRITDESyQLTEL---------DAILFTRQICEGVHYLHQHYILHLDLKPENILcvnSTGNQIKIID 147
                        90
                ....*....|
gi 21219970 287 LGAIRRIDDR 296
Cdd:cd14192 148 FGLARRYKPR 157
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
246-298 3.90e-06

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: 47.69  E-value: 3.90e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21219970 246 VITYGCKILGALEYLHDRGLLYCDMKPENVI---HYGREIKVIDLGAIRRIDDRSS 298
Cdd:cd14191 102 CIKYMRQISEGVEYIHKQGIVHLDLKPENIMcvnKTGTKIKLIDFGLARRLENAGS 157
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
168-288 3.96e-06

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: 47.72  E-value: 3.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 168 DAVARRAAVEERRSLTTLHHRDIVRI--VTHVQHQVpgdaeptgYIVMEYVGGRSLswirFA--------PEEELARLFG 237
Cdd:cd14075  41 DQKTQRLLSREISSMEKLHHPNIIRLyeVVETLSKL--------HLVMEYASGGEL----YTkistegklSESEAKPLFA 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21219970 238 tggfefghvitygcKILGALEYLHDRGLLYCDMKPENVIHYG-REIKVIDLG 288
Cdd:cd14075 109 --------------QIVSAVKHMHENNIIHRDLKAENVFYASnNCVKVGDFG 146
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
172-294 4.17e-06

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: 47.58  E-value: 4.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 172 RRAAVEERRSLTTLHHRDIVRIVTHVQhqvpgdAEPTGYIVMEYVGGRSLswirfapeeeLARLFGTGGFEFGHVITYGC 251
Cdd:cd14107  42 RARAFQERDILARLSHRRLTCLLDQFE------TRKTLILILELCSSEEL----------LDRLFLKGVVTEAEVKLYIQ 105
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21219970 252 KILGALEYLHDRGLLYCDMKPENV--IHYGRE-IKVIDLGAIRRID 294
Cdd:cd14107 106 QVLEGIGYLHGMNILHLDIKPDNIlmVSPTREdIKICDFGFAQEIT 151
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
212-288 4.32e-06

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: 48.12  E-value: 4.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 212 VMEYVGGRSLSW-----IRFApeEELARLfgtggfefghvitYGCKILGALEYLHDRGLLYCDMKPENVI-----Hygre 281
Cdd:cd05571  73 VMEYVNGGELFFhlsreRVFS--EDRTRF-------------YGAEIVLALGYLHSQGIVYRDLKLENLLldkdgH---- 133

                ....*..
gi 21219970 282 IKVIDLG 288
Cdd:cd05571 134 IKITDFG 140
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
131-295 4.35e-06

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


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 47.65  E-value: 4.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 131 YAVLGYLAVGGHGWVYLAEDtRVPGLHVVLKGLINTGDAVARR-AAVEERRSLTTLHHRDIVRIVTHVQHqvpgdaEPTG 209
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKA-KSDSEHCVIKEIDLTKMPVKEKeASKKEVILLAKMKHPNIVTFFASFQE------NGRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 210 YIVMEYVGGRSLswirfapeeeLARLFGTGG--FEFGHVITYGCKILGALEYLHDRGLLYCDMKPENVI--HYGREIKVI 285
Cdd:cd08225  75 FIVMEYCDGGDL----------MKRINRQRGvlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFlsKNGMVAKLG 144
                       170
                ....*....|
gi 21219970 286 DLGAIRRIDD 295
Cdd:cd08225 145 DFGIARQLND 154
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
158-405 4.71e-06

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: 47.43  E-value: 4.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 158 VVLKGLINTGDAVARRAAV-----------------EERRSLTTLHHRDIVRIV-THVQhqvpgdaEPTGYIVMEYVGGR 219
Cdd:cd06631  16 TVYCGLTSTGQLIAVKQVEldtsdkekaekeyeklqEEVDLLKTLKHVNIVGYLgTCLE-------DNVVSIFMEFVPGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 220 SLSWI--RFAPEEELArlfgtggfefghVITYGCKILGALEYLHDRGLLYCDMKPENVIHYGR-EIKVIDLGAIRRIDDR 296
Cdd:cd06631  89 SIASIlaRFGALEEPV------------FCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNgVIKLIDFGCAKRLCIN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 297 SSGLVHT------HG---YAPPKRERDrRGLDVDSDLYTVGRTLkvlaeraarpaglaarsFEALIRR---ATHPEPAAR 364
Cdd:cd06631 157 LSSGSQSqllksmRGtpyWMAPEVINE-TGHGRKSDIWSIGCTV-----------------FEMATGKppwADMNPMAAI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 21219970 365 FrsaaemsrqlwevlredqALG-GREPYPERSTRFEPTAAVF 405
Cdd:cd06631 219 F------------------AIGsGRKPVPRLPDKFSPEARDF 242
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
170-331 5.22e-06

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 47.73  E-value: 5.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 170 VARRAAVEERRSLTTLH----HRDIVRIvthvqHQVPGDAEPTgYIVMEYVGGRSLSwirfapeEELARLFGTGGFEFGH 245
Cdd:cd14179  40 VSKRMEANTQREIAALKlcegHPNIVKL-----HEVYHDQLHT-FLVMELLKGGELL-------ERIKKKQHFSETEASH 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 246 VITygcKILGALEYLHDRGLLYCDMKPENVIHYGR----EIKVIDLGAIRRIDDRSSGL---VHTHGYAPPKReRDRRGL 318
Cdd:cd14179 107 IMR---KLVSAVSHMHDVGVVHRDLKPENLLFTDEsdnsEIKIIDFGFARLKPPDNQPLktpCFTLHYAAPEL-LNYNGY 182
                       170
                ....*....|...
gi 21219970 319 DVDSDLYTVGRTL 331
Cdd:cd14179 183 DESCDLWSLGVIL 195
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
185-328 5.54e-06

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: 47.23  E-value: 5.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21219970 185 LHHRDIVRIVTHVQhqvpgDAEPTgYIVMEYVGGRSLSWIRFAPEEELARlfgtggfefgHVITYGCKILGALEYLHDRG 264
Cdd:cd14189  58 LHHKHVVKFSHHFE-----DAENI-YIFLELCSRKSLAHIWKARHTLLEP----------EVRYYLKQIISGLKYLHLKG 121
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21219970 265 LLYCDMKPEN-VIHYGREIKVIDLGAIRRI---DDRSSGLVHTHGYAPPKrERDRRGLDVDSDLYTVG 328
Cdd:cd14189 122 ILHRDLKLGNfFINENMELKVGDFGLAARLeppEQRKKTICGTPNYLAPE-VLLRQGHGPESDVWSLG 188