NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|927602445|ref|NP_001300879|]
View 

aurora kinase B isoform 1 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
70-339 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14117:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 270  Bit Score: 539.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  70 RHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd14117    1 RKFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR 229
Cdd:cd14117   81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLR 309
Cdd:cd14117  161 RRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLR 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 927602445 310 HNPSERLPLAQVSAHPWVRANSRRVLPPSA 339
Cdd:cd14117  241 YHPSERLPLKGVMEHPWVKANSRRVLPPVY 270
 
Name Accession Description Interval E-value
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
70-339 0e+00

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 539.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  70 RHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd14117    1 RKFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR 229
Cdd:cd14117   81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLR 309
Cdd:cd14117  161 RRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLR 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 927602445 310 HNPSERLPLAQVSAHPWVRANSRRVLPPSA 339
Cdd:cd14117  241 YHPSERLPLKGVMEHPWVKANSRRVLPPVY 270
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
77-327 1.49e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 276.33  E-value: 1.49e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445    77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH-APSLRRKTMCG 235
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQlDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASH-NETYRRIVKVDLKFP---ASVPMGAQDLISKLLRHN 311
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPppeWDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 927602445   312 PSERLPLAQVSAHPWV 327
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
77-327 1.06e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 199.01  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIeKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  157 APRGELYKELQKSCTFDEQRTATIMEELADALmychgkkvihrdikpenlllglkgelkiadfgwsvhAPSLRRKTMCGT 236
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGL------------------------------------ESGSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  237 LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL---KFPASVPMGAQDLISKLLRHNPS 313
Cdd:pfam00069 124 PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafpELPSNLSEEAKDLLKKLLKKDPS 203
                         250
                  ....*....|....
gi 927602445  314 ERLPLAQVSAHPWV 327
Cdd:pfam00069 204 KRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
74-344 1.49e-57

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 193.69  E-value: 1.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG--WSVHAPSL-RR 230
Cdd:COG0515   86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGiaRALGGATLtQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL----KFPASVPMGAQDLISK 306
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPpppsELRPDLPPALDAIVLR 245
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 927602445 307 LLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA 344
Cdd:COG0515  246 ALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAA 283
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
69-337 1.31e-56

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 186.95  E-value: 1.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  69 TRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEK-EGVEHqLRREIEIQAHLHHPNILRLYNYFYDR 147
Cdd:PTZ00263  12 TSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKmKQVQH-VAQEKSILMELSHPFIVNMMCSFQDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS 227
Cdd:PTZ00263  91 NRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 lRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKL 307
Cdd:PTZ00263 171 -RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGL 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 927602445 308 LRHNPSERL-----PLAQVSAHP------WVRANSRRVLPP 337
Cdd:PTZ00263 250 LQTDHTKRLgtlkgGVADVKNHPyfhganWDKLYARYYPAP 290
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
78-276 6.83e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 93.32  E-value: 6.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQ-------IEKegvehqLRREIEIQAHLHHPNILRLYNYFYDRRRI 150
Cdd:NF033483  10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKVL-RPDlardpefVAR------FRREAQSAASLSHPNIVSVYDVGEDGGIP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPrGELYKE-LQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPS 227
Cdd:NF033483  83 YIVMEYVD-GRTLKDyIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIarALSSTT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 228 LRRK-TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF--ESA 276
Cdd:NF033483 162 MTQTnSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFdgDSP 213
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
103-320 2.55e-19

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: 89.13  E-value: 2.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   103 VALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLynyfYDR-----RRIYLILEYAPRGELYKELQKSCTFDEQRT 177
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVAL----LDSgeappGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   178 ATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAP--------SLRRKT-MCGTLDYLPPEMI 245
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNimvSQTGVRPHAKVLDFGIGTLLPgvrdadvaTLTRTTeVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445   246 EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET-YRRIVKVDLKFP---ASVPMGaqDLISKLLRHNPSERLPLAQ 320
Cdd:TIGR03903  162 RGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEIlYQQLSPVDVSLPpwiAGHPLG--QVLRKALNKDPRQRAASAP 238
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
75-205 3.69e-09

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 58.43  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   75 DDFEIGRPLGKGKFGNVYLAREKKSH-----FIVALKvlfksqiekEGVEHQLRREIEIQAHLHHPNILRLYNyfyDRRR 149
Cdd:NF033442  510 GGFEVRRRLGTGSTSRALLVRDRDADgeervLKVALD---------DEHAARLRAEAEVLGRLRHPRIVALVE---GPLE 577
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  150 I----YLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN 205
Cdd:NF033442  578 IggrtALLLEYAGEQTLAERLRKEGRLSLDLLERFGDDLLSAVVHLEGQGVWHRDIKPDN 637
 
Name Accession Description Interval E-value
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
70-339 0e+00

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 539.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  70 RHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd14117    1 RKFTIDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR 229
Cdd:cd14117   81 IYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLR 309
Cdd:cd14117  161 RRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLR 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 927602445 310 HNPSERLPLAQVSAHPWVRANSRRVLPPSA 339
Cdd:cd14117  241 YHPSERLPLKGVMEHPWVKANSRRVLPPVY 270
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
76-328 2.27e-170

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: 473.89  E-value: 2.27e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCG 235
Cdd:cd14007   81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNRRKTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd14007  161 TLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSKR 240
                        250
                 ....*....|...
gi 927602445 316 LPLAQVSAHPWVR 328
Cdd:cd14007  241 LSLEQVLNHPWIK 253
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
72-327 8.74e-160

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: 447.10  E-value: 8.74e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14116    2 WALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK 231
Cdd:cd14116   82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHN 311
Cdd:cd14116  162 TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHN 241
                        250
                 ....*....|....*.
gi 927602445 312 PSERLPLAQVSAHPWV 327
Cdd:cd14116  242 PSQRPMLREVLEHPWI 257
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
77-327 1.49e-92

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 276.33  E-value: 1.49e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445    77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKD--RERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH-APSLRRKTMCG 235
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQlDPGEKLTTFVG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASH-NETYRRIVKVDLKFP---ASVPMGAQDLISKLLRHN 311
Cdd:smart00220 159 TPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPppeWDISPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 927602445   312 PSERLPLAQVSAHPWV 327
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
76-326 1.03e-85

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: 259.33  E-value: 1.03e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSED-EEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHA-PSLRRK 231
Cdd:cd05117   80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENillASKDPDSPIKIIDFGLAKIFeEGEKLK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQDLISKL 307
Cdd:cd05117  160 TVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDLIKRL 239
                        250
                 ....*....|....*....
gi 927602445 308 LRHNPSERLPLAQVSAHPW 326
Cdd:cd05117  240 LVVDPKKRLTAAEALNHPW 258
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
76-326 6.13e-85

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: 257.06  E-value: 6.13e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEK-IKREIEIMKLLNHPNIIKLYEVIETENKIYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHAPSLRRKTMC 234
Cdd:cd14003   80 YASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSnEFRGGSLLKTFC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd14003  160 GTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPS 239
                        250
                 ....*....|...
gi 927602445 314 ERLPLAQVSAHPW 326
Cdd:cd14003  240 KRITIEEILNHPW 252
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
83-326 3.34e-79

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: 242.42  E-value: 3.34e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS--LRRKTMCGTLDYL 240
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSdgDRTYTFCGTPEYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL---P 317
Cdd:cd05123  161 APEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLgsgG 240

                 ....*....
gi 927602445 318 LAQVSAHPW 326
Cdd:cd05123  241 AEEIKAHPF 249
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
75-326 2.07e-74

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


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 230.13  E-value: 2.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14099    1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKT 232
Cdd:cd14099   81 ELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAarLEYDGERKKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMG--AQDLISKLLR 309
Cdd:cd14099  161 LCGTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLSISdeAKDLIRSMLQ 240
                        250
                 ....*....|....*..
gi 927602445 310 HNPSERLPLAQVSAHPW 326
Cdd:cd14099  241 PDPTKRPSLDEILSHPF 257
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
75-326 3.43e-72

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: 225.17  E-value: 3.43e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQDESKLYFVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG-------------- 220
Cdd:cd05581   81 EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvlgpdsspest 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 -----WSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPAS 295
Cdd:cd05581  161 kgdadSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPEN 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 927602445 296 VPMGAQDLISKLLRHNPSERL------PLAQVSAHPW 326
Cdd:cd05581  241 FPPDAKDLIQKLLVLDPSKRLgvnengGYDELKAHPF 277
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
76-326 5.46e-66

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: 208.80  E-value: 5.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTM-- 233
Cdd:cd14663   81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRQDGLlh 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 --CGTLDYLPPEMIEGRMHN-EKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRH 310
Cdd:cd14663  161 ttCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDP 240
                        250
                 ....*....|....*.
gi 927602445 311 NPSERLPLAQVSAHPW 326
Cdd:cd14663  241 NPSTRITVEQIMASPW 256
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
75-337 4.29e-65

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: 207.43  E-value: 4.29e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIiKLKQVEH-VLNEKRILSEVRHPFIVNLLGSFQDDRNLYMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSlRRKTM 233
Cdd:cd05580   80 MEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD-RTYTL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd05580  159 CGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVVDLT 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 314 ERLPL-----AQVSAHPWVRA------NSRRVLPP 337
Cdd:cd05580  239 KRLGNlkngvEDIKNHPWFAGidwdalLQRKIPAP 273
Pkinase pfam00069
Protein kinase domain;
77-327 1.06e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 199.01  E-value: 1.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIeKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKI-KKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  157 APRGELYKELQKSCTFDEQRTATIMEELADALmychgkkvihrdikpenlllglkgelkiadfgwsvhAPSLRRKTMCGT 236
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGL------------------------------------ESGSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  237 LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL---KFPASVPMGAQDLISKLLRHNPS 313
Cdd:pfam00069 124 PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYafpELPSNLSEEAKDLLKKLLKKDPS 203
                         250
                  ....*....|....
gi 927602445  314 ERLPLAQVSAHPWV 327
Cdd:pfam00069 204 KRLTATQALQHPWF 217
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
75-327 9.50e-61

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


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 195.46  E-value: 9.50e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14186    1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRK 231
Cdd:cd14186   81 EMCHNGEMSRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQlkMPHEKHF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHN 311
Cdd:cd14186  161 TMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKN 240
                        250
                 ....*....|....*.
gi 927602445 312 PSERLPLAQVSAHPWV 327
Cdd:cd14186  241 PADRLSLSSVLDHPFM 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
77-327 1.58e-60

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 194.78  E-value: 1.58e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14081    3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW-SVHAPSLRRKTMCG 235
Cdd:cd14081   83 VSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMaSLQPEGSLLETSCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGR-MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSE 314
Cdd:cd14081  163 SPHYACPEVIKGEkYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPEK 242
                        250
                 ....*....|...
gi 927602445 315 RLPLAQVSAHPWV 327
Cdd:cd14081  243 RITIEEIKKHPWF 255
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
83-326 3.72e-60

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: 193.98  E-value: 3.72e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQR----TATIMEeladALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR-KTMCGTL 237
Cdd:cd05572   81 WTILRDRGLFDEYTarfyTACVVL----AFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKtWTFCGTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN--ETYRRIVKV--DLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd05572  157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPE 236
                        250
                 ....*....|....*...
gi 927602445 314 ERLPLAQVSA-----HPW 326
Cdd:cd05572  237 ERLGYLKGGIrdikkHKW 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
85-326 4.48e-60

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: 193.97  E-value: 4.48e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  85 KGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYK 164
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 165 ELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-----------------VHAPS 227
Cdd:cd05579   83 LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSkvglvrrqiklsiqkksNGAPE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMG--AQDLIS 305
Cdd:cd05579  163 KEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDPEVSdeAKDLIS 242
                        250       260
                 ....*....|....*....|....
gi 927602445 306 KLLRHNPSERL---PLAQVSAHPW 326
Cdd:cd05579  243 KLLTPDPEKRLgakGIEEIKNHPF 266
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
77-327 1.33e-59

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


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 192.22  E-value: 1.33e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR-RKTMCG 235
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKlLQTFCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGR-MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASvPMGAQDLISKLLRHNPSE 314
Cdd:cd14073  163 SPLYASPEIVNGTpYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQ-PSDASGLIRWMLTVNPKR 241
                        250
                 ....*....|...
gi 927602445 315 RLPLAQVSAHPWV 327
Cdd:cd14073  242 RATIEDIANHWWV 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
76-327 4.07e-59

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: 190.88  E-value: 4.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKI---NLESKEKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSC-TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH-APSLRRKTM 233
Cdd:cd05122   78 FCSGGSLKDLLKNTNkTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQlSDGKTRNTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF-ESASHnETYRRIVKVDL-KFPASVPMGA--QDLISKLLR 309
Cdd:cd05122  158 VGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYsELPPM-KALFLIATNGPpGLRNPKKWSKefKDFLKKCLQ 236
                        250
                 ....*....|....*...
gi 927602445 310 HNPSERLPLAQVSAHPWV 327
Cdd:cd05122  237 KDPEKRPTAEQLLKHPFI 254
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
83-327 3.91e-58

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: 188.92  E-value: 3.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEK-----------EGVEHQLRREIEIQAHLHHPNILRLYNYFYD--RRR 149
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLRKrregkndrgkiKNALDDVRREIAIMKKLDHPNIVRLYEVIDDpeSDK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYK--ELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHA 225
Cdd:cd14008   81 LYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSemFED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCGTLDYLPPEMIEGRM---HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPM--GA 300
Cdd:cd14008  161 GNDTLQKTAGTPAFLAPELCDGDSktySGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPPELspEL 240
                        250       260
                 ....*....|....*....|....*..
gi 927602445 301 QDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14008  241 KDLLRRMLEKDPEKRITLKEIKEHPWV 267
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
83-325 1.18e-57

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: 185.94  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKL--LEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS----LRRKTMCGTL 237
Cdd:cd00180   79 KDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSddslLKTTGGTTPP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELlvgnppfesashnetyrrivkvdlkfpasvpMGAQDLISKLLRHNPSERLP 317
Cdd:cd00180  159 YYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRPS 207

                 ....*...
gi 927602445 318 LAQVSAHP 325
Cdd:cd00180  208 AKELLEHL 215
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
74-344 1.49e-57

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 193.69  E-value: 1.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:COG0515    6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG--WSVHAPSL-RR 230
Cdd:COG0515   86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGiaRALGGATLtQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL----KFPASVPMGAQDLISK 306
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPpppsELRPDLPPALDAIVLR 245
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 927602445 307 LLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA 344
Cdd:COG0515  246 ALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAA 283
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
83-326 1.19e-56

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: 184.35  E-value: 1.19e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQE-NLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVH-APSLRRKTMCGTLD 238
Cdd:cd14009   80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNlllSTSGDDPVLKIADFGFARSlQPASMAETLCGSPL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGA----QDLISKLLRHNPSE 314
Cdd:cd14009  160 YMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPFPIAAQLspdcKDLLRRLLRRDPAE 239
                        250
                 ....*....|..
gi 927602445 315 RLPLAQVSAHPW 326
Cdd:cd14009  240 RISFEEFFAHPF 251
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
69-337 1.31e-56

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 186.95  E-value: 1.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  69 TRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEK-EGVEHqLRREIEIQAHLHHPNILRLYNYFYDR 147
Cdd:PTZ00263  12 TSSWKLSDFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKmKQVQH-VAQEKSILMELSHPFIVNMMCSFQDE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS 227
Cdd:PTZ00263  91 NRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 lRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKL 307
Cdd:PTZ00263 171 -RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGL 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 927602445 308 LRHNPSERL-----PLAQVSAHP------WVRANSRRVLPP 337
Cdd:PTZ00263 250 LQTDHTKRLgtlkgGVADVKNHPyfhganWDKLYARYYPAP 290
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
77-320 2.24e-56

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: 183.94  E-value: 2.24e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR---KTM 233
Cdd:cd14014   82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLtqtGSV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLK----FPASVPMGAQDLISKLLR 309
Cdd:cd14014  162 LGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPppspLNPDVPPALDAIILRALA 241
                        250
                 ....*....|.
gi 927602445 310 HNPSERLPLAQ 320
Cdd:cd14014  242 KDPEERPQSAA 252
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
75-337 4.00e-56

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


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 186.34  E-value: 4.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRAERDILADADSPWIVRLHYAFQDEDHLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV----------- 223
Cdd:cd05573   81 EYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTkmnksgdresy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 ----------------HAPSLRRKTMC----GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYR 283
Cdd:cd05573  161 lndsvntlfqdnvlarRRPHKQRRVRAysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYS 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 927602445 284 RIV--KVDLKFPASVPMG--AQDLISKLLRhNPSERL-PLAQVSAHPWVR----ANSRRVLPP 337
Cdd:cd05573  241 KIMnwKESLVFPDDPDVSpeAIDLIRRLLC-DPEDRLgSAEEIKAHPFFKgidwENLRESPPP 302
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
77-327 2.88e-55

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: 181.23  E-value: 2.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFI--VALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTKSGLKekVACKIIDKKKAPKDFLEKFLPRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR---- 230
Cdd:cd14080   82 EYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGdvls 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKV-DLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPM---GAQDLISK 306
Cdd:cd14080  162 KTFCGSAAYAAPEILQGIPYDPKKyDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPSSVKKlspECKDLIDQ 241
                        250       260
                 ....*....|....*....|.
gi 927602445 307 LLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14080  242 LLEPDPTKRATIEEILNHPWL 262
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
75-337 9.22e-55

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: 181.09  E-value: 9.22e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWsvhAPSLRRK--T 232
Cdd:cd05612   81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGF---AKKLRDRtwT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNP 312
Cdd:cd05612  158 LCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDR 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 927602445 313 SERL-----PLAQVSAHPWVR------ANSRRVLPP 337
Cdd:cd05612  238 TRRLgnmknGADDVKNHRWFKsvdwddVPQRKLKPP 273
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
77-326 1.71e-54

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 179.06  E-value: 1.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCK--GKEHMIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWSVHAPSLRRkT 232
Cdd:cd14095   80 VKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENllvvEHEDGSKSLKLADFGLATEVKEPLF-T 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN--ETYRRIVKVDLKFPA----SVPMGAQDLISK 306
Cdd:cd14095  159 VCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDqeELFDLILAGEFEFLSpywdNISDSAKDLISR 238
                        250       260
                 ....*....|....*....|
gi 927602445 307 LLRHNPSERLPLAQVSAHPW 326
Cdd:cd14095  239 MLVVDPEKRYSAGQVLDHPW 258
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
75-327 2.54e-54

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 178.60  E-value: 2.54e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKS-QIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRgKSEKE--LRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWsvhAPSLRRKTM 233
Cdd:cd14002   79 TEYA-QGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGF---ARAMSCNTL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 C-----GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd14002  155 VltsikGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLL 234
                        250
                 ....*....|....*....
gi 927602445 309 RHNPSERLPLAQVSAHPWV 327
Cdd:cd14002  235 NKDPSKRLSWPDLLEHPFV 253
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
77-326 5.49e-53

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


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 175.52  E-value: 5.49e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLK--GKEDMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWSVHA--PSLrr 230
Cdd:cd14185   80 VRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENllvqHNPDKSTTLKLADFGLAKYVtgPIF-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 kTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN--ETYRRIVKVDLKFPA----SVPMGAQDLI 304
Cdd:cd14185  158 -TVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDqeELFQIIQLGHYEFLPpywdNISEAAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14185  237 SRLLVVDPEKRYTAKQVLQHPW 258
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
83-337 8.73e-53

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: 176.64  E-value: 8.73e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQL--RREIEIQAHlhHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIKVLKKEVIiEDDDVECTMteKRVLALANR--HPFLTGLHACFQTEDRLYFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------WsvhaPSLRRKTM 233
Cdd:cd05570   81 GDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGmckegiW----GGNTTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd05570  157 CGTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPA 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 314 ERL---PL--AQVSAHP------WVRANSRRVLPP 337
Cdd:cd05570  237 RRLgcgPKgeADIKAHPffrnidWDKLEKKEVEPP 271
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
74-326 1.05e-52

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 174.38  E-value: 1.05e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14079    1 IGNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvhapSLRR--- 230
Cdd:cd14079   81 MEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLS----NIMRdge 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 --KTMCGTLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKL 307
Cdd:cd14079  157 flKTSCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRM 236
                        250
                 ....*....|....*....
gi 927602445 308 LRHNPSERLPLAQVSAHPW 326
Cdd:cd14079  237 LVVDPLKRITIPEIRQHPW 255
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
76-325 2.84e-52

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: 173.42  E-value: 2.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKERE-EALNEVKLLSKLKHPNIVKYYESFEENGKLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCT----FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-------VH 224
Cdd:cd08215   80 YADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISkvlesttDL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 ApslrrKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL-KFPASVPMGAQDL 303
Cdd:cd08215  160 A-----KTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYpPIPSQYSSELRDL 234
                        250       260
                 ....*....|....*....|..
gi 927602445 304 ISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd08215  235 VNSMLQKDPEKRPSANEILSSP 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
76-326 4.86e-52

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: 173.05  E-value: 4.86e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQL-RREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLfQREINILKSLEHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN--LLLGLKGELKIADFGWS--VHAPSLrR 230
Cdd:cd14098   81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENilITQDDPVIVKISDFGLAkvIHTGTF-L 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNE------KVDLWCIGVLCYELLVGNPPFESASHNETYRRI------VKVDLKFPASvPM 298
Cdd:cd14098  160 VTFCGTMAYLAPEILMSKEQNLqggysnLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIrkgrytQPPLVDFNIS-EE 238
                        250       260
                 ....*....|....*....|....*...
gi 927602445 299 GaQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14098  239 A-IDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
77-326 1.97e-51

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


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 171.29  E-value: 1.97e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKYMNKQKCIEKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH-APSLRRKTMCG 235
Cdd:cd05578   82 LLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKlTDGTLATSTSG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFE---SASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNP 312
Cdd:cd05578  162 TKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEihsRTSIEEIRAKFETASVLYPAGWSEEAIDLINKLLERDP 241
                        250
                 ....*....|....*
gi 927602445 313 SERLP-LAQVSAHPW 326
Cdd:cd05578  242 QKRLGdLSDLKNHPY 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
76-327 2.92e-50

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 168.28  E-value: 2.92e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14069    2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPE-NIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWsvhAPSLRRK---- 231
Cdd:cd14069   81 YASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGL---ATVFRYKgker 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 ---TMCGTLDYLPPEMIEGRMHN-EKVDLWCIGVLCYELLVGNPPFESASHN----ETYRRIVKVDLKFPASVPMGAQDL 303
Cdd:cd14069  158 llnKMCGTLPYVAPELLAKKKYRaEPVDVWSCGIVLFAMLAGELPWDQPSDScqeySDWKENKKTYLTPWKKIDTAALSL 237
                        250       260
                 ....*....|....*....|....
gi 927602445 304 ISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14069  238 LRKILTENPNKRITIEDIKKHPWY 261
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
80-324 6.06e-50

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: 167.41  E-value: 6.06e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd14189    6 GRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRKTMCGTL 237
Cdd:cd14189   86 KSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARlePPEQRKKTICGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLP 317
Cdd:cd14189  166 NYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLT 245

                 ....*..
gi 927602445 318 LAQVSAH 324
Cdd:cd14189  246 LDQILEH 252
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
75-328 2.00e-49

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: 167.20  E-value: 2.00e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEK-EGVEHQLRREIEIQAhLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKlKQVEHTLNEKRILQA-INFPFLVKLEYSFKDNSNLYMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSlRRKTM 233
Cdd:cd14209   80 MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG-RTWTL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd14209  159 CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLT 238
                        250       260
                 ....*....|....*....|
gi 927602445 314 ERL-----PLAQVSAHPWVR 328
Cdd:cd14209  239 KRFgnlknGVNDIKNHKWFA 258
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
83-337 8.24e-49

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: 166.38  E-value: 8.24e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd05571    3 LGKGTFGKVILCREKATGELYAIKILKKEVIiAKDEVAHTLT-ENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR--KTMCGTLDY 239
Cdd:cd05571   82 LFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGAttKTFCGTPEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL--- 316
Cdd:cd05571  162 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKRLggg 241
                        250       260
                 ....*....|....*....|....*....
gi 927602445 317 --PLAQVSAHPWVRANS------RRVLPP 337
Cdd:cd05571  242 prDAKEIMEHPFFASINwddlyqKKIPPP 270
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
75-328 1.35e-48

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 165.49  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05574    1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLPTLYASFQTSTHLCFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQK---SCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA------ 225
Cdd:cd05574   81 DYCPGGELFRLLQKqpgKR-LPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSsvtppp 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 -------------------------PSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNE 280
Cdd:cd05574  160 vrkslrkgsrrssvksieketfvaePSARSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRDE 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 927602445 281 TYRRIVKVDLKFPASVPMGAQ--DLISKLLRHNPSERL----PLAQVSAHPWVR 328
Cdd:cd05574  240 TFSNILKKELTFPESPPVSSEakDLIRKLLVKDPSKRLgskrGASEIKRHPFFR 293
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
75-326 4.29e-48

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: 162.54  E-value: 4.29e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14083    3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALK--GKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAPSLRRK 231
Cdd:cd14083   81 ELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENllyYSPDEDSKIMISDFGLSKMEDSGVMS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKL 307
Cdd:cd14083  161 TACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEYEFDSpywdDISDSAKDFIRHL 240
                        250
                 ....*....|....*....
gi 927602445 308 LRHNPSERLPLAQVSAHPW 326
Cdd:cd14083  241 MEKDPNKRYTCEQALEHPW 259
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
75-328 1.17e-47

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 161.61  E-value: 1.17e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEgveHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIhVDGDEEFR---KQLLRELKTLRSCESPYVVKCYGAFYKEGEISIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPS--LRR 230
Cdd:cd06623   78 LEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENtlDQC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN---ETYRRIVKVDLKFPASVPMGAQ--DLIS 305
Cdd:cd06623  158 NTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPsffELMQAICDGPPPSLPAEEFSPEfrDFIS 237
                        250       260
                 ....*....|....*....|...
gi 927602445 306 KLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd06623  238 ACLQKDPKKRPSAAELLQHPFIK 260
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
77-327 1.20e-47

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


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 161.43  E-value: 1.20e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAH-LFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL-LGLKGELKIADFGWSVH-APSLRRKTM 233
Cdd:cd14074   84 GDGGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVfFEKQGLVKLTDFGFSNKfQPGEKLETS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNE-KVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNP 312
Cdd:cd14074  164 CGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIRDP 243
                        250
                 ....*....|....*
gi 927602445 313 SERLPLAQVSAHPWV 327
Cdd:cd14074  244 KKRASLEEIENHPWL 258
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
83-316 1.30e-47

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 163.26  E-value: 1.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEG-VEHQL-RREIEIQaHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNeVKHIMaERNVLLK-NVKHPFLVGLHYSFQTKDKLYFVLDYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRKTMCGTLD 238
Cdd:cd05575   82 ELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEgiEPSDTTSTFCGTPE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL 316
Cdd:cd05575  162 YLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRL 239
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
83-326 2.00e-47

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: 160.51  E-value: 2.00e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKRDKKKE----AVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN--LLLGLKGELKIADFGWSVH-APSLRRKTMCGTLDY 239
Cdd:cd14006   77 LDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENilLADRPSPQIKIIDFGLARKlNPGEELKEIFGTPEF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKF----PASVPMGAQDLISKLLRHNPSER 315
Cdd:cd14006  157 VAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFseeyFSSVSQEAKDFIRKLLVKEPRKR 236
                        250
                 ....*....|.
gi 927602445 316 LPLAQVSAHPW 326
Cdd:cd14006  237 PTAQEALQHPW 247
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
75-327 2.36e-47

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: 160.96  E-value: 2.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALE--GKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL---LLGLKGELKIADFGWS-VHAPSLRR 230
Cdd:cd14167   81 QLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLlyySLDEDSKIMISDFGLSkIEGSGSVM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISK 306
Cdd:cd14167  161 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSpywdDISDSAKDFIQH 240
                        250       260
                 ....*....|....*....|.
gi 927602445 307 LLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14167  241 LMEKDPEKRFTCEQALQHPWI 261
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
83-337 4.61e-47

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: 161.80  E-value: 4.61e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAR---EKKSHFIVALKVLFKSQI--EKEGVEHQlRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd05584    4 LGKGGYGKVFQVRkttGSDKGKIFAMKVLKKASIvrNQKDTAHT-KAERNILEAVKHPFIVDLHYAFQTGGKLYLILEYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW---SVHAPSLRRkTMC 234
Cdd:cd05584   83 SGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLckeSIHDGTVTH-TFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSE 314
Cdd:cd05584  162 GTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVSS 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 315 RL-----PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05584  242 RLgsgpgDAEEIKAHPffrhinWDDLLAKKVEPP 275
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
77-327 5.03e-47

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 159.61  E-value: 5.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQ-KLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHAPSLRRKTMCG 235
Cdd:cd14072   81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSnEFTPGNKLDTFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHN-EKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSE 314
Cdd:cd14072  161 SPPYAAPELFQGKKYDgPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSK 240
                        250
                 ....*....|...
gi 927602445 315 RLPLAQVSAHPWV 327
Cdd:cd14072  241 RGTLEQIMKDRWM 253
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
83-326 5.05e-47

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: 159.70  E-value: 5.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEGVEHqlrrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIkCRKAKDREDVRN----EIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKE-LQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL--LLGLKGELKIADFGWS-VHAPSLRRKTMCGTL 237
Cdd:cd14103   77 LFERvVDDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENIlcVSRTGNQIKIIDFGLArKYDPDKKLKVLFGTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKLLRHNPS 313
Cdd:cd14103  157 EFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDFDDeafdDISDEAKDFISKLLVKDPR 236
                        250
                 ....*....|...
gi 927602445 314 ERLPLAQVSAHPW 326
Cdd:cd14103  237 KRMSAAQCLQHPW 249
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
77-327 6.29e-47

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


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 159.73  E-value: 6.29e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHfIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDSSGR-LVAIKSIRKDRIKDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHAPSLRRKTMCG 235
Cdd:cd14161   84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSnLYNQDKFLQTYCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPaSVPMGAQDLISKLLRHNPSE 314
Cdd:cd14161  164 SPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREP-TKPSDACGLIRWLLMVNPER 242
                        250
                 ....*....|...
gi 927602445 315 RLPLAQVSAHPWV 327
Cdd:cd14161  243 RATLEDVASHWWV 255
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
77-327 9.04e-47

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 160.29  E-value: 9.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAR-EKKSHFIVALKVLFK---SQIEKEGVE-HQLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVpLRNTGKPVAIKVVRKadlSSDNLKGSSrANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELK---------------- 215
Cdd:cd14096   83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEPIPFIPsivklrkadddetkvd 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 216 -----------------IADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASH 278
Cdd:cd14096  163 egefipgvggggigivkLADFGLSKQVWDSNTKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFYDESI 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 927602445 279 NETYRRIVKVDLKFPA----SVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14096  243 ETLTEKISRGDYTFLSpwwdEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
83-326 1.44e-46

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


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 158.61  E-value: 1.44e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHF-IVALKVLFKSQIEKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14121    3 LGSGTYATVYKAYRKSGAReVVAVKCVSKSSLNKASTEN-LLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN--LLLGLKGELKIADFGWSVH-APSLRRKTMCGTLD 238
Cdd:cd14121   82 LSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNllLSSRYNPVLKLADFGFAQHlKPNDEAHSLRGSPL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVD-LKFPASVPMGA--QDLISKLLRHNPSER 315
Cdd:cd14121  162 YMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRPELSAdcRDLLLRLLQRDPDRR 241
                        250
                 ....*....|.
gi 927602445 316 LPLAQVSAHPW 326
Cdd:cd14121  242 ISFEEFFAHPF 252
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
77-327 1.49e-46

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 158.87  E-value: 1.49e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVK-LLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL-------KIADFGWSVHAPSLR 229
Cdd:cd14097   82 CEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSIIDnndklniKVTDFGLSVQKYGLG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 R---KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQD 302
Cdd:cd14097  162 EdmlQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAAKN 241
                        250       260
                 ....*....|....*....|....*
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14097  242 VLQQLLKVDPAHRMTASELLDNPWI 266
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
83-337 1.98e-46

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 160.04  E-value: 1.98e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIvSRSEVTHTLA-ERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV--HAPSLRRKTMCGTLDY 239
Cdd:cd05585   81 LFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKlnMKDDDKTNTFCGTPEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPL- 318
Cdd:cd05585  161 LAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYn 240
                        250       260
                 ....*....|....*....|....*..
gi 927602445 319 --AQVSAHP------WVRANSRRVLPP 337
Cdd:cd05585  241 gaQEIKNHPffdqidWKRLLMKKIQPP 267
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
75-328 2.05e-46

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


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 160.09  E-value: 2.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-IEKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEmLEKEQVAH-VRAERDILAEADNPWVVKLYYSFQDEENLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHapsLRRKTM 233
Cdd:cd05599   80 MEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTG---LKKSHL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 C----GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPASVPMG--AQDLIS 305
Cdd:cd05599  157 AystvGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPEVPISpeAKDLIE 236
                        250       260
                 ....*....|....*....|....*.
gi 927602445 306 KLLrHNPSERL---PLAQVSAHPWVR 328
Cdd:cd05599  237 RLL-CDAEHRLganGVEEIKSHPFFK 261
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
77-327 2.15e-46

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: 158.23  E-value: 2.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRR---- 230
Cdd:cd14162   82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFarGVMKTKDGKpkls 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKV-DLWCIGVLCYELLVGNPPFESASHNETYRRIVKvDLKFPASVPMG--AQDLISKL 307
Cdd:cd14162  162 ETYCGSYAYASPEILRGIPYDPFLsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR-RVVFPKNPTVSeeCKDLILRM 240
                        250       260
                 ....*....|....*....|
gi 927602445 308 LRHNPsERLPLAQVSAHPWV 327
Cdd:cd14162  241 LSPVK-KRITIEEIKRDPWF 259
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
76-327 2.63e-46

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: 158.07  E-value: 2.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELE-ALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH----APSLRRK 231
Cdd:cd06606   80 YVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRlaeiATGEGTK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET--YrRIVKVDLK--FPASVPMGAQDLISKL 307
Cdd:cd06606  160 SLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAalF-KIGSSGEPppIPEHLSEEAKDFLRKC 238
                        250       260
                 ....*....|....*....|
gi 927602445 308 LRHNPSERLPLAQVSAHPWV 327
Cdd:cd06606  239 LQRDPKKRPTADELLQHPFL 258
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
77-326 2.64e-46

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


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 157.94  E-value: 2.64e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLK-KIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHAPSLRRKTMCG 235
Cdd:cd14071   81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSnFFKPGELLKTWCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHN-EKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSE 314
Cdd:cd14071  161 SPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSK 240
                        250
                 ....*....|..
gi 927602445 315 RLPLAQVSAHPW 326
Cdd:cd14071  241 RLTIEQIKKHKW 252
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
82-337 3.15e-46

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: 159.39  E-value: 3.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  82 PLGKGKFGNVYLAREKKSHFIVALKVLFKsqiekegvEHQLRREIEIQAHLH-HPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd14092   13 ALGDGSFSVCRKCVHKKTGQEFAVKIVSR--------RLDTSREVQLLRLCQgHPNIVKLHEVFQDELHTYLVMELLRGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWS-VHAPSLRRKTMCGT 236
Cdd:cd14092   85 ELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENllfTDEDDDAEIKIVDFGFArLKPENQPLKTPCFT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 LDYLPPEMIEGRM----HNEKVDLWCIGVLCYELLVGNPPFESASHN----ETYRRIVKVDLKFPA----SVPMGAQDLI 304
Cdd:cd14092  165 LPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSFDGeewkNVSSEAKSLI 244
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPWVRANSRRVLPP 337
Cdd:cd14092  245 QGLLTVDPSKRLTMSELRNHPWLQGSSSPSSTP 277
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
83-337 8.60e-46

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 158.33  E-value: 8.60e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSH---FIVALKVLFKSQIEkegVEHQLRREIE--IQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd05582    3 LGQGSFGKVFLVRKITGPdagTLYAMKVLKKATLK---VRDRVRTKMErdILADVNHPFIVKLHYAFQTEGKLYLILDFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT--MCG 235
Cdd:cd05582   80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAysFCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd05582  160 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANR 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 316 L-----PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05582  240 LgagpdGVEEIKRHPffatidWNKLYRKEIKPP 272
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
111-326 9.80e-46

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 156.75  E-value: 9.80e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 111 SQIEKEGVEHQLRREIEIQAHLH-HPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALM 189
Cdd:cd14093   44 SENEAEELREATRREIEILRQVSgHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVE 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 190 YCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH-APSLRRKTMCGTLDYLPPEMIEGRM------HNEKVDLWCIGVL 262
Cdd:cd14093  124 FLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRlDEGEKLRELCGTPGYLAPEVLKCSMydnapgYGKEVDMWACGVI 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 263 CYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14093  204 MYTLLAGCPPFWHRKQMVMLRNIMEGKYEFGspewDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
81-328 1.22e-45

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 156.49  E-value: 1.22e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-IEKEGVEHQL--RREIEIQAHlhHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd05611    2 KPISKGAFGSVYLAKKRSTGDYFAIKVLKKSDmIAKNQVTNVKaeRAIMMIQGE--SPYVAKLYYSFQSKDYLYLVMEYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRR--KTMCG 235
Cdd:cd05611   80 NGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLS-RNGLEKRhnKKFVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMG----AQDLISKLLRHN 311
Cdd:cd05611  159 TPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFcspeAVDLINRLLCMD 238
                        250       260
                 ....*....|....*....|
gi 927602445 312 PSERLP---LAQVSAHPWVR 328
Cdd:cd05611  239 PAKRLGangYQEIKSHPFFK 258
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
80-324 1.26e-45

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 156.33  E-value: 1.26e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd14188    6 GKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSL--RRKTMCGTL 237
Cdd:cd14188   86 RSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLehRRRTICGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLP 317
Cdd:cd14188  166 NYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDRPS 245

                 ....*..
gi 927602445 318 LAQVSAH 324
Cdd:cd14188  246 LDEIIRH 252
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
81-337 4.11e-45

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 156.99  E-value: 4.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDVIlQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA--PSLRRKTMCGTL 237
Cdd:cd05590   81 GDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGifNGKTTSTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL- 316
Cdd:cd05590  161 DYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLg 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 927602445 317 PLAQ-----VSAHP------WVRANSRRVLPP 337
Cdd:cd05590  241 SLTLggeeaILRHPffkeldWEKLNRRQIEPP 272
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
83-337 5.93e-45

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


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 156.32  E-value: 5.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEVIiAKDEVAHTVT-ESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS--LRRKTMCGTLDY 239
Cdd:cd05595   82 LFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITdgATMKTFCGTPEY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL--- 316
Cdd:cd05595  162 LAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLggg 241
                        250       260
                 ....*....|....*....|....*....
gi 927602445 317 --PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05595  242 psDAKEVMEHRfflsinWQDVVQKKLLPP 270
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
74-327 6.64e-45

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: 154.86  E-value: 6.64e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEH-----QLRREIEIQAHLHHPNILRLYNYFYDRR 148
Cdd:cd14084    5 RKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREinkprNIETEIEILKKLSHPCIIKIEDFFDAED 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 RIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWS--V 223
Cdd:cd14084   85 DYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENvllSSQEEECLIKITDFGLSkiL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLrRKTMCGTLDYLPPEMI--EGRM-HNEKVDLWCIGVLCYELLVGNPPFESASHNETYR-RIVKVDLKFPA----S 295
Cdd:cd14084  165 GETSL-MKTLCGTPTYLAPEVLrsFGTEgYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKeQILSGKYTFIPkawkN 243
                        250       260       270
                 ....*....|....*....|....*....|..
gi 927602445 296 VPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14084  244 VSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
75-343 1.09e-44

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 154.98  E-value: 1.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVehqlRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14085    3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKL-KKTVDKKIV----RTEIGVLLRLSHPNIIKLKEIFETPTEISLVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAP-SLRR 230
Cdd:cd14085   78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENllyATPAPDAPLKIADFGLSKIVDqQVTM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF-ESASHNETYRRIVKVDLKFPA----SVPMGAQDLIS 305
Cdd:cd14085  158 KTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILNCDYDFVSpwwdDVSLNAKDLVK 237
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 927602445 306 KLLRHNPSERLPLAQVSAHPWVRA-NSRRVLPPSALQSV 343
Cdd:cd14085  238 KLIVLDPKKRLTTQQALQHPWVTGkAANFAHMDTAQKKL 276
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
83-341 1.26e-44

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 154.38  E-value: 1.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14166   11 LGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDS---SLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDY 239
Cdd:cd14166   88 FDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENllyLTPDENSKIMITDFGLSKMEQNGIMSTACGTPGY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKLLRHNPSER 315
Cdd:cd14166  168 VAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESpfwdDISESAKDFIRHLLEKNPSKR 247
                        250       260
                 ....*....|....*....|....*....
gi 927602445 316 LPLAQVSAHPWVRANS---RRVLPPSALQ 341
Cdd:cd14166  248 YTCEKALSHPWIIGNTalhRDIYPSVSEQ 276
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
76-327 2.49e-44

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


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 152.93  E-value: 2.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRREIEIQAHL-------HHPNILRLYNYFYDR 147
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlVDTWVRDRKLGTVPLEIHIldtlnkrSHPNIVKLLDFFEDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEyaPRGE---LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH 224
Cdd:cd14004   81 EFYYLVME--KHGSgmdLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTMCGTLDYLPPEMIEGRMHNEK-VDLWCIGVLCYELLVGNPPFESASHnetyrrIVKVDLKFPASVPMGAQDL 303
Cdd:cd14004  159 IKSGPFDTFVGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSEDLIDL 232
                        250       260
                 ....*....|....*....|....
gi 927602445 304 ISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14004  233 ISRMLNRDVGDRPTIEELLTDPWL 256
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
77-327 2.51e-44

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: 152.88  E-value: 2.51e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLA-----REKkshfiVALKVLFKSQIEKEgVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGihqltKEK-----VAIKILDKTKLDQK-TQRLLSREISSMEKLHHPNIIRLYEVVETLSKLH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA-PSLRR 230
Cdd:cd14075   78 LVMEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAkRGETL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLR 309
Cdd:cd14075  158 NTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQ 237
                        250
                 ....*....|....*...
gi 927602445 310 HNPSERLPLAQVSAHPWV 327
Cdd:cd14075  238 PVPSDRYSIDEIKNSEWL 255
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
76-337 9.54e-44

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 153.54  E-value: 9.54e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSH---FIVALKVLFKSQI-EKEGVEHQLRREIEIQAHLHH-PNILRLYNYFYDRRRI 150
Cdd:cd05614    1 NFELLKVLGTGAYGKVFLVRKVSGHdanKLYAMKVLRKAALvQKAKTVEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPS 227
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSkefLTEEK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQD 302
Cdd:cd05614  161 ERTYSFCGTIEYMAPEIIRGKSgHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 927602445 303 LISKLLRHNPSERLPLA-----QVSAHP------WVRANSRRVLPP 337
Cdd:cd05614  241 LLQKLLCKDPKKRLGAGpqgaqEIKEHPffkgldWEALALRKVNPP 286
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
77-327 1.30e-43

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 151.58  E-value: 1.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALR--GKEAMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLK---GELKIADFGWSVHAPSLRRKTM 233
Cdd:cd14169   83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPfedSKIMISDFGLSKIEAQGMLSTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKLLR 309
Cdd:cd14169  163 CGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEYEFDSpywdDISESAKDFIRHLLE 242
                        250
                 ....*....|....*...
gi 927602445 310 HNPSERLPLAQVSAHPWV 327
Cdd:cd14169  243 RDPEKRFTCEQALQHPWI 260
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
77-326 1.80e-43

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 150.70  E-value: 1.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYF-YDRRRIYLILE 155
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLPRELEILARLNHKSIIKTYEIFeTSDGKVYIVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvhAPSLR------ 229
Cdd:cd14165   83 LGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFS--KRCLRdengri 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 --RKTMCGTLDYLPPEMIEGRMHNEKV-DLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQ--DLI 304
Cdd:cd14165  161 vlSKTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRSKNLTSEckDLI 240
                        250       260
                 ....*....|....*....|..
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14165  241 YRLLQPDVSQRLCIDEVLSHPW 262
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
73-316 3.12e-43

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 152.54  E-value: 3.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRrEIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd05593   13 TMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIiAKDEVAHTLT-ESRVLKNTRHPFLTSLKYSFQTKDRLC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA--PSLR 229
Cdd:cd05593   92 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGitDAAT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLR 309
Cdd:cd05593  172 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLI 251

                 ....*..
gi 927602445 310 HNPSERL 316
Cdd:cd05593  252 KDPNKRL 258
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
75-332 3.92e-43

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 150.09  E-value: 3.92e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDE-IE-DIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELyKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRKT 232
Cdd:cd06609   79 EYCGGGSV-LDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQltSTMSKRNT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKVDLKFPASVPMGA-----QDLISKL 307
Cdd:cd06609  158 FVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPL---SDLHPMRVLFLIPKNNPPSLEGNKfskpfKDFVELC 234
                        250       260
                 ....*....|....*....|....*
gi 927602445 308 LRHNPSERLPLAQVSAHPWVRANSR 332
Cdd:cd06609  235 LNKDPKERPSAKELLKHKFIKKAKK 259
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
76-325 3.98e-43

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: 149.46  E-value: 3.98e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVnLGSLSQKE--REDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCT----FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR 230
Cdd:cd08530   79 EYAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVdlKFPASVPMGAQDL---ISKL 307
Cdd:cd08530  159 KTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRG--KFPPIPPVYSQDLqqiIRSL 236
                        250
                 ....*....|....*...
gi 927602445 308 LRHNPSERLPLAQVSAHP 325
Cdd:cd08530  237 LQVNPKKRPSCDKLLQSP 254
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
75-326 1.16e-42

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 148.64  E-value: 1.16e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCC--GKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWS--VHAPSL 228
Cdd:cd14184   79 ELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENllvcEYPDGTKSLKLGDFGLAtvVEGPLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 rrkTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASH--NETYRRIVKVDLKFPA----SVPMGAQD 302
Cdd:cd14184  159 ---TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNlqEDLFDQILLGKLEFPSpywdNITDSAKE 235
                        250       260
                 ....*....|....*....|....
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14184  236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
77-327 1.22e-42

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: 148.14  E-value: 1.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd06627    2 YQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLK-SVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSL--RRKTMC 234
Cdd:cd06627   81 VENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVekDENSVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPP-FESASHNETYrRIVKVD-LKFPASVPMGAQDLISKLLRHNP 312
Cdd:cd06627  161 GTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPyYDLQPMAALF-RIVQDDhPPLPENISPELRDFLLQCFQKDP 239
                        250
                 ....*....|....*
gi 927602445 313 SERLPLAQVSAHPWV 327
Cdd:cd06627  240 TLRPSAKELLKHPWL 254
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
76-316 1.83e-42

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 149.00  E-value: 1.83e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSH---FIVALKVLFKSQI-EKEGVEHQLRREIEIQAHLHH-PNILRLYNYFYDRRRI 150
Cdd:cd05613    1 NFELLKVLGTGAYGKVFLVRKVSGHdagKLYAMKVLKKATIvQKAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPS 227
Cdd:cd05613   81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSkefLLDEN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIEG--RMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQ 301
Cdd:cd05613  161 ERAYSFCGTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAK 240
                        250
                 ....*....|....*
gi 927602445 302 DLISKLLRHNPSERL 316
Cdd:cd05613  241 DIIQRLLMKDPKKRL 255
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
75-332 1.84e-42

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


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 149.11  E-value: 1.84e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQ-LRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSAR--DHQkLEREARICRLLKHPNIVRLHDSISEEGFHYLV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAP--SL 228
Cdd:cd14086   79 FDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENlllASKSKGAAVKLADFGLAIEVQgdQQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLI 304
Cdd:cd14086  159 AWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLI 238
                        250       260
                 ....*....|....*....|....*...
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPWVRANSR 332
Cdd:cd14086  239 NQMLTVNPAKRITAAEALKHPWICQRDR 266
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
76-327 6.26e-42

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 146.82  E-value: 6.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEI--------QAH----LHHPNILRLYNY 143
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRASNAGLKKEREKRLEKEIsrdirtirEAAlsslLNHPHICRLRDF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 144 FYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS- 222
Cdd:cd14077   82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSn 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRRKTMCGTLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQ 301
Cdd:cd14077  162 LYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSECK 241
                        250       260
                 ....*....|....*....|....*.
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14077  242 SLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
83-329 7.74e-42

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 146.77  E-value: 7.74e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSH---FIVALKVLFKSQI--EKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd05583    2 LGTGAYGKVFLVRKVGGHdagKLYAMKVLKKATIvqKAKTAEHTMTERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLRRKTMC 234
Cdd:cd05583   82 NGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSkefLPGENDRAYSFC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMIEG--RMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd05583  162 GTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFtvdgERNSQSEISKRILKSHPPIPKTFSAEAKDFILKLL 241
                        250       260
                 ....*....|....*....|....*.
gi 927602445 309 RHNPSERL-----PLAQVSAHPWVRA 329
Cdd:cd05583  242 EKDPKKRLgagprGAHEIKEHPFFKG 267
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
71-337 9.67e-42

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 148.24  E-value: 9.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQ-AHLHHPNILRLYNYFYDRRR 149
Cdd:cd05602    3 HAKPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKHIMSERNVLlKNVKHPFLVGLHFSFQTTDK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APS 227
Cdd:cd05602   83 LYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKEniEPN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKL 307
Cdd:cd05602  163 GTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGL 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 927602445 308 LRHNPSERL----PLAQVSAH------PWVRANSRRVLPP 337
Cdd:cd05602  243 LQKDRTKRLgakdDFTEIKNHiffspiNWDDLINKKITPP 282
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
80-321 1.93e-41

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 145.46  E-value: 1.93e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd14187   12 GRFLGKGGFAKCYEITDADTKEVFAGKIVPKSLLLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTL 237
Cdd:cd14187   92 RSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLAtkVEYDGERKKTLCGTP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLP 317
Cdd:cd14187  172 NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPT 251

                 ....
gi 927602445 318 LAQV 321
Cdd:cd14187  252 INEL 255
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
72-337 2.10e-41

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 147.38  E-value: 2.10e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRI 150
Cdd:cd05619    2 LTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVlMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFQTKENL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA--PSL 228
Cdd:cd05619   82 FFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENmlGDA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd05619  162 KTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLF 241
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 927602445 309 RHNPSERLPL-AQVSAHP------WVRANSRRVLPP 337
Cdd:cd05619  242 VREPERRLGVrGDIRQHPffreinWEALEEREIEPP 277
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
77-327 2.13e-41

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 145.37  E-value: 2.13e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRreieIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREVCESELN----VLRRVRHTNIIQLIEVFETKERVYMVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHA---PSLRR 230
Cdd:cd14087   79 ATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENllyYHPGPDSKIMITDFGLASTRkkgPNCLM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISK 306
Cdd:cd14087  159 KTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGepwpSVSNLAKDFIDR 238
                        250       260
                 ....*....|....*....|.
gi 927602445 307 LLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14087  239 LLTVNPGERLSATQALKHPWI 259
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
83-315 2.44e-41

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 144.60  E-value: 2.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKShfIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd13999    1 IGSGSFGEVYKGKWRGT--DVAIKKLKVEDDNDELLK-EFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLDY 239
Cdd:cd13999   78 YDLLHkKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSriKNSTTEKMTGVVGTPRW 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESAS--------HNETYRRIVkvdlkfPASVPMGAQDLISKLLRHN 311
Cdd:cd13999  158 MAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSpiqiaaavVQKGLRPPI------PPDCPPELSKLIKRCWNED 231

                 ....
gi 927602445 312 PSER 315
Cdd:cd13999  232 PEKR 235
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
83-337 2.59e-41

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


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 146.76  E-value: 2.59e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQL--RREIEIQAHlhHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05592    3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVlEDDDVECTMieRRVLALASQ--HPFLTHLFCTFQTESHLFFVMEYLNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK--TMCGTL 237
Cdd:cd05592   81 GDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKasTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL- 316
Cdd:cd05592  161 DYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLg 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 927602445 317 ----PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05592  241 vpecPAGDIRDHPffktidWDKLERREIDPP 271
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
83-325 3.33e-41

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 144.43  E-value: 3.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKK-SHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKS--QNLLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---------LLLGLKGELKIADFGWSVHAPS-LRRK 231
Cdd:cd14120   79 LADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNillshnsgrKPSPNDIRLKIADFGFARFLQDgMMAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET---YRRIVKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd14120  159 TLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPSGTSPALKDLLLGLL 238
                        250
                 ....*....|....*..
gi 927602445 309 RHNPSERLPLAQVSAHP 325
Cdd:cd14120  239 KRNPKDRIDFEDFFSHP 255
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
83-316 1.27e-40

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 145.11  E-value: 1.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQ-AHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA--PSLRRKTMCGTLDY 239
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGmePEETTSTFCGTPEY 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL 316
Cdd:cd05603  163 LAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRL 239
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
76-316 1.38e-40

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 143.46  E-value: 1.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLG--KGKFGNVYLAREKKSHfivalKVLFKSQIEKEGVehqlrREIEIQAHL---HHPNILRLYNYFYDRRRI 150
Cdd:PHA03390  15 NCEIVKKLKliDGKFGKVSVLKHKPTQ-----KLFVQKIIKAKNF-----NAIEPMVHQlmkDNPNFIKLYYSVTTLKGH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL-LGLKGELKIADFGWS--VHAPS 227
Cdd:PHA03390  85 VLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLyDRAKDRIYLCDYGLCkiIGTPS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRktmcGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESaSHNETY------RRIVKvDLKFPASVPMGAQ 301
Cdd:PHA03390 165 CYD----GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKE-DEDEELdlesllKRQQK-KLPFIKNVSKNAN 238
                        250
                 ....*....|....*
gi 927602445 302 DLISKLLRHNPSERL 316
Cdd:PHA03390 239 DFVQSMLKYNINYRL 253
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
83-337 2.22e-40

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 144.33  E-value: 2.22e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd05604    4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKVIlNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTM--CGTLDY 239
Cdd:cd05604   84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTtfCGTPEY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL--- 316
Cdd:cd05604  164 LAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRLgak 243
                        250       260
                 ....*....|....*....|....*...
gi 927602445 317 -PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05604  244 eDFLEIKNHPffesinWTDLVQKKIPPP 271
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
83-337 4.52e-40

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 143.40  E-value: 4.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQL--RREIEIQAHlhHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05591    3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDVIlQDDDVDCTMteKRILALAAK--HPFLTALHSCFQTKDRLFFVMEYVNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRKTMCGTL 237
Cdd:cd05591   81 GDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEgiLNGKTTTTFCGTP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLP 317
Cdd:cd05591  161 DYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLG 240
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 318 L-------AQVSAHP------WVRANSRRVLPP 337
Cdd:cd05591  241 CvasqggeDAIRQHPffreidWEALEQRKVKPP 273
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
76-315 5.76e-40

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 141.39  E-value: 5.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfksQIEKEGVEHQLR----REIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALK-----QIDISRMSRKMReeaiDEARVLSKLNSPYVIKYYDSFVDKGKLN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKsctfdeQRTATIMEEL--------ADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW-- 221
Cdd:cd08529   76 IVMEYAENGDLHSLIKS------QRGRPLPEDQiwkffiqtLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVak 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 222 SVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKfPASVPMGAQ 301
Cdd:cd08529  150 ILSDTTNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYP-PISASYSQD 228
                        250
                 ....*....|....*.
gi 927602445 302 --DLISKLLRHNPSER 315
Cdd:cd08529  229 lsQLIDSCLTKDYRQR 244
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
75-337 6.82e-40

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 143.22  E-value: 6.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05601    1 KDFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRK 231
Cdd:cd05601   81 EYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAakLSSDKTVTS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TM-CGTLDYLPPEM---IEGR---MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPA--SVPMGA 300
Cdd:cd05601  161 KMpVGTPDYIAPEVltsMNGGskgTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfKKFLKFPEdpKVSESA 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 301 QDLISKLLRHnPSERLPLAQVSAHP------WvrANSRRVLPP 337
Cdd:cd05601  241 VDLIKGLLTD-AKERLGYEGLCCHPffsgidW--NNLRQTVPP 280
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
79-327 7.14e-40

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 141.47  E-value: 7.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNVYLA--REKKSHFI---VALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14076    5 LGRTLGEGEFGKVKLGwpLPKANHRSgvqVAIKLIRRDTQQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV---HAPSLRR 230
Cdd:cd14076   85 LEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANtfdHFNGDLM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMI--EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN-------ETYRRIVKVDLKFPASVPMGAQ 301
Cdd:cd14076  165 STSCGSPCYAAPELVvsDSMYAGRKADIWSCGVILYAMLAGYLPFDDDPHNpngdnvpRLYRYICNTPLIFPEYVTPKAR 244
                        250       260
                 ....*....|....*....|....*.
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14076  245 DLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
49-316 7.28e-40

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 144.02  E-value: 7.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  49 PTAAPGQKVMENSSGTPdiltRH-FTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRrEI 126
Cdd:cd05594    2 PSDNSGAEEMEVSLTKP----KHkVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIvAKDEVAHTLT-EN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 127 EIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK-VIHRDIKPEN 205
Cdd:cd05594   77 RVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKnVVYRDLKLEN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 206 LLLGLKGELKIADFGWSVHA--PSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYR 283
Cdd:cd05594  157 LMLDKDGHIKITDFGLCKEGikDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFE 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 284 RIVKVDLKFPASVPMGAQDLISKLLRHNPSERL 316
Cdd:cd05594  237 LILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRL 269
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
77-331 7.99e-40

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 142.49  E-value: 7.99e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALK--GKESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL---LLGLKGELKIADFGWS-VHAPSLRRKT 232
Cdd:cd14168   90 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLlyfSQDEESKIMISDFGLSkMEGKGDVMST 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKLL 308
Cdd:cd14168  170 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKADYEFDSpywdDISDSAKDFIRNLM 249
                        250       260
                 ....*....|....*....|...
gi 927602445 309 RHNPSERLPLAQVSAHPWVRANS 331
Cdd:cd14168  250 EKDPNKRYTCEQALRHPWIAGDT 272
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
77-327 1.11e-39

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


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 140.60  E-value: 1.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVlfksqIEKEGVEHQL---RREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14078    5 YELHETIGSGGFAKVKLATHILTGEKVAIKI-----MDKKALGDDLprvKTEIEALKNLSHQHICRLYHVIETDNKIFMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR--- 230
Cdd:cd14078   80 LEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDhhl 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLR 309
Cdd:cd14078  160 ETCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQ 239
                        250
                 ....*....|....*...
gi 927602445 310 HNPSERLPLAQVSAHPWV 327
Cdd:cd14078  240 VDPKKRITVKELLNHPWV 257
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
76-325 1.37e-39

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 140.75  E-value: 1.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDR--RRIYL 152
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMsEKE--KQQLVSEVNILRELKHPNIVRYYDRIVDRanTTLYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQKSCT----FDEQRTATIMEELADALMYCH-----GKKVIHRDIKPENLLLGLKGELKIADFGWS- 222
Cdd:cd08217   79 VMEYCEGGDLAQLIKKCKKenqyIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLAr 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 -VHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVdlKFPASVPMGAQ 301
Cdd:cd08217  159 vLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEG--KFPRIPSRYSS 236
                        250       260
                 ....*....|....*....|....*..
gi 927602445 302 DL---ISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd08217  237 ELnevIKSMLNVDPDKRPSVEELLQLP 263
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
77-327 1.57e-39

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 140.06  E-value: 1.57e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRREIEIQAHL-----HHPNILRLYNYFYDRRRI 150
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVtEWAMINGPVPVPLEIALLLkaskpGVPGVIRLLDWYERPDGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEY-APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL-LGLKGELKIADFGwsvHAPSL 228
Cdd:cd14005   82 LLIMERpEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLiNLRTGEVKLIDFG---CGALL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RR---KTMCGTLDYLPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPFESAShnetyrRIVKVDLKFPASVPMGAQDLI 304
Cdd:cd14005  159 KDsvyTDFDGTRVYSPPEWIrHGRYHGRPATVWSLGILLYDMLCGDIPFENDE------QILRGNVLFRPRLSKECCDLI 232
                        250       260
                 ....*....|....*....|...
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14005  233 SRCLQFDPSKRPSLEQILSHPWF 255
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
76-342 2.87e-39

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 140.46  E-value: 2.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKegvehqlRREIEI-QAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDP-------SEEIEIlLRYGQHPNIITLRDVYDDGNSVYLVT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELY-KELQKSCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWsvhAPSLR 229
Cdd:cd14091   74 ELLRGGELLdRILRQKF-FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNilyaDESGDPESLRICDFGF---AKQLR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RK-----TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESAShNETYRRIV------KVDLKFP--ASV 296
Cdd:cd14091  150 AEngllmTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGP-NDTPEVILarigsgKIDLSGGnwDHV 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 927602445 297 PMGAQDLISKLLRHNPSERLPLAQVSAHPWVRanSRRVLPPSALQS 342
Cdd:cd14091  229 SDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR--NRDSLPQRQLTD 272
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
80-327 2.88e-39

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 140.63  E-value: 2.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVlfksqIEKE--GVEHQLRREIEIQAHLH-HPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14090    7 GELLGEGAYASVQTCINLYTGKEYAVKI-----IEKHpgHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWS----------- 222
Cdd:cd14090   82 MRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENilcESMDKVSPVKICDFDLGsgiklsstsmt 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 -VHAPSLrrKTMCGTLDYLPPEMI-----EGRMHNEKVDLWCIGVLCYELLVGNPPFE---------------SASHNET 281
Cdd:cd14090  162 pVTTPEL--LTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYgrcgedcgwdrgeacQDCQELL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 282 YRRIVKVDLKFP----ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14090  240 FHSIQEGEYEFPekewSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
75-337 3.29e-39

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 141.30  E-value: 3.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-IEKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05598    1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMKTLRKKDvLKRNQVAH-VKAERDILAEADNEWVVKLYYSFQDKENLYFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------WSvH--- 224
Cdd:cd05598   80 MDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrWT-Hdsk 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 ---APSLrrktmCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPASVPMG 299
Cdd:cd05598  159 yylAHSL-----VGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEANLS 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 927602445 300 --AQDLISKLLRhNPSERL---PLAQVSAHPWVR----ANSRRVLPP 337
Cdd:cd05598  234 peAKDLILRLCC-DAEDRLgrnGADEIKAHPFFAgidwEKLRKQKAP 279
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
64-327 1.47e-38

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 137.87  E-value: 1.47e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  64 TPDILTRHFTIDdfeiGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgVEHQLRREIEI-QAHLHHPNILRLYN 142
Cdd:cd14106    1 STENINEVYTVE----STPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQD-CRNEILHEIAVlELCKDCPRVVNLHE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 143 YFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL---KIADF 219
Cdd:cd14106   76 VYETRSELILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLgdiKLCDF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 220 GWS-VHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----A 294
Cdd:cd14106  156 GISrVIGEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPeelfK 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 295 SVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14106  236 DVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
77-326 2.01e-38

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 136.98  E-value: 2.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqieKEGVEHQLR--REIEIQAHL----HHPNILRLYNYFYDR--R 148
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI------KNDFRHPKAalREIKLLKHLndveGHPNIVKLLDVFEHRggN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 RIYLILEYAPRgELYKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN-LLLGLKGELKIADFGWSVHAP 226
Cdd:cd05118   75 HLCLVFELMGM-NLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENiLINLELGQLKLADFGLARSFT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRKTMCGTLDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVdlkfpasvpMG---AQD 302
Cdd:cd05118  154 SPPYTPYVATRWYRAPEvLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRL---------LGtpeALD 224
                        250       260
                 ....*....|....*....|....
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd05118  225 LLSKMLKYDPAKRITASQALAHPY 248
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
116-326 2.43e-38

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


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 137.79  E-value: 2.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 116 EGVEHQLRREIEIQAHLH-HPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK 194
Cdd:cd14181   56 EEVRSSTLKEIHILRQVSgHPSIITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHAN 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 195 KVIHRDIKPENLLLGLKGELKIADFGWSVH-APSLRRKTMCGTLDYLPPEMIEGRM------HNEKVDLWCIGVLCYELL 267
Cdd:cd14181  136 NIVHRDLKPENILLDDQLHIKLSDFGFSCHlEPGEKLRELCGTPGYLAPEILKCSMdethpgYGKEVDLWACGVILFTLL 215
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 268 VGNPPFESASHNETYRRIVKVDLKFpaSVPM------GAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14181  216 AGSPPFWHRRQMLMLRMIMEGRYQF--SSPEwddrssTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
70-332 2.62e-38

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: 138.63  E-value: 2.62e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  70 RHFTIDDFEigRPLGKGKFGNVYLAREKKSHFIVALKVLFKSqiekegVEHQLRREIE-IQAHLHHPNILRLYNYFYDRR 148
Cdd:cd14179    4 QHYELDLKD--KPLGEGSFSICRKCLHKKTNQEYAVKIVSKR------MEANTQREIAaLKLCEGHPNIVKLHEVYHDQL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 RIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHA 225
Cdd:cd14179   76 HTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENllfTDESDNSEIKIIDFGFARLK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRR--KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFES-------ASHNETYRRIVKVDLKFPA-- 294
Cdd:cd14179  156 PPDNQplKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQChdksltcTSAEEIMKKIKQGDFSFEGea 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 927602445 295 --SVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSR 332
Cdd:cd14179  236 wkNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQ 275
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
75-327 3.13e-38

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 137.23  E-value: 3.13e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIE--KEGVEH-QLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14105    5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasRRGVSReDIEREVSILRQVLHPNIITLHDVFENKTDVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWSvHA-- 225
Cdd:cd14105   85 LILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENimllDKNVPIPRIKLIDFGLA-HKie 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMG----AQ 301
Cdd:cd14105  164 DGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYFSNtselAK 243
                        250       260
                 ....*....|....*....|....*.
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14105  244 DFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
76-337 3.85e-38

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 138.59  E-value: 3.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-IEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVvIQDDDVECTMVEKRVLALSGKPPFLTQLHSCFQTMDRLYFVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------WSvhapSL 228
Cdd:cd05616   81 EYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGmckeniWD----GV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd05616  157 TTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLM 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 927602445 309 RHNPSERL---PLAQ--VSAHP------WVRANSRRVLPP 337
Cdd:cd05616  237 TKHPGKRLgcgPEGErdIKEHAffryidWEKLERKEIQPP 276
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
77-327 4.22e-38

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 136.66  E-value: 4.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRR-RIYLILE 155
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLPRELQIVERLDHKNIIHVYEMLESADgKIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENlLLGLKGELKIADFGWSVHAPSLRR---KT 232
Cdd:cd14163   82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCEN-ALLQGFTLKLTDFGFAKQLPKGGRelsQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHN-EKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKvDLKFPA--SVPMGAQDLISKLLR 309
Cdd:cd14163  161 FCGSTAYAAPEVLQGVPHDsRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQK-GVSLPGhlGVSRTCQDLLKRLLE 239
                        250
                 ....*....|....*...
gi 927602445 310 HNPSERLPLAQVSAHPWV 327
Cdd:cd14163  240 PDMVLRPSIEEVSWHPWL 257
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
75-327 7.94e-38

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 136.28  E-value: 7.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14183    6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCR--GKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGL----KGELKIADFGWS--VHAPSL 228
Cdd:cd14183   84 ELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSKSLKLGDFGLAtvVDGPLY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 rrkTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET--YRRIVKVDLKFPA----SVPMGAQD 302
Cdd:cd14183  164 ---TVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEvlFDQILMGQVDFPSpywdNVSDSAKE 240
                        250       260
                 ....*....|....*....|....*
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14183  241 LITMMLQVDVDQRYSALQVLEHPWV 265
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
76-326 9.65e-38

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 139.01  E-value: 9.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05600   12 DFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKVLFKLNEVNHVLTERDILTTTNSPWLVKLLYAFQDPENVYLAME 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV------------ 223
Cdd:cd05600   92 YVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASgtlspkkiesmk 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 -------------HAPSLRRKTM--------------CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESA 276
Cdd:cd05600  172 irleevkntafleLTAKERRNIYramrkedqnyansvVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSGS 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 277 SHNETY----------RRIVKVDLKFPASVPMGAQDLISKLLRhNPSERL-PLAQVSAHPW 326
Cdd:cd05600  252 TPNETWanlyhwkktlQRPVYTDPDLEFNLSDEAWDLITKLIT-DPQDRLqSPEQIKNHPF 311
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
77-326 1.01e-37

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


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 136.07  E-value: 1.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKI-RLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRgELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHAPSLRRKT-- 232
Cdd:cd07829   80 CDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLArAFGIPLRTYThe 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 -McgTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASH----------------------------NETY 282
Cdd:cd07829  159 vV--TLWYRAPEILLGsKHYSTAVDIWSVGCIFAELITGKPLFPGDSEidqlfkifqilgtpteeswpgvtklpdyKPTF 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 927602445 283 RRIVKVDLK--FPASVPMGAqDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07829  237 PKWPKNDLEkvLPRLDPEGI-DLLSKMLQYNPAKRISAKEALKHPY 281
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
83-337 1.17e-37

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 137.14  E-value: 1.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQL--RREIEIQAHlhHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDELYAIKILKKDVIiQDDDVECTMveKRVLALSGK--PPFLTQLHSCFQTMDRLYFVMEYVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRKTMCGTL 237
Cdd:cd05587   82 GDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEgiFGGKTTRTFCGTP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLP 317
Cdd:cd05587  162 DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKRLG 241
                        250       260       270
                 ....*....|....*....|....*....|.
gi 927602445 318 L-----AQVSAHP------WVRANSRRVLPP 337
Cdd:cd05587  242 CgptgeRDIKEHPffrridWEKLERREIQPP 272
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
75-327 1.83e-37

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 135.02  E-value: 1.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKS-QIEKEGVehqlRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14114    2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPhESDKETV----RKEIQIMNQLHHPKLINLHDAFEDDNEMVLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL--LLGLKGELKIADFGWSVHA-PSLR 229
Cdd:cd14114   78 LEFLSGGELFERIaAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENImcTTKRSNEVKLIDFGLATHLdPKES 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQDLIS 305
Cdd:cd14114  158 VKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFIR 237
                        250       260
                 ....*....|....*....|..
gi 927602445 306 KLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14114  238 KLLLADPNKRMTIHQALEHPWL 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
75-327 1.84e-37

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 135.08  E-value: 1.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFK--SQIEKEGV-EHQLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14196    5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKrqSRASRRGVsREEIEREVSILRQVLHPNIITLHDVYENRTDVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL----LLGLKGELKIADFGWSvH--A 225
Cdd:cd14196   85 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImlldKNIPIPHIKLIDFGLA-HeiE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----DLKFPASVPMGAQ 301
Cdd:cd14196  164 DGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVsydfDEEFFSHTSELAK 243
                        250       260
                 ....*....|....*....|....*.
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14196  244 DFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
83-325 2.28e-37

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 134.65  E-value: 2.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKegvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd06614    8 IGEGASGEVYKATDRATGKEVAIKKMrLRKQNKE-----LIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRKTMCGTLD 238
Cdd:cd06614   83 LTDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQltKEKSKRNSVVGTPY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV---DLKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd06614  163 WMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITTKgipPLKNPEKWSPEFKDFLNKCLVKDPEKR 242
                        250
                 ....*....|
gi 927602445 316 LPLAQVSAHP 325
Cdd:cd06614  243 PSAEELLQHP 252
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
74-337 3.91e-37

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 136.28  E-value: 3.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-IEKEGVEHQLRrEIEIQAHLHHPNIL-RLYNYFYDRRRIY 151
Cdd:cd05615    9 LTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVvIQDDDVECTMV-EKRVLALQDKPPFLtQLHSCFQTVDRLY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLR 229
Cdd:cd05615   88 FVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEhmVEGVT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLR 309
Cdd:cd05615  168 TRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMT 247
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 927602445 310 HNPSERLPLAQ-----VSAHP------WVRANSRRVLPP 337
Cdd:cd05615  248 KHPAKRLGCGPegerdIREHAffrridWDKLENREIQPP 286
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
83-327 3.99e-37

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: 133.92  E-value: 3.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEK-EGVEHQLRREIEIQAHLHHPNILRLYNYFYD--RRRIYLILEYAPR 159
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRiPNGEANVKREIQILRRLNHRNVIKLVDVLYNeeKQKLYMVMEYCVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 G---ELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG----WSVHAPSLRRKT 232
Cdd:cd14119   81 GlqeMLDSAPDKR--LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGvaeaLDLFAEDDTCTT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEG--RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRH 310
Cdd:cd14119  159 SQGSPAFQPPEIANGqdSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLEK 238
                        250
                 ....*....|....*..
gi 927602445 311 NPSERLPLAQVSAHPWV 327
Cdd:cd14119  239 DPEKRFTIEQIRQHPWF 255
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
74-337 4.79e-37

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


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 136.35  E-value: 4.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05596   25 AEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYMV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKeLQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG--WSVHAPSL-RR 230
Cdd:cd05596  105 MDYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGtcMKMDKDGLvRS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMI--EGRM--HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPASVPMG--AQD 302
Cdd:cd05596  184 DTAVGTPDYISPEVLksQGGDgvYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnhKNSLQFPDDVEISkdAKS 263
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 303 LISKLL--RHNPSERLPLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05596  264 LICAFLtdREVRLGRNGIEEIKAHPffkndqWTWDNIRETVPP 306
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
77-326 5.71e-37

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 133.57  E-value: 5.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVlfksqIEK-EGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKY-----IERgEKIDENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLL--GLKGELKIADFGWS----VHApslR 229
Cdd:cd14665   77 YAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSkssvLHS---Q 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKV-DLWCIGVLCYELLVGNPPFESASHNETYR----RIVKVDLKFPASVPMG--AQD 302
Cdd:cd14665  154 PKSTVGTPAYIAPEVLLKKEYDGKIaDVWSCGVTLYVMLVGAYPFEDPEEPRNFRktiqRILSVQYSIPDYVHISpeCRH 233
                        250       260
                 ....*....|....*....|....
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14665  234 LISRIFVADPATRITIPEIRNHEW 257
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
74-322 6.08e-37

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: 133.96  E-value: 6.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSqiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd13996    5 LNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLT--EKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQK---SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL-LLGLKGELKIADFG--------- 220
Cdd:cd13996   83 MELCEGGTLRDWIDRrnsSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIfLDNDDLQVKIGDFGlatsignqk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 ---WSVHAPSLRRKTM----CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVgnpPFESAShnETYRRIVKV-DLKF 292
Cdd:cd13996  163 relNNLNNNNNGNTSNnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLH---PFKTAM--ERSTILTDLrNGIL 237
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 293 PASV----PMGAQdLISKLLRHNPSERLPLAQVS 322
Cdd:cd13996  238 PESFkakhPKEAD-LIQSLLSKNPEERPSAEQLL 270
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
83-326 1.03e-36

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: 133.60  E-value: 1.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVlFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRgEL 162
Cdd:cd07833    9 VGEGAYGVVLKCRNKATGEIVAIKK-FKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER-TL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKT-MCGTLD 238
Cdd:cd07833   87 LELLEASPGgLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFarALTARPASPLTdYVATRW 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----------------------------- 288
Cdd:cd07833  167 YRAPELLVGdTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKClgplppshqelfssnprfagvafpepsqp 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 927602445 289 ---DLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07833  247 eslERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
83-326 1.49e-36

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: 132.45  E-value: 1.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGvehqLRREIEIQAHL-HHPNILRLYNYFYDRRRIYLIL-EYAPRG 160
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKD----FLREYNISLELsVHPHIIKTYDVAFETEDYYVFAqEYAPYG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKI--ADFGWSVHAPSLRRKtMCGTLD 238
Cdd:cd13987   77 DLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVklCDFGLTRRVGSTVKR-VSGTIP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMH-----NEKVDLWCIGVLCYELLVGNPPFESA-SHNETYRRIVKVDLKFPASVPMG-------AQDLIS 305
Cdd:cd13987  156 YTAPEVCEAKKNegfvvDPSIDVWAFGVLLFCCLTGNFPWEKAdSDDQFYEEFVRWQKRKNTAVPSQwrrftpkALRMFK 235
                        250       260
                 ....*....|....*....|....
gi 927602445 306 KLLRHNPSERLPLAQVS---AHPW 326
Cdd:cd13987  236 KLLAPEPERRCSIKEVFkylGDRW 259
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
69-327 1.86e-36

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 132.34  E-value: 1.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  69 TRHFTIDDFEIgrpLGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEGVehqlRREIEIQAHLHHPNILRLYNYFYDR 147
Cdd:cd14193    1 NSYYNVNKEEI---LGGGRFGQVHKCEEKSSGLKLAAKIIkARSQKEKEEV----KNEIEVMNQLNHANLIQLYDAFESR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL--LGLKGELKIADFGWSV- 223
Cdd:cd14193   74 NDIVLVMEYVDGGELFDRIiDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILcvSREANQVKIIDFGLARr 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMG 299
Cdd:cd14193  154 YKPREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEdeefADISEE 233
                        250       260
                 ....*....|....*....|....*...
gi 927602445 300 AQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14193  234 AKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
76-326 2.65e-36

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 132.03  E-value: 2.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEI-GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiekegvehQLRREIEIQ----AHLHHPNILRLY-NYFYDRRR 149
Cdd:cd14089    1 DYTIsKQVLGLGINGKVLECFHKKTGEKFALKVLRDNP--------KARREVELHwrasGCPHIVRIIDVYeNTYQGRKC 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKI---ADFGWS-- 222
Cdd:cd14089   73 LLVVMECMEGGELFSRIQEraDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNAIlklTDFGFAke 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 -VHAPSLrrKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNE----TYRRIVKVDLKFP---- 293
Cdd:cd14089  153 tTTKKSL--QTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAispgMKKRIRNGQYEFPnpew 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 294 ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14089  231 SNVSEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
75-327 3.27e-36

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 132.07  E-value: 3.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFK--SQIEKEGVEHQ-LRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKrrTKSSRRGVSREdIEREVSILKEIQHPNVITLHEVYENKTDVI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWSVHAPS 227
Cdd:cd14194   85 LILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENimllDRNVPKPRIKIIDFGLAHKIDF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRR-KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQD 302
Cdd:cd14194  165 GNEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEdeyfSNTSALAKD 244
                        250       260
                 ....*....|....*....|....*
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14194  245 FIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
83-327 3.53e-36

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: 131.66  E-value: 3.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNV--YLAREKKSHFIVALKVLFKSQIE--KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRR-IYLILEYA 157
Cdd:cd13994    1 IGKGATSVVriVTKKNPRSGVLYAVKEYRRRDDEskRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGkWCLVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYK--ELQKSCTFDEQRTatIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV--HAP----SLR 229
Cdd:cd13994   81 PGGDLFTliEKADSLSLEEKDC--FFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEvfGMPaekeSPM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNE------TYRRIVKVDLKFPA--SVPMGA 300
Cdd:cd13994  159 SAGLCGSEPYMAPEvFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSAKKSDsaykayEKSGDFTNGPYEPIenLLPSEC 238
                        250       260
                 ....*....|....*....|....*..
gi 927602445 301 QDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd13994  239 RRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
73-325 3.95e-36

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 133.85  E-value: 3.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd05610    2 SIEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---------- 222
Cdd:cd05610   82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnm 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 ---VHAPSLRRKT------------------------------------------MCGTLDYLPPEMIEGRMHNEKVDLW 257
Cdd:cd05610  162 mdiLTTPSMAKPKndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWW 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 258 CIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP---ASVPMGAQDLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd05610  242 ALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAGLKELKQHP 312
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
83-337 4.10e-36

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 133.08  E-value: 4.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQL--RREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIvAKKEVAHTIgeRNILVRTALDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvhAPSLRRK----TMCG 235
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS--KADLTDNkttnTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASV-PMGAQDLISKLLRHNPS 313
Cdd:cd05586  159 TTEYLAPEvLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDVlSDEGRSFVKGLLNRNPK 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 314 ERL----PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05586  239 HRLgahdDAVELKEHPffadidWDLLSKKKITPP 272
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
73-327 4.30e-36

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 131.67  E-value: 4.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRP--LGKGKFGNVYLARE-KKSHFIVALKVLFKSQIEKEGVehQLRREIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd14201    2 VVGDFEYSRKdlVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQI--LLGKEIKILKELQHENIVALYDVQEMPNS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL---------KIADFG 220
Cdd:cd14201   80 VFLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKkssvsgiriKIADFG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 WSVHAPS-LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET---YRRIVKVDLKFPASV 296
Cdd:cd14201  160 FARYLQSnMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLrmfYEKNKNLQPSIPRET 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 927602445 297 PMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14201  240 SPYLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
75-327 5.37e-36

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 131.30  E-value: 5.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKegVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRDGRK--VRKAAKNEINILKMVKHPNILQLVDVFETRKEYFIFL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL---LGLKGELKIADFgwsvHAPSLRR- 230
Cdd:cd14088   79 ELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyynRLKNSKIVISDF----HLAKLENg 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 --KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETY--------RRIVKVDLKFPA----SV 296
Cdd:cd14088  155 liKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYenhdknlfRKILAGDYEFDSpywdDI 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 927602445 297 PMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14088  235 SQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
75-329 9.00e-36

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


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 130.89  E-value: 9.00e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIE--KEGV-EHQLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14195    5 DHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSssRRGVsREEIEREVNILREIQHPNIITLHDIFENKTDVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL----LLGLKGELKIADFGWSVHAPS 227
Cdd:cd14195   85 LILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImlldKNVPNPRIKLIDFGIAHKIEA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRR-KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQD 302
Cdd:cd14195  165 GNEfKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDeeyfSNTSELAKD 244
                        250       260
                 ....*....|....*....|....*..
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWVRA 329
Cdd:cd14195  245 FIRRLLVKDPKKRMTIAQSLEHSWIKA 271
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
77-327 1.29e-35

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 130.13  E-value: 1.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRP--LGKGKFGNVYLAREKKSH-FIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14202    2 FEFSRKdlIGHGAFAVVFKGRHKEKHdLEVAVKCINKKNLAKS--QTLLGKEIKILKELKHENIVALYDFQEIANSVYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG---------ELKIADFGWSVH 224
Cdd:cd14202   80 MEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFARY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APS-LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET---YRRIVKVDLKFPASVPMGA 300
Cdd:cd14202  160 LQNnMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLrlfYEKNKSLSPNIPRETSSHL 239
                        250       260
                 ....*....|....*....|....*..
gi 927602445 301 QDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14202  240 RQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
80-327 1.93e-35

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


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 129.44  E-value: 1.93e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALK-VLFKS--QIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd06632    5 GQLLGSGSFGSVYEGFNGDTGDFFAVKeVSLVDddKKSRESVK-QLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR-KTMCG 235
Cdd:cd06632   84 VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFaKSFKG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMI--EGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKV----DL-KFPASVPMGAQDLISKLL 308
Cdd:cd06632  164 SPYWMAPEVImqKNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFKIgnsgELpPIPDHLSPDAKDFIRLCL 240
                        250
                 ....*....|....*....
gi 927602445 309 RHNPSERLPLAQVSAHPWV 327
Cdd:cd06632  241 QRDPEDRPTASQLLEHPFV 259
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
74-333 2.14e-35

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 129.86  E-value: 2.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd06611    4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKII---QIESEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWIL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGEL---YKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSL-- 228
Cdd:cd06611   81 IEFCDGGALdsiMLELERG--LTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTlq 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMI-----EGRMHNEKVDLWCIGVLCYELLVGNPPfesasHNETYrrIVKVDLKFPASVP------ 297
Cdd:cd06611  159 KRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPP-----HHELN--PMRVLLKILKSEPptldqp 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 927602445 298 ----MGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRR 333
Cdd:cd06611  232 skwsSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQSDN 271
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
77-326 2.44e-35

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 129.12  E-value: 2.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhqlrREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKIDENVQ----REIINHRSLRHPNIIRFKEVVLTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLL--GLKGELKIADFGWS----VHApslRR 230
Cdd:cd14662   78 AAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLdgSPAPRLKICDFGYSkssvLHS---QP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKV-DLWCIGVLCYELLVGNPPFESASHNETYR----RIVKVDLKFP--ASVPMGAQDL 303
Cdd:cd14662  155 KSTVGTPAYIAPEVLSRKEYDGKVaDVWSCGVTLYVMLVGAYPFEDPDDPKNFRktiqRIMSVQYKIPdyVRVSQDCRHL 234
                        250       260
                 ....*....|....*....|...
gi 927602445 304 ISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14662  235 LSRIFVANPAKRITIPEIKNHPW 257
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
74-304 2.78e-35

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 131.72  E-value: 2.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-IEKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd05627    1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADmLEKEQVAH-IRAERDILVEADGAWVVKMFYSFQDKRNLYL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---------- 222
Cdd:cd05627   80 IMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCtglkkahrte 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 -----VHAP---------SLRRK-------------TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFES 275
Cdd:cd05627  160 fyrnlTHNPpsdfsfqnmNSKRKaetwkknrrqlaySTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCS 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 276 ASHNETYRRIV--KVDLKFPASVPMG--AQDLI 304
Cdd:cd05627  240 ETPQETYRKVMnwKETLVFPPEVPISekAKDLI 272
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
83-328 3.68e-35

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 129.76  E-value: 3.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVlfksqIEKEGVEHQLR--REIEIQAHLH-HPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd14174   10 LGEGAYAKVQGCVSLQNGKEYAVKI-----IEKNAGHSRSRvfREVETLYQCQgNKNILELIEFFEDDTRFYLVFEKLRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGW-----------SVHA 225
Cdd:cd14174   85 GSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENilcESPDKVSPVKICDFDLgsgvklnsactPITT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLrrKTMCGTLDYLPPEMIE-----GRMHNEKVDLWCIGVLCYELLVGNPPFES---------------ASHNETYRRI 285
Cdd:cd14174  165 PEL--TTPCGSAEYMAPEVVEvftdeATFYDKRCDLWSLGVILYIMLSGYPPFVGhcgtdcgwdrgevcrVCQNKLFESI 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 927602445 286 VKVDLKFP----ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd14174  243 QEGKYEFPdkdwSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
75-328 7.77e-35

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 130.74  E-value: 7.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05629    1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS------------ 222
Cdd:cd05629   81 EFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsayy 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 --------------------VHAPSL--------------RRK---TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYE 265
Cdd:cd05629  161 qkllqgksnknridnrnsvaVDSINLtmsskdqiatwkknRRLmaySTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFE 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 266 LLVGNPPFESASHNETYRRIV--KVDLKFPASVPMG--AQDLISKLLRHnPSERL---PLAQVSAHPWVR 328
Cdd:cd05629  241 CLIGWPPFCSENSHETYRKIInwRETLYFPDDIHLSveAEDLIRRLITN-AENRLgrgGAHEIKSHPFFR 309
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
83-343 1.18e-34

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 127.98  E-value: 1.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQlrREIEIQAHLHH---PNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDVSDIQ--KEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELyKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG--WSVHAPSLRRKTMCGTL 237
Cdd:cd06917   87 GSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGvaASLNQNSSKRSTFVGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKVDLKFPASVPMGA-----QDLISKLLRHN 311
Cdd:cd06917  166 YWMAPEVItEGKYYDTKADIWSLGITTYEMATGNPPY---SDVDALRAVMLIPKSKPPRLEGNGyspllKEFVAACLDEE 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 927602445 312 PSERLPLAQVSAHPWVRANSRrvLPPSALQSV 343
Cdd:cd06917  243 PKDRLSADELLKSKWIKQHSK--TPTSVLKEL 272
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
76-325 1.31e-34

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 127.16  E-value: 1.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQ-LRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKE--ERQaALNEVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCT--FDEQRTATIMEELADALMYCHGKKVIHRDIKPEN-LLLGLKGELKIADFGWS-VHAPSLRR 230
Cdd:cd08220   79 EYAPGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNiLLNKKRTVVKIGDFGISkILSSKSKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASV-PMGAQDLISKLLR 309
Cdd:cd08220  159 YTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFAPISDRySEELRHLILSMLH 238
                        250
                 ....*....|....*.
gi 927602445 310 HNPSERLPLAQVSAHP 325
Cdd:cd08220  239 LDPNKRPTLSEIMAQP 254
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
77-326 1.90e-34

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: 127.68  E-value: 1.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLY----NYFYDRRR--I 150
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKI-RMENEKEGFPITAIREIKLLQKLDHPNVVRLKeivtSKGSAKYKgsI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPR---GELYKELQKsctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW-----S 222
Cdd:cd07840   80 YMVFEYMDHdltGLLDNPEVK---FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLarpytK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRRKTMcgTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPF---------------------------- 273
Cdd:cd07840  157 ENNADYTNRVI--TLWYRPPELLLGaTRYGPEVDMWSVGCILAELFTGKPIFqgkteleqlekifelcgspteenwpgvs 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 274 -----ESASHNETYRRIVKVdlKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07840  235 dlpwfENLKPKKPYKRRLRE--VFKNVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
75-327 2.20e-34

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: 126.66  E-value: 2.20e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKvLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14191    2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGK-FFKAYSAKE--KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA--DFGWS---VHAPSL 228
Cdd:cd14191   79 EMVSGGELFERIiDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKliDFGLArrlENAGSL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 rrKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQDLI 304
Cdd:cd14191  159 --KVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFI 236
                        250       260
                 ....*....|....*....|...
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14191  237 SNLLKKDMKARLTCTQCLQHPWL 259
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
72-327 2.30e-34

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 126.96  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIgrpLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14190    4 FSIHSKEV---LGGGKFGKVHTCTEKRTGLKLAAKVI-NKQNSKD--KEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL--LLGLKGELKIADFGWS-VHAPS 227
Cdd:cd14190   78 LFMEYVEGGELFERIvDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENIlcVNRTGHQVKIIDFGLArRYNPR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQDL 303
Cdd:cd14190  158 EKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDF 237
                        250       260
                 ....*....|....*....|....
gi 927602445 304 ISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14190  238 VSNLIIKERSARMSATQCLKHPWL 261
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
83-337 2.64e-34

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 128.19  E-value: 2.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQL--RREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGELFAIKALKKGDIiARDEVESLMceKRIFETVNSARHPFLVNLFACFQTPEHVCFVMEYAAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKScTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRRKTMCGTL 237
Cdd:cd05589   87 GDLMMHIHED-VFSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEgmGFGDRTSTFCGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERL- 316
Cdd:cd05589  166 EFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNPERRLg 245
                        250       260       270
                 ....*....|....*....|....*....|.
gi 927602445 317 ----PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05589  246 aserDAEDVKKQPffrnidWEALLARKIKPP 276
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
78-326 2.75e-34

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 127.06  E-value: 2.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRpLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEkEGVEHQLRREIE-IQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd07832    4 ILGR-IGEGAHGIVFKAKDRETGETVALKKVALRKLE-GGIPNQALREIKaLQACQGHPYVVKLRDVFPHGTGFVLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRG--ELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV--HAPSLRRKT 232
Cdd:cd07832   82 MLSSlsEVLRDEERP--LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARlfSEEDPRLYS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 -MCGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-------------------DLK 291
Cdd:cd07832  160 hQVATRWYRAPELLYGsRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTlgtpnektwpeltslpdynKIT 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 927602445 292 FPASVPM-----------GAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07832  240 FPESKGIrleeifpdcspEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
83-337 2.91e-34

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 128.14  E-value: 2.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd05620    3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVlIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW---SVHAPSlRRKTMCGTLD 238
Cdd:cd05620   83 LMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMckeNVFGDN-RASTFCGTPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPL 318
Cdd:cd05620  162 YIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLGV 241
                        250       260
                 ....*....|....*....|....*.
gi 927602445 319 -AQVSAHP------WVRANSRRVLPP 337
Cdd:cd05620  242 vGNIRGHPffktinWTALEKRELDPP 267
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
83-327 3.44e-34

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


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 126.71  E-value: 3.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKE----------GVEHQLR----------REIEIQAHLHHPNILRLYN 142
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLLKQagffrrppprRKPGALGkpldpldrvyREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 143 YFYD--RRRIYLILEYAPRGELYkELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG 220
Cdd:cd14118   82 VLDDpnEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 WS--VHAPSLRRKTMCGTLDYLPPEMIEGRMHN---EKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPAS 295
Cdd:cd14118  161 VSneFEGDDALLSSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPDD 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 296 VPMGAQ--DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14118  241 PVVSEQlkDLILRMLDKNPSERITLPEIKEHPWV 274
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
76-326 3.91e-34

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


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 126.75  E-value: 3.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNLILRNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS------------- 222
Cdd:cd05609   81 YVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSkiglmslttnlye 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 ----VHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPAS--- 295
Cdd:cd05609  161 ghieKDTREFLDKQVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGdda 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 296 VPMGAQDLISKLLRHNPSERLPLA---QVSAHPW 326
Cdd:cd05609  241 LPDDAQDLITRLLQQNPLERLGTGgaeEVKQHPF 274
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
75-326 4.00e-34

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 128.17  E-value: 4.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFI-VALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:PTZ00426  30 EDFNFIRTLGTGSFGRVILATYKNEDFPpVAIKRFEKSKIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRRKTM 233
Cdd:PTZ00426 110 LEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFA-KVVDTRTYTL 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:PTZ00426 189 CGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLT 268
                        250
                 ....*....|....*...
gi 927602445 314 ERL-----PLAQVSAHPW 326
Cdd:PTZ00426 269 KRYgnlkkGAQNVKEHPW 286
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
113-327 1.15e-33

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 125.52  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 113 IEKEGVEHQLR--REIEIQAHLH-HPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALM 189
Cdd:cd14173   35 IEKRPGHSRSRvfREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALD 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 190 YCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWS-----------VHAPSLRrkTMCGTLDYLPPEMI-----EGRMH 250
Cdd:cd14173  115 FLHNKGIAHRDLKPENilcEHPNQVSPVKICDFDLGsgiklnsdcspISTPELL--TPCGSAEYMAPEVVeafneEASIY 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 251 NEKVDLWCIGVLCYELLVGNPPFES---------------ASHNETYRRIVKVDLKFP----ASVPMGAQDLISKLLRHN 311
Cdd:cd14173  193 DKRCDLWSLGVILYIMLSGYPPFVGrcgsdcgwdrgeacpACQNMLFESIQEGKYEFPekdwAHISCAAKDLISKLLVRD 272
                        250
                 ....*....|....*.
gi 927602445 312 PSERLPLAQVSAHPWV 327
Cdd:cd14173  273 AKQRLSAAQVLQHPWV 288
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
75-327 1.19e-33

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 125.10  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIG-RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRreieIQAHLHHPNILRLY-NYFYDRRRIYL 152
Cdd:cd14172    3 DDYKLSkQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARREVEHHWR----ASGGPHIVHILDVYeNMHHGKRCLLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGW----SV 223
Cdd:cd14172   79 IMECMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENllyTSKEKDAVLKLTDFGFaketTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPslrRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFES----ASHNETYRRIVKVDLKFP----AS 295
Cdd:cd14172  159 QNA---LQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSntgqAISPGMKRRIRMGQYGFPnpewAE 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 927602445 296 VPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14172  236 VSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
80-327 2.54e-33

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 124.00  E-value: 2.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEH--QLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd06625    5 GKLLGQGAFGQVYLCYDADTGRELAVKQVEIDPINTEASKEvkALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMC--- 234
Cdd:cd06625   85 PGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSSTGMksv 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 -GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPP---FES-------ASHNETYrrivkvdlKFPASVPMGAQDL 303
Cdd:cd06625  165 tGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPwaeFEPmaaifkiATQPTNP--------QLPPHVSEDARDF 236
                        250       260
                 ....*....|....*....|....
gi 927602445 304 ISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06625  237 LSLIFVRNKKQRPSAEELLSHSFV 260
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
75-327 2.98e-33

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


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 123.99  E-value: 2.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEAL--QKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTM 233
Cdd:cd06605   79 EYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSLAKTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN------ETYRRIVKVDlkfPASVPMG-----AQD 302
Cdd:cd06605  159 VGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKpsmmifELLSYIVDEP---PPLLPSGkfspdFQD 235
                        250       260
                 ....*....|....*....|....*
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06605  236 FVSQCLQKDPTERPSYKELMEHPFI 260
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
124-326 6.92e-33

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 123.10  E-value: 6.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 124 REIEIQAHLH-HPNILRLYNYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIK 202
Cdd:cd14182   58 KEIDILRKVSgHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 203 PENLLLGLKGELKIADFGWSVH-APSLRRKTMCGTLDYLPPEMIEGRMHNE------KVDLWCIGVLCYELLVGNPPFES 275
Cdd:cd14182  138 PENILLDDDMNIKLTDFGFSCQlDPGEKLREVCGTPGYLAPEIIECSMDDNhpgygkEVDMWSTGVIMYTLLAGSPPFWH 217
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 276 ASHNETYRRIVKVDLKFPA----SVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14182  218 RKQMLMLRMIMSGNYQFGSpewdDRSDTVKDLISRFLVVQPQKRYTAEEALAHPF 272
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
77-327 7.93e-33

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 122.66  E-value: 7.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYF-YDRRRIYLILE 155
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIeVANGRLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRgELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN-LLLGLKGELKIADFGWS--VHAPSLRRKT 232
Cdd:cd14164   82 AAAT-DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENiLLSADDRKIKIADFGFArfVEDYPELSTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHN-EKVDLWCIGVLCYELLVGNPPFESASHNETyrRIVKVDLKFPASVPMG--AQDLISKLLR 309
Cdd:cd14164  161 FCGSRAYTPPEVILGTPYDpKKYDVWSLGVVLYVMVTGTMPFDETNVRRL--RLQQRGVLYPSGVALEepCRALIRTLLQ 238
                        250
                 ....*....|....*...
gi 927602445 310 HNPSERLPLAQVSAHPWV 327
Cdd:cd14164  239 FNPSTRPSIQQVAGNSWL 256
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
77-340 1.25e-32

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 123.07  E-value: 1.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIE--KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKeaKDGINFTALREIKLLQELKHPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPrGELYKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRK 231
Cdd:cd07841   82 EFME-TDLEKVIKdKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLarSFGSPNRKMT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV---------------------- 288
Cdd:cd07841  161 HQVVTRWYRAPELLFGaRHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEAlgtpteenwpgvtslpdyvefk 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 289 -----DLK--FPAsVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVrANSRRVLPPSAL 340
Cdd:cd07841  241 pfpptPLKqiFPA-ASDDALDLLQRLLTLNPNKRITARQALEHPYF-SNDPAPTPPSQL 297
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
75-327 1.55e-32

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 121.60  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVlfksqIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd06612    3 EVFDILEKLGEGSYGSVYKAIHKETGQVVAIKV-----VPVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELyKELQKSC--TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS--LRR 230
Cdd:cd06612   78 EYCGAGSV-SDIMKITnkTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDtmAKR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKV------DLKFPASVPMGAQDLI 304
Cdd:cd06612  157 NTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY---SDIHPMRAIFMIpnkpppTLSDPEKWSPEFNDFV 233
                        250       260
                 ....*....|....*....|...
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06612  234 KKCLVKDPEERPSAIQLLQHPFI 256
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
75-334 3.19e-32

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 122.27  E-value: 3.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVY--LAREKKSHFIVALKVLFK-SQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14094    3 DVYELCEVIGKGPFSVVRrcIHRETGQQFAVKIVDVAKfTSSPGLSTE-DLKREASICHMLKHPHIVELLETYSSDGMLY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCT----FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL---KIADFGWSVH 224
Cdd:cd14094   82 MVFEFMDGADLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSapvKLGGFGVAIQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKT--MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFeSASHNETYRRIVKVDLKFPA----SVPM 298
Cdd:cd14094  162 LGESGLVAggRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPF-YGTKERLFEGIIKGKYKMNPrqwsHISE 240
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 927602445 299 GAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRV 334
Cdd:cd14094  241 SAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYA 276
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
81-315 3.79e-32

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 120.72  E-value: 3.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAR---EKKSHFIVALKVL--FKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd00192    1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTLkeDASESERK----DFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKS-CTFDEQRTATI-MEEL-------ADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV-HA 225
Cdd:cd00192   77 YMEGGDLLDFLRKSrPVFPSPEPSTLsLKDLlsfaiqiAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRdIY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCGTLD---YLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGA 300
Cdd:cd00192  157 DDDYYRKKTGGKLpirWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKgYRLPKPENCPDEL 236
                        250
                 ....*....|....*
gi 927602445 301 QDLISKLLRHNPSER 315
Cdd:cd00192  237 YELMLSCWQLDPEDR 251
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
78-326 4.04e-32

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: 120.86  E-value: 4.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRplgkGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREieiqahLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd14010    7 EIGR----GKHSVVYKGRRKGTIEFVAIKCVDKSKRPEVLNEVRLTHE------LKHPNVLKFYEWYETSNHLWLVVEYC 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--------------- 222
Cdd:cd14010   77 TGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeilkelfgqfs 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 ----VHAPSLRRKTMcGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP---AS 295
Cdd:cd14010  157 degnVNKVSKKQAKR-GTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEDPPPPppkVS 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 296 VPMGA--QDLISKLLRHNPSERLPLAQVSAHP-W 326
Cdd:cd14010  236 SKPSPdfKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
79-327 4.26e-32

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 120.69  E-value: 4.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEG-VEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd14070    6 IGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSyVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLVMELC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK----TM 233
Cdd:cd14070   86 PGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSdpfsTQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF--ESASHNETYRRIVKVDLK-FPASVPMGAQDLISKLLRH 310
Cdd:cd14070  166 CGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFtvEPFSLRALHQKMVDKEMNpLPTDLSPGAISFLRSLLEP 245
                        250
                 ....*....|....*..
gi 927602445 311 NPSERLPLAQVSAHPWV 327
Cdd:cd14070  246 DPLKRPNIKQALANRWL 262
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
77-325 4.87e-32

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


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 121.46  E-value: 4.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALK-VL----FKSqiekegvehqlrREIEIQAHLHHPNILRLYNYFY----DR 147
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkVLqdkrYKN------------RELQIMRRLKHPNIVKLKYFFYssgeKK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYL--ILEYAPrGELYKELqKSCTFDEQRTATI-----MEELADALMYCHGKKVIHRDIKPENL-LLGLKGELKIADF 219
Cdd:cd14137   74 DEVYLnlVMEYMP-ETLYRVI-RHYSKNKQTIPIIyvklySYQLFRGLAYLHSLGICHRDIKPQNLlVDPETGVLKLCDF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 220 GwSvhAPSLRRKTMC----GTLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV------ 288
Cdd:cd14137  152 G-S--AKRLVPGEPNvsyiCSRYYRAPELIFGATDyTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVlgtptr 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 289 -DLK----------------------FPASVPMGAQDLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd14137  229 eQIKamnpnytefkfpqikphpwekvFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
83-327 5.69e-32

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 120.46  E-value: 5.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHqlrrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14113   15 LGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKRDQVTH----ELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAPSLRR-KTMCGTLD 238
Cdd:cd14113   91 LDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENilvDQSLSKPTIKLADFGDAVQLNTTYYiHQLLGSPE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQDLISKLLRHNPSE 314
Cdd:cd14113  171 FAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLLQMDPAK 250
                        250
                 ....*....|...
gi 927602445 315 RLPLAQVSAHPWV 327
Cdd:cd14113  251 RPSAALCLQEQWL 263
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
75-304 6.03e-32

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 123.23  E-value: 6.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-IEKEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05628    1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADmLEKEQVGH-IRAERDILVEADSLWVVKMFYSFQDKLNLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------------- 220
Cdd:cd05628   80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGlctglkkahrtef 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 -----------WSVHAPSLRRK-------------TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESA 276
Cdd:cd05628  160 yrnlnhslpsdFTFQNMNSKRKaetwkrnrrqlafSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                        250       260       270
                 ....*....|....*....|....*....|..
gi 927602445 277 SHNETYRRIV--KVDLKFPASVPMG--AQDLI 304
Cdd:cd05628  240 TPQETYKKVMnwKETLIFPPEVPISekAKDLI 271
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
75-341 6.09e-32

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 121.29  E-value: 6.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvehqlrREIEI-QAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14175    1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS-------EEIEIlLRYGQHPNIITLKDVYDDGKHVYLV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG----ELKIADFGWsvhAPSLR 229
Cdd:cd14175   74 TELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESgnpeSLRICDFGF---AKQLR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RK-----TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFE---SASHNETYRRIVKVDLKFPA----SVP 297
Cdd:cd14175  151 AEngllmTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFTLSGgnwnTVS 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 927602445 298 MGAQDLISKLLRHNPSERLPLAQVSAHPWVraNSRRVLPPSALQ 341
Cdd:cd14175  231 DAAKDLVSKMLHVDPHQRLTAKQVLQHPWI--TQKDKLPQSQLN 272
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
75-328 6.25e-32

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


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 123.19  E-value: 6.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05621   52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKeLQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS---LRRK 231
Cdd:cd05621  132 EYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDEtgmVHCD 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGR----MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPASVPMG--AQDL 303
Cdd:cd05621  211 TAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhKNSLNFPDDVEISkhAKNL 290
                        250       260
                 ....*....|....*....|....*..
gi 927602445 304 ISKLL--RHNPSERLPLAQVSAHPWVR 328
Cdd:cd05621  291 ICAFLtdREVRLGRNGVEEIKQHPFFR 317
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
77-327 9.75e-32

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: 119.68  E-value: 9.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREK--KSHFIVALKVLFKSQI-EKEGVehqlRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKsdSEHCVIKEIDLTKMPVkEKEAS----KKEVILLAKMKHPNIVTFFASFQENGRLFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKEL--QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLK-GELKIADFGWS--VHAPSL 228
Cdd:cd08225   78 MEYCDGGDLMKRInrQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNgMVAKLGDFGIArqLNDSME 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVdlKFPASVPMGAQD---LIS 305
Cdd:cd08225  158 LAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQG--YFAPISPNFSRDlrsLIS 235
                        250       260
                 ....*....|....*....|..
gi 927602445 306 KLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd08225  236 QLFKVSPRDRPSITSILKRPFL 257
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
77-315 1.47e-31

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 119.38  E-value: 1.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKS----QIEKEGVEHQLRREIEIQAHLH-HPNILRLYNYFYDRRRIY 151
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnsKDGNDFQKLPQLREIDLHRRVSrHPNIITLHDVFETEVAIY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRT--ATIMEELADALMYCHGKKVIHRDIKPEN-LLLGLKGELKIADFGWSVHAPsL 228
Cdd:cd13993   82 IVLEYCPNGDLFEAITENRIYVGKTEliKNVFLQLIDAVKHCHSLGIYHRDIKPENiLLSQDEGTVKLCDFGLATTEK-I 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIE--GRMHNE----KVDLWCIGVLCYELLVGNPPFESASHNE--TYRRIVKVDLKFPASVPMgA 300
Cdd:cd13993  161 SMDFGVGSEFYMAPECFDevGRSLKGypcaAGDIWSLGIILLNLTFGRNPWKIASESDpiFYDYYLNSPNLFDVILPM-S 239
                        250
                 ....*....|....*...
gi 927602445 301 QD---LISKLLRHNPSER 315
Cdd:cd13993  240 DDfynLLRQIFTVNPNNR 257
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
75-325 1.83e-31

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 119.38  E-value: 1.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKV--LFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRidLEKCQTSMD----ELRKEIQAMSQCNHPNVVSYYTSFVVGDELWL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELY---KELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS------V 223
Cdd:cd06610   77 VMPLLSGGSLLdimKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSaslatgG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTMCGTLDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKVDLKFPASVPMGAQ- 301
Cdd:cd06610  157 DRTRKVRKTFVGTPCWMAPEvMEQVRGYDFKADIWSFGITAIELATGAAPY---SKYPPMKVLMLTLQNDPPSLETGADy 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 927602445 302 --------DLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd06610  234 kkysksfrKMISLCLQKDPSKRPTAEELLKHK 265
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
77-335 2.36e-31

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 119.75  E-value: 2.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLrrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd06644   14 WEIIGELGDGAFGKVYKAKNKETGALAAAKVI-ETKSEEELEDYMV--EIEILATCNHPYIVKLLGAFYWDGKLWIMIEF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGE---LYKELQKSCTfdEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsVHAPSL----R 229
Cdd:cd06644   91 CPGGAvdaIMLELDRGLT--EPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFG--VSAKNVktlqR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMI-----EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVD---LKFPASVPMGAQ 301
Cdd:cd06644  167 RDSFIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFR 246
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPWV-RANSRRVL 335
Cdd:cd06644  247 DFLKTALDKHPETRPSAAQLLEHPFVsSVTSNRPL 281
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
78-315 2.56e-31

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 118.40  E-value: 2.56e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445    78 EIGRPLGKGKFGNVYLAR----EKKSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEQQ--IEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   154 LEYAPRGELYKELQKS-CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT 232
Cdd:smart00219  80 MEYMEGGDLLSYLRKNrPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   233 MCGT---LDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVD-LKFPASVPMGAQDLISKL 307
Cdd:smart00219 160 KRGGklpIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEYLKNGYrLPQPPNCPPELYDLMLQC 239

                   ....*...
gi 927602445   308 LRHNPSER 315
Cdd:smart00219 240 WAEDPEDR 247
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
76-272 2.80e-31

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 118.56  E-value: 2.80e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfkSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVI--KLEPGDDFE-IIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTM 233
Cdd:cd06613   78 YCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSaqLTATIAKRKSF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 927602445 234 CGTLDYLPPEMIEGRM---HNEKVDLWCIGVLCYELLVGNPP 272
Cdd:cd06613  158 IGTPYWMAPEVAAVERkggYDGKCDIWALGITAIELAELQPP 199
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
75-337 3.37e-31

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 121.65  E-value: 3.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKeLQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS---LRRK 231
Cdd:cd05622  153 EYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKegmVRCD 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGR----MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFP--ASVPMGAQDL 303
Cdd:cd05622  232 TAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMnhKNSLTFPddNDISKEAKNL 311
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 927602445 304 ISKLL--RHNPSERLPLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05622  312 ICAFLtdREVRLGRNGVEEIKRHLffkndqWAWETLRDTVAP 353
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
83-327 3.79e-31

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: 118.14  E-value: 3.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEGVehqlRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAAKIIkVKGAKEREEV----KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL--LLGLKGELKIADFGWS-VHAPSLRRKTMCGTL 237
Cdd:cd14192   88 LFDRItDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENIlcVNSTGNQIKIIDFGLArRYKPREKLKVNFGTP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKLLRHNPS 313
Cdd:cd14192  168 EFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDAeafeNLSEEAKDFISRLLVKEKS 247
                        250
                 ....*....|....
gi 927602445 314 ERLPLAQVSAHPWV 327
Cdd:cd14192  248 CRMSATQCLKHEWL 261
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
83-326 4.65e-31

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


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 118.55  E-value: 4.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYaprgeL 162
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALKKI-RLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLYLVFEF-----L 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQK------SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPsLRRKTM- 233
Cdd:cd07835   81 DLDLKKymdsspLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLAraFGVP-VRTYTHe 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----------------DLK--FP- 293
Cdd:cd07835  160 VVTLWYRAPEILLGsKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTlgtpdedvwpgvtslpDYKptFPk 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 294 -ASVPMG---------AQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07835  240 wARQDLSkvvpsldedGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
69-327 6.31e-31

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 119.74  E-value: 6.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  69 TRHFTiDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIE-KEGVEHQLRreieiqaHLHHPNILRLYNYFYDR 147
Cdd:cd14176   14 SIQFT-DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDpTEEIEILLR-------YGQHPNIITLKDVYDDG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG----ELKIADFGWsv 223
Cdd:cd14176   86 KYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGF-- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 hAPSLRRK-----TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN---ETYRRIVKVDLKFPA- 294
Cdd:cd14176  164 -AKQLRAEngllmTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDtpeEILARIGSGKFSLSGg 242
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 927602445 295 ---SVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14176  243 ywnSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
74-337 6.89e-31

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 120.14  E-value: 6.89e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEH-QLRREIEIQAHlHHPNILRLYNYFYDRRRIY 151
Cdd:cd05618   19 LQDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVnDDEDIDWvQTEKHVFEQAS-NHPFLVGLHSCFQTESRLF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA--PSLR 229
Cdd:cd05618   98 FVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGlrPGDT 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET---------YRRIVKVDLKFPASVPMGA 300
Cdd:cd05618  178 TSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNpdqntedylFQVILEKQIRIPRSLSVKA 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 927602445 301 QDLISKLLRHNPSERL------PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05618  258 ASVLKSFLNKDPKERLgchpqtGFADIQGHPffrnvdWDLMEQKQVVPP 306
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
74-327 9.55e-31

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: 118.37  E-value: 9.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLY----------NY 143
Cdd:cd07864    6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKV-RLDNEKEGFPITAIREIKILRQLNHRSVVNLKeivtdkqdalDF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 144 FYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS- 222
Cdd:cd07864   85 KKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLAr 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 -VHAPSLRRKT-MCGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASH--------------------- 278
Cdd:cd07864  165 lYNSEESRPYTnKVITLWYRPPELLLGeERYGPAIDVWSCGCILGELFTKKPIFQANQElaqlelisrlcgspcpavwpd 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 279 ------------NETYRRIVKVDLKFpasVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07864  245 viklpyfntmkpKKQYRRRLREEFSF---IPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
78-315 9.78e-31

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 116.88  E-value: 9.78e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445    78 EIGRPLGKGKFGNVYLAR----EKKSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDASEQQ--IEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   154 LEYAPRGELYKELQKSctfdeqRTATI-MEEL-------ADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA 225
Cdd:smart00221  80 MEYMPGGDLLDYLRKN------RPKELsLSDLlsfalqiARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   226 PSLRRKTMCGT---LDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVD-LKFPASVPMGA 300
Cdd:smart00221 154 YDDDYYKVKGGklpIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFtLGEEPYPGMSNAEVLEYLKKGYrLPKPPNCPPEL 233
                          250
                   ....*....|....*
gi 927602445   301 QDLISKLLRHNPSER 315
Cdd:smart00221 234 YKLMLQCWAEDPEDR 248
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
80-337 1.06e-30

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 118.44  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSqiekegVEHQLRREIE-IQAHLHHPNILRLYNYFYDRRRIYLILEYAP 158
Cdd:cd14180   11 EPALGEGSFSVCRKCRHRQSGQEYAVKIISRR------MEANTQREVAaLRLCQSHPNIVALHEVLHDQYHTYLVMELLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWS--VHAPSLRRKTM 233
Cdd:cd14180   85 GGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENilyADESDGAVLKVIDFGFArlRPQGSRPLQTP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESAS----HNETYRRIVKV-------DLKFPASVPMGAQD 302
Cdd:cd14180  165 CFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRgkmfHNHAADIMHKIkegdfslEGEAWKGVSEEAKD 244
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPP 337
Cdd:cd14180  245 LVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTP 279
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
76-321 1.29e-30

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 116.99  E-value: 1.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfKSQIeKEGVEHQLR----REIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALK---KVQI-FEMMDAKARqdclKEIDLLQQLNHPNIIKYLASFIENNELN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELyKELQKSCT-----FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VH 224
Cdd:cd08224   77 IVLELADAGDL-SRLIKHFKkqkrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGrfFS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN--ETYRRIVKVDLK-FPA-SVPMGA 300
Cdd:cd08224  156 SKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPpLPAdLYSQEL 235
                        250       260
                 ....*....|....*....|.
gi 927602445 301 QDLISKLLRHNPSERLPLAQV 321
Cdd:cd08224  236 RDLVAACIQPDPEKRPDISYV 256
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
83-315 4.58e-30

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 115.29  E-value: 4.58e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd08218    8 IGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKERE-ESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKEL--QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLD 238
Cdd:cd08218   87 YKRInaQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIArvLNSTVELARTCIGTPY 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL-KFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd08218  167 YLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKRNPRDR 244
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
68-320 6.00e-30

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: 115.54  E-value: 6.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  68 LTRHFTidDFEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfKSQI-EKEGVEHQLRREIEIQAHLHHPNILRLYNYFYD 146
Cdd:cd14046    1 FSRYLT--DFEELQVLGKGAFGQVVKVRNKLDGRYYAIK---KIKLrSESKNNSRILREVMLLSRLNHQHVVRYYQAWIE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 147 RRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---- 222
Cdd:cd14046   76 RANLYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAtsnk 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 ---VHAPSLRRKT-------------MCGTLDYLPPEMIEGR--MHNEKVDLWCIGVLCYELLVgnpPFESASHNETYRR 284
Cdd:cd14046  156 lnvELATQDINKStsaalgssgdltgNVGTALYVAPEVQSGTksTYNEKVDMYSLGIIFFEMCY---PFSTGMERVQILT 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 927602445 285 IVK-----VDLKFPASVPMGAQDLISKLLRHNPSERlPLAQ 320
Cdd:cd14046  233 ALRsvsieFPPDFDDNKHSKQAKLIRWLLNHDPAKR-PSAQ 272
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
83-328 7.23e-30

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


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 114.85  E-value: 7.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVK---KMDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGAL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 yKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW----SVHAPslRRKTMCGTLD 238
Cdd:cd06648   92 -TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFcaqvSKEVP--RRKSLVGTPY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVD---LKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd06648  169 WMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEppkLKNLHKVSPRLRSFLDRMLVRDPAQR 248
                        250
                 ....*....|...
gi 927602445 316 LPLAQVSAHPWVR 328
Cdd:cd06648  249 ATAAELLNHPFLA 261
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
77-327 9.06e-30

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: 114.67  E-value: 9.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQieKEGVEhQLRREIEIQAHLH------HPNILRLYNYFYDRRRI 150
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII-KNN--KDYLD-QSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYApRGELYKELQKSCT--FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA--DFGWSVHAP 226
Cdd:cd14133   77 CIVFELL-SQNLYEFLKQNKFqyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKiiDFGSSCFLT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SlRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASvpMGAQ----- 301
Cdd:cd14133  156 Q-RLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAH--MLDQgkadd 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 927602445 302 ----DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14133  233 elfvDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
75-337 9.08e-30

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 116.29  E-value: 9.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKsctFDEQrtatIMEELAD--------ALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP 226
Cdd:cd05597   81 DYYCGGDLLTLLSK---FEDR----LPEEMARfylaemvlAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKLR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 S---LRRKTMCGTLDYLPPEMIE------GRMHNEkVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPAS 295
Cdd:cd05597  154 EdgtVQSSVAVGTPDYISPEILQamedgkGRYGPE-CDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKEHFSFPDD 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 296 ---VPMGAQDLISKLLrHNPSERL---PLAQVSAHPWVRA----NSRRVLPP 337
Cdd:cd05597  233 eddVSEEAKDLIRRLI-CSRERRLgqnGIDDFKKHPFFEGidwdNIRDSTPP 283
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
83-326 1.17e-29

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 114.72  E-value: 1.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVlfkSQIEKEGVEHQLR-------REIEIQAHLHHPNILRLYNYF-YDRRRIYLIL 154
Cdd:cd13990    8 LGKGGFSEVYKAFDLVEQRYVACKI---HQLNKDWSEEKKQnyikhalREYEIHKSLDHPRIVKLYDVFeIDTDSFCTVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPEN---LLLGLKGELKIADFGWS--VHAPS 227
Cdd:cd13990   85 EYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNillHSGNVSGEIKITDFGLSkiMDDES 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTM------CGTLDYLPPEMI----EGRMHNEKVDLWCIGVLCYELLVGNPPF------ESASHNETYRRIVKVDLK 291
Cdd:cd13990  165 YNSDGMeltsqgAGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQMLYGRKPFghnqsqEAILEENTILKATEVEFP 244
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 292 FPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd13990  245 SKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
75-340 1.22e-29

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 115.11  E-value: 1.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvehqlrREIEIQAHL-HHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14178    3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPS-------EEIEILLRYgQHPNIITLKDVYDDGKFVYLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG----ELKIADFGWsvhAPSLR 229
Cdd:cd14178   76 MELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGF---AKQLR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RK-----TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN---ETYRRIVKVDLKFPA----SVP 297
Cdd:cd14178  153 AEngllmTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDtpeEILARIGSGKYALSGgnwdSIS 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 298 MGAQDLISKLLRHNPSERLPLAQVSAHPWVRanSRRVLPPSAL 340
Cdd:cd14178  233 DAAKDIVSKMLHVDPHQRLTAPQVLRHPWIV--NREYLSQNQL 273
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
76-323 1.48e-29

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 114.14  E-value: 1.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKS-HFIVALKVLF-------KSQIEKEGVEHQLRREIEI-QAHLHHPNILRLYNYFYD 146
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRKKSNgQTLLALKEINmtnpafgRTEQERDKSVGDIISEVNIiKEQLRHPNIVRYYKTFLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 147 RRRIYLILEY---APRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHG-KKVIHRDIKPENLLLGLKGELKIADFGW 221
Cdd:cd08528   81 NDRLYIVMELiegAPLGEHFSSLkEKNEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDFGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 222 SVH--APSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKfPASVPMG 299
Cdd:cd08528  161 AKQkgPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE-PLPEGMY 239
                        250       260
                 ....*....|....*....|....*..
gi 927602445 300 AQDL---ISKLLRHNPSERLPLAQVSA 323
Cdd:cd08528  240 SDDItfvIRSCLTPDPEARPDIVEVSS 266
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
83-326 1.55e-29

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: 114.05  E-value: 1.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE------- 155
Cdd:cd14082   11 LGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQ-ESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEklhgdml 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 ----YAPRGELykelqksctfDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWS--VHAP 226
Cdd:cd14082   90 emilSSEKGRL----------PERITKFLVTQILVALRYLHSKNIVHCDLKPENvllASAEPFPQVKLCDFGFAriIGEK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRkTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF-ESASHNEtyrRIVKVDLKFPAS----VPMGAQ 301
Cdd:cd14082  160 SFRR-SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFnEDEDIND---QIQNAAFMYPPNpwkeISPDAI 235
                        250       260
                 ....*....|....*....|....*
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14082  236 DLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
75-327 1.86e-29

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 114.35  E-value: 1.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLrrEIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd06643    5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVI-DTKSEEELEDYMV--EIDILASCDHPNIVKLLDAFYYENNLWILI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGEL---YKELQKSCTfdEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSL--R 229
Cdd:cd06643   82 EFCAGGAVdavMLELERPLT--EPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTlqR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMI-----EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVD---LKFPASVPMGAQ 301
Cdd:cd06643  160 RDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFK 239
                        250       260
                 ....*....|....*....|....*.
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06643  240 DFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
74-337 3.34e-29

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 115.12  E-value: 3.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEH-QLRREIEIQAHlHHPNILRLYNYFYDRRRIY 151
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVhDDEDIDWvQTEKHVFEQAS-SNPFLVGLHSCFQTTSRLF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA--PSLR 229
Cdd:cd05617   93 LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGlgPGDT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET-------YRRIVKVDLKFPASVPMGAQD 302
Cdd:cd05617  173 TSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDmntedylFQVILEKPIRIPRFLSVKASH 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 927602445 303 LISKLLRHNPSERL------PLAQVSAHPWVRA------NSRRVLPP 337
Cdd:cd05617  253 VLKGFLNKDPKERLgcqpqtGFSDIKSHTFFRSidwdllEKKQVTPP 299
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
84-327 4.18e-29

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: 112.61  E-value: 4.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  84 GKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhqlrREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELY 163
Cdd:cd14111   12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGVL----QEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 164 KELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG--WSVHAPSLRRKT-MCGTLDYL 240
Cdd:cd14111   88 HSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGsaQSFNPLSLRQLGrRTGTLEYM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVD-LKFPASVPMGAQDLISKLLRHNPSERLP 317
Cdd:cd14111  168 APEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILvaKFDaFKLYPNVSQSASLFLKKVLSSYPWSRPT 247
                        250
                 ....*....|
gi 927602445 318 LAQVSAHPWV 327
Cdd:cd14111  248 TKDCFAHAWL 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
75-327 1.07e-28

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 112.01  E-value: 1.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHqlrrEIEI-QAHLHHPNILRLYNYFYDRR----- 148
Cdd:cd06608    6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEIKL----EINIlRKFSNHPNIATFYGAFIKKDppggd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 -RIYLILEYAPRG---ELYKELQKSC-TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV 223
Cdd:cd06608   82 dQLWLVMEYCGGGsvtDLVKGLRKKGkRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPS--LRRKTMCGTLDYLPPEMIE-----GRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVD---LKFP 293
Cdd:cd06608  162 QLDStlGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFKIPRNPpptLKSP 241
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 294 ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06608  242 EKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
83-326 1.11e-28

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 111.21  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHqlrrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKKEQAAH----EAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG---ELKIADFGWSVHAPSLRR-KTMCGTLD 238
Cdd:cd14115   77 LDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDAVQISGHRHvHHLLGNPE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP----ASVPMGAQDLISKLLRHNPSE 314
Cdd:cd14115  157 FAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPdeyfGDVSQAARDFINVILQEDPRR 236
                        250
                 ....*....|..
gi 927602445 315 RLPLAQVSAHPW 326
Cdd:cd14115  237 RPTAATCLQHPW 248
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
77-315 3.24e-28

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 110.28  E-value: 3.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   77 FEIGRPLGKGKFGNVYLAREKKSHF----IVALKVLfksqieKEGVEHQLR----REIEIQAHLHHPNILRLYNYFYDRR 148
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGEntkiKVAVKTL------KEGADEEERedflEEASIMKKLDHPNIVKLLGVCTQGE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  149 RIYLILEYAPRGELYKELQKSC-TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHA 225
Cdd:pfam07714  75 PLYIVTEYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSrdIYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  226 PSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK-VDLKFPASVPMGAQ 301
Cdd:pfam07714 155 DDYYRKRGGGKLpiKWMAPESLKDGKFTSKSDVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDgYRLPQPENCPDELY 234
                         250
                  ....*....|....
gi 927602445  302 DLISKLLRHNPSER 315
Cdd:pfam07714 235 DLMKQCWAYDPEDR 248
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
83-287 3.45e-28

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 110.44  E-value: 3.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAReKKSHFIVALKVLFKSqiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14066    1 IGSGGFGTVYKGV-LENGTVVAVKRLNEM--NCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFD----EQRTAtIMEELADALMYCHG---KKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLRRKT 232
Cdd:cd14066   78 EDRLHCHKGSPplpwPQRLK-IAKGIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLArliPPSESVSKTS 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 927602445 233 -MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVK 287
Cdd:cd14066  157 aVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVE 212
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
80-327 5.44e-28

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 109.93  E-value: 5.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQ------LRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd06628    5 GALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKDRKksmldaLQREIALLRELQHENIVQYLGSSSDANHLNIF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSL--- 228
Cdd:cd06628   85 LEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISkkLEANSLstk 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 ---RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRI-VKVDLKFPASVPMGAQDLI 304
Cdd:cd06628  165 nngARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIgENASPTIPSNISSEARDFL 244
                        250       260
                 ....*....|....*....|...
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06628  245 EKTFEIDHNKRPTADELLKHPFL 267
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
76-315 5.66e-28

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 109.68  E-value: 5.66e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQlRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEI-RLPKSSSAVEDS-RKEAVLLAKMKHPNIVAFKESFEADGHLYIVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKE--LQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRK 231
Cdd:cd08219   79 YCDGGDLMQKikLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSArlLTSPGAYAC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLK-FPASVPMGAQDLISKLLRH 310
Cdd:cd08219  159 TYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKR 238

                 ....*
gi 927602445 311 NPSER 315
Cdd:cd08219  239 NPRSR 243
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
83-326 1.10e-27

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 109.44  E-value: 1.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfKSQIEK--EGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPrg 160
Cdd:cd07839    8 IGEGTYGTVFKAKNRETHEIVALK---RVRLDDddEGVPSSALREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCD-- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 elyKELQK---SC--TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTM 233
Cdd:cd07839   83 ---QDLKKyfdSCngDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLarAFGIPVRCYSAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKV----------------DLKFPAS 295
Cdd:cd07839  160 VVTLWYRPPDVLFGaKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLlgtpteeswpgvsklpDYKPYPM 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 927602445 296 VPMGA-------------QDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07839  240 YPATTslvnvvpklnstgRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
80-327 1.28e-27

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: 108.93  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd06626    5 GNKIGEGTFGKVYTAVNLDTGELMAMKEI-RFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH-------APSLRRKT 232
Cdd:cd06626   84 GTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKlknntttMAPGEVNS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEK---VDLWCIGVLCYELLVGNPPFesASHNETYRRIVKVDLKFPASVP-------MGaQD 302
Cdd:cd06626  164 LVGTPAYMAPEVITGNKGEGHgraADIWSLGCVVLEMATGKRPW--SELDNEWAIMYHVGMGHKPPIPdslqlspEG-KD 240
                        250       260
                 ....*....|....*....|....*
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06626  241 FLSRCLESDPKKRPTASELLDHPFI 265
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
77-326 1.31e-27

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


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 109.13  E-value: 1.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKI-RLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 -----------APRGELYKELQKSCTFdeqrtatimeELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VH 224
Cdd:cd07860   81 lhqdlkkfmdaSALTGIPLPLIKSYLF----------QLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLArAF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTM-CGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-------------- 288
Cdd:cd07860  151 GVPVRTYTHeVVTLWYRAPEILLGcKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTlgtpdevvwpgvts 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 927602445 289 --DLK--FP--------ASVPM---GAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07860  231 mpDYKpsFPkwarqdfsKVVPPldeDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
83-328 1.44e-27

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


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 108.48  E-value: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEGVEHqlrrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIKQMnLQQQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTMCGTLDY 239
Cdd:cd06647   91 LTDVVTETC-MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcaQITPEQSKRSTMVGTPYW 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesasHNETYRRIV-------KVDLKFPASVPMGAQDLISKLLRHNP 312
Cdd:cd06647  170 MAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY----LNENPLRALyliatngTPELQNPEKLSAIFRDFLNRCLEMDV 245
                        250
                 ....*....|....*.
gi 927602445 313 SERLPLAQVSAHPWVR 328
Cdd:cd06647  246 EKRGSAKELLQHPFLK 261
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-327 1.69e-27

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 109.09  E-value: 1.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEI--GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiekegvehqlRREIEIQAHLH---HPNILRLYNYF---- 144
Cdd:cd14171    3 LEEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKILLDRP----------KARTEVRLHMMcsgHPNIVQIYDVYansv 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 145 ------YDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELK 215
Cdd:cd14171   73 qfpgesSPRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENlllKDNSEDAPIK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 216 IADFGWS-VHAPSLrrKTMCGTLDYLPPEMIEGR-----------------MHNEKVDLWCIGVLCYELLVGNPPFESAS 277
Cdd:cd14171  153 LCDFGFAkVDQGDL--MTPQFTPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFYSEH 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 278 H-----NETYRRIVKVDLKFPAS----VPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14171  231 PsrtitKDMKRKIMTGSYEFPEEewsqISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
73-326 1.79e-27

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 109.33  E-value: 1.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALK-VLFKSqiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRR-- 149
Cdd:cd07866    6 KLRDYEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHN--EKDGFPITALREIKILKKLKHPNVVPLIDMAVERPDks 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 ------IYLILEYAPR---GELYKElqkSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG 220
Cdd:cd07866   84 krkrgsVYMVTPYMDHdlsGLLENP---SVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 ----WSVHAPSLRRKTMCGTLDYL---------PPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESAS--------- 277
Cdd:cd07866  161 larpYDGPPPNPKGGGGGGTRKYTnlvvtrwyrPPELLLGeRRYTTAVDIWGIGCVFAEMFTRRPILQGKSdidqlhlif 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 278 ----------------------HNETYRRIVKVDLKFPASVPMGAqDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07866  241 klcgtpteetwpgwrslpgcegVHSFTNYPRTLEERFGKLGPEGL-DLLSKLLSLDPYKRLTASDALEHPY 310
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
77-326 1.81e-27

Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 108.78  E-value: 1.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVL---FKSqiekegVEHQLR-REIE-IQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMkkkFYS------WEECMNlREVKsLRKLNEHPNIVKLKEVFRENDELY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPrGELYK--ELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsvhapsLR 229
Cdd:cd07830   75 FVFEYME-GNLYQlmKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFG-------LA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMC--------GTLDYLPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV------------ 288
Cdd:cd07830  147 REIRSrppytdyvSTRWYRAPEILlRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVlgtptkqdwpeg 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 927602445 289 -------DLKFPASVPMG-----------AQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07830  227 yklasklGFRFPQFAPTSlhqlipnaspeAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
66-327 1.86e-27

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 108.47  E-value: 1.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  66 DILTRHFTIDDFEIGRplgkGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEI-QAHLHHPNILRLYNYF 144
Cdd:cd14198    3 DNFNNFYILTSKELGR----GKFAVVRQCISKSTGQEYAAKFL-KKRRRGQDCRAEILHEIAVlELAKSNPRVVNLHEVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 145 YDRRRIYLILEYAPRGELYKElqksCTFD------EQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL---K 215
Cdd:cd14198   78 ETTSEIILILEYAAGGEIFNL----CVPDlaemvsENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLgdiK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 216 IADFGWSV---HAPSLRRktMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKF 292
Cdd:cd14198  154 IVDFGMSRkigHACELRE--IMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDY 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 927602445 293 P----ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14198  232 SeetfSSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
81-322 1.98e-27

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 108.58  E-value: 1.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQlrrEIEIQAHL-HHPNILRLY----NYFYDRRRIYLILE 155
Cdd:cd13985    6 KQLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIK---EIEIMKRLcGHPNIVQYYdsaiLSSEGRKEVLLLME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPrGELYKELQKSCT--FDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKGELKIADFGwSV--HAPSLR 229
Cdd:cd13985   83 YCP-GSLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG-SAttEHYPLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCG----------TLDYLPPEMI---EGRMHNEKVDLWCIGVLCYELLVGNPPFESAShnetyrrIVK-VDLKFP-- 293
Cdd:cd13985  161 RAEEVNiieeeiqkntTPMYRAPEMIdlySKKPIGEKADIWALGCLLYKLCFFKLPFDESS-------KLAiVAGKYSip 233
                        250       260       270
                 ....*....|....*....|....*....|.
gi 927602445 294 --ASVPMGAQDLISKLLRHNPSERLPLAQVS 322
Cdd:cd13985  234 eqPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
77-327 2.34e-27

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 107.89  E-value: 2.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI----EKEGVehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVgelqPDETV--DANREAKLLSKLDHPAIVKFHDSFVEKESFCI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGEL---YKELQKS-CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELkIADFGWS--VHAP 226
Cdd:cd08222   80 VTEYCEGGDLddkISEYKKSgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNVIK-VGDFGISriLMGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL-KFPASVPMGAQDLIS 305
Cdd:cd08222  159 SDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYS 238
                        250       260
                 ....*....|....*....|..
gi 927602445 306 KLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd08222  239 RMLNKDPALRPSAAEILKIPFI 260
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
83-333 2.72e-27

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 108.22  E-value: 2.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06640   12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAEDE-IE-DIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YkELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLDYL 240
Cdd:cd06640   90 L-DLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAgqLTDTQIKRNTFVGTPFWM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPfESASHNetyRRIVKVDLKFPASVPMGA-----QDLISKLLRHNPSER 315
Cdd:cd06640  169 APEVIQQSAYDSKADIWSLGITAIELAKGEPP-NSDMHP---MRVLFLIPKNNPPTLVGDfskpfKEFIDACLNKDPSFR 244
                        250
                 ....*....|....*...
gi 927602445 316 LPLAQVSAHPWVRANSRR 333
Cdd:cd06640  245 PTAKELLKHKFIVKNAKK 262
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
80-325 2.85e-27

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


Pssm-ID: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 107.90  E-value: 2.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALK-VLF--KSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd06630    5 GPLLGTGAFSSCYQARDVKTGTLMAVKqVSFcrNSSSEQEEVVEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEW 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLK-GELKIADFGwsvHAPSLRRKT--- 232
Cdd:cd06630   85 MAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFG---AAARLASKGtga 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 ------MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKF-PASVP----MGAQ 301
Cdd:cd06630  162 gefqgqLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATtPPPIPehlsPGLR 241
                        250       260
                 ....*....|....*....|....
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd06630  242 DVTLRCLELQPEDRPPARELLKHP 265
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
77-324 3.05e-27

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: 108.15  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALK-VLFKSQiekEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRR-----I 150
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKkILCHSK---EDVK-EAMREIENYRLFNHPNILRLLDSQIVKEAggkkeV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQ----KSCTFDEQRTATIMEELADALMYCH---GKKVIHRDIKPENLLLGLKGELKIADFGWSV 223
Cdd:cd13986   78 YLLLPYYKRGSLQDEIErrlvKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDEPILMDLGSMN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSL---RRKTMC--------GTLDYLPPEMIEGRMH---NEKVDLWCIGVLCYELLVGNPPFESASHNETYRR--IVK 287
Cdd:cd13986  158 PARIEiegRREALAlqdwaaehCTMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPFERIFQKGDSLAlaVLS 237
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 927602445 288 VDLKFP--ASVPMGAQDLISKLLRHNPSERLPLAQVSAH 324
Cdd:cd13986  238 GNYSFPdnSRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
75-317 3.08e-27

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 108.30  E-value: 3.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQieKEGVEHQLRREIEIQAHLHHPNILRLYN-YFYDRRRIYLI 153
Cdd:cd06620    5 QDLETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDA--KSSVRKQILRELQILHECHSPYIVSFYGaFLNENNNIIIC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT 232
Cdd:cd06620   83 MEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSIADT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesASHNetyrrivkvDLKFPASVPMGAQDLISKLLrHNP 312
Cdd:cd06620  163 FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF--AGSN---------DDDDGYNGPMGILDLLQRIV-NEP 230

                 ....*
gi 927602445 313 SERLP 317
Cdd:cd06620  231 PPRLP 235
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
75-308 3.11e-27

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 110.48  E-value: 3.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05624   72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP---SLRR 230
Cdd:cd05624  152 DYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLKMNddgTVQS 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGR-----MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVD--LKFPA---SVPMGA 300
Cdd:cd05624  232 SVAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMNHEerFQFPShvtDVSEEA 311

                 ....*...
gi 927602445 301 QDLISKLL 308
Cdd:cd05624  312 KDLIQRLI 319
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
83-337 5.07e-27

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: 107.61  E-value: 5.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCT--FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR-KTMCGTLDY 239
Cdd:cd05577   81 KYHIYNVGTrgFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKiKGRVGTHGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSE 314
Cdd:cd05577  161 MAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFrqrkEKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPER 240
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 315 RLPLAQVSA-----HPWVRA-NSRRV----LPP 337
Cdd:cd05577  241 RLGCRGGSAdevkeHPFFRSlNWQRLeagmLEP 273
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
81-320 5.80e-27

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 106.74  E-value: 5.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALK-VLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd08221    6 RVLGRGAFGEAVLYRKTEDNSLVVWKeVNLSRLSEKE--RRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKEL--QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCG 235
Cdd:cd08221   84 GNLHDKIaqQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISkvLDSESSMAESIVG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASV-PMGAQDLISKLLRHNPSE 314
Cdd:cd08221  164 TPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDIDEQySEEIIQLVHDCLHQDPED 243

                 ....*.
gi 927602445 315 RlPLAQ 320
Cdd:cd08221  244 R-PTAE 248
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
75-325 9.78e-27

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 107.00  E-value: 9.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVlFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKK-FKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRG--ELYKELQKSCTFDEQRTatIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLR 229
Cdd:cd07848   80 EYVEKNmlELLEEMPNGVPPEKVRS--YIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFArnlSEGSNAN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-------------------DL 290
Cdd:cd07848  158 YTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVlgplpaeqmklfysnprfhGL 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 927602445 291 KFPA-SVPMGAQ------------DLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd07848  238 RFPAvNHPQSLErrylgilsgvllDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
75-327 1.54e-26

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 106.64  E-value: 1.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvehqlrREIEI-QAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd14177    4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPS-------EEIEIlMRYGQHPNIITLKDVYDDGRYVYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL----LLGLKGELKIADFGWsvhAPSLR 229
Cdd:cd14177   77 TELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNIlymdDSANADSIRICDFGF---AKQLR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RK-----TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-DLKFPAS------VP 297
Cdd:cd14177  154 GEnglllTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIgSGKFSLSggnwdtVS 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 927602445 298 MGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14177  234 DAAKDLLSHMLHVDPHQRYTAEQVLKHSWI 263
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
60-344 1.65e-26

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 107.60  E-value: 1.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  60 NSSGTPDILTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQieKEGVEHQLRREIEIQAHLHHPNILR 139
Cdd:PLN00034  59 SSSASGSAPSAAKSLSELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNH--EDTVRRQICREIEILRDVNHPNVVK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 140 LYNYFYDRRRIYLILEYAPRGELykelQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADF 219
Cdd:PLN00034 137 CHDMFDHNGEIQVLLEFMDGGSL----EGTHIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADF 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 220 GWSvhapSLRRKTM--C----GTLDYLPPEMI-----EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV 288
Cdd:PLN00034 213 GVS----RILAQTMdpCnssvGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAI 288
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 289 DLKFPASVPMGA----QDLISKLLRHNPSERLPLAQVSAHPWV-RANSRRVLPPSALQSVA 344
Cdd:PLN00034 289 CMSQPPEAPATAsrefRHFISCCLQREPAKRWSAMQLLQHPFIlRAQPGQGQGGPNLHQLL 349
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
83-337 1.92e-26

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 106.61  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKMM---DLRKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGAL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 yKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW----SVHAPslRRKTMCGTLD 238
Cdd:cd06659  106 -TDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFcaqiSKDVP--KRKSLVGTPY 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV---DLKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd06659  183 WMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKASPVLRDFLERMLVRDPQER 262
                        250       260
                 ....*....|....*....|...
gi 927602445 316 LPLAQVSAHPW-VRANSRRVLPP 337
Cdd:cd06659  263 ATAQELLDHPFlLQTGLPECLVP 285
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
75-342 2.18e-26

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 106.27  E-value: 2.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEI-GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiekegvehQLRREIEIQAHL----HHPNILRLYNYFYDRRR 149
Cdd:cd14170    1 DDYKVtSQVLGLGINGKVLQIFNKRTQEKFALKMLQDCP--------KARREVELHWRAsqcpHIVRIVDVYENLYAGRK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLI-LEYAPRGELYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKI---ADFGWSV 223
Cdd:cd14170   73 CLLIvMECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIlklTDFGFAK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRR-KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFES----ASHNETYRRIVKVDLKFP----A 294
Cdd:cd14170  153 ETTSHNSlTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSnhglAISPGMKTRIRMGQYEFPnpewS 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 927602445 295 SVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVraNSRRVLPPSALQS 342
Cdd:cd14170  233 EVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWI--MQSTKVPQTPLHT 278
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
83-315 2.45e-26

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: 105.21  E-value: 2.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKshFIVALKVLFKSQIEKEgvehqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14058    1 VGRGSFGVVCKARWRN--QIVAVKIIESESEKKA-----FEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIME---ELADALMYCHG---KKVIHRDIKPENL-LLGLKGELKIADFGwSVHAPSLRRKTMCG 235
Cdd:cd14058   74 YNVLHGKEPKPIYTAAHAMSwalQCAKGVAYLHSmkpKALIHRDLKPPNLlLTNGGTVLKICDFG-TACDISTHMTNNKG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL--------VGNPPFES--ASHNETYRRIVKVdlkfpasVPMGAQDLIS 305
Cdd:cd14058  153 SAAWMAPEVFEGSKYSEKCDVFSWGIILWEVItrrkpfdhIGGPAFRImwAVHNGERPPLIKN-------CPKPIESLMT 225
                        250
                 ....*....|
gi 927602445 306 KLLRHNPSER 315
Cdd:cd14058  226 RCWSKDPEKR 235
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
80-327 3.81e-26

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


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 105.16  E-value: 3.81e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKvlfksQIE------------KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDR 147
Cdd:cd06629    6 GELIGKGTYGRVYLAMNATTGEMLAVK-----QVElpktssdradsrQKTVVDALKSEIDTLKDLDHPNIVQYLGFEETE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP- 226
Cdd:cd06629   81 DYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDd 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 ---SLRRKTMCGTLDYLPPEMIE--GRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKVDLK-----FPASV 296
Cdd:cd06629  161 iygNNGATSMQGSVFWMAPEVIHsqGQGYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFKLGNKrsappVPEDV 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 297 PM--GAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06629  238 NLspEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
74-328 4.42e-26

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 105.29  E-value: 4.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:PLN00009   1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQ-EDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRgELYKELQKSCTF--DEQRTATIMEELADALMYCHGKKVIHRDIKPENLLL-GLKGELKIADFGWSvHAPSLRR 230
Cdd:PLN00009  80 FEYLDL-DLKKHMDSSPDFakNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIdRRTNALKLADFGLA-RAFGIPV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCG---TLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----------------DL 290
Cdd:PLN00009 158 RTFTHevvTLWYRAPEILLGsRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRIlgtpneetwpgvtslpDY 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 927602445 291 K--FP--------ASVPM---GAQDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:PLN00009 238 KsaFPkwppkdlaTVVPTlepAGVDLLSKMLRLDPSKRITARAALEHEYFK 288
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
83-287 4.57e-26

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 105.20  E-value: 4.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd07846    9 VGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKM-VKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 yKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLDY 239
Cdd:cd07846   88 -DDLEKYPNgLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFArtLAAPGEVYTDYVATRWY 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 927602445 240 LPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVK 287
Cdd:cd07846  167 RAPELLVGDTkYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIK 215
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
81-334 4.96e-26

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: 105.11  E-value: 4.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd05630    6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKEL--QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR-KTMCGTL 237
Cdd:cd05630   86 DLKFHIyhMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTiKGRVGTV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN---ETYRRIVK-VDLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd05630  166 GYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKikrEEVERLVKeVPEEYSEKFSPQARSLCSMLLCKDPA 245
                        250       260
                 ....*....|....*....|....*..
gi 927602445 314 ERL-----PLAQVSAHPWVRA-NSRRV 334
Cdd:cd05630  246 ERLgcrggGAREVKEHPLFKKlNFKRL 272
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
81-274 6.16e-26

Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 porphyrin-binding domain [Signal transduction mechanisms];


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 107.78  E-value: 6.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLARE--KKSHFIVALKVLF-----KSQIEKegVEHQLRRE-IEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:COG5752   38 KPLGQGGFGRTFLAVDedIPSHPHCVIKQFYfpeqgPSSFQK--AVELFRQEaVRLDELGKHPQIPELLAYFEQDQRLYL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKI-ADFGWSVHAPS---L 228
Cdd:COG5752  116 VQEFIEGQTLAQELEKKGVFSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANIIRRRSDGKLVlIDFGVAKLLTItalL 195
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGrmhneKV----DLWCIGVLCYELLVGNPPFE 274
Cdd:COG5752  196 QTGTIIGTPEYMAPEQLRG-----KVfpasDLYSLGVTCIYLLTGVSPFD 240
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
74-327 6.26e-26

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 104.66  E-value: 6.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQ-----------------------IEKEGVEHQLRREIEIQA 130
Cdd:cd14199    1 LNQYKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmrqagfprrppprgaraapegcTQPRGPIERVYQEIAILK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 131 HLHHPNILRLYNYFYD--RRRIYLILEYAPRGELYkELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLL 208
Cdd:cd14199   81 KLDHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 209 GLKGELKIADFGWSVH---APSLRRKTMcGTLDYLPPEMI-EGR--MHNEKVDLWCIGVLCYELLVGNPPFESASHNETY 282
Cdd:cd14199  160 GEDGHIKIADFGVSNEfegSDALLTNTV-GTPAFMAPETLsETRkiFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLH 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 927602445 283 RRIVKVDLKFP--ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14199  239 SKIKTQPLEFPdqPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
78-333 6.32e-26

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 104.81  E-value: 6.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRpLGKGKFGNVYLAREKKSHFIVALKVLFKSQieKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRR--RIYLILE 155
Cdd:cd06621    5 ELSS-LGEGAGGSVTKCRLRNTKTIFALKTITTDP--NPDVQKQILRELEINKSCASPYIVKYYGAFLDEQdsSIGIAME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGEL---YKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK 231
Cdd:cd06621   82 YCEGGSLdsiYKKVKKkGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNSLAG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESashnETYRRIVKVDLK---FPASVPM---------- 298
Cdd:cd06621  162 TFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFPP----EGEPPLGPIELLsyiVNMPNPElkdepengik 237
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 927602445 299 ---GAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRR 333
Cdd:cd06621  238 wseSFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKK 275
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
83-326 6.61e-26

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 104.87  E-value: 6.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQieKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYaprgeL 162
Cdd:cd07836    8 LGEGTYATVYKGRNRTTGEIVALKEIHLDA--EEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEY-----M 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQK-------SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTM 233
Cdd:cd07836   81 DKDLKKymdthgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLarAFGIPVNTFSNE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV------------------------ 288
Cdd:cd07836  161 VVTLWYRAPDVLLGsRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRImgtptestwpgisqlpeykptfpr 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 927602445 289 ----DLK--FPASVPMGAqDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07836  241 yppqDLQqlFPHADPLGI-DLLHRLLQLNPELRISAHDALQHPW 283
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
83-273 8.65e-26

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 104.45  E-value: 8.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVEHQLRR---EIEIQAHLHHPNILRL------YNYFYDRRRIYLI 153
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIK---KCRQELSPSDKNRERwclEVQIMKKLNHPNVVSArdvppeLEKLSPNDLPLLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQK---SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKI---ADFGWsvhAPS 227
Cdd:cd13989   78 MEYCSGGDLRKVLNQpenCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRVIyklIDLGY---AKE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMC----GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd13989  155 LDQGSLCtsfvGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
73-328 9.48e-26

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 104.76  E-value: 9.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRR--RI 150
Cdd:cd07845    5 SVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDN-ERDGIPISSLREITLLLNLRHPNIVELKEVVVGKHldSI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRgELYKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG----WSVHA 225
Cdd:cd07845   84 FLVMEYCEQ-DLASLLDNmPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGlartYGLPA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMcgTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-------------DL- 290
Cdd:cd07845  163 KPMTPKVV--TLWYRAPELLLGcTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLlgtpnesiwpgfsDLp 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 291 -----------------KFPASVPMGAqDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd07845  241 lvgkftlpkqpynnlkhKFPWLSEAGL-RLLNFLLMYDPKKRATAEEALESSYFK 294
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
75-308 9.64e-26

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 106.64  E-value: 9.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05623   72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVM 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV---HAPSLRR 230
Cdd:cd05623  152 DYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSCLklmEDGTVQS 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIE------GRmHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFP---ASVPMG 299
Cdd:cd05623  232 SVAVGTPDYISPEILQamedgkGK-YGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKERFQFPtqvTDVSEN 310

                 ....*....
gi 927602445 300 AQDLISKLL 308
Cdd:cd05623  311 AKDLIRRLI 319
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
83-333 1.07e-25

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 104.00  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06641   12 IGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDE-IE-DIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKScTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLDYL 240
Cdd:cd06641   90 LDLLEPG-PLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAgqLTDTQIKRN*FVGTPFWM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPfesasHNETYRriVKVDLKFPASVP--------MGAQDLISKLLRHNP 312
Cdd:cd06641  169 APEVIKQSAYDSKADIWSLGITAIELARGEPP-----HSELHP--MKVLFLIPKNNPptlegnysKPLKEFVEACLNKEP 241
                        250       260
                 ....*....|....*....|.
gi 927602445 313 SERLPLAQVSAHPWVRANSRR 333
Cdd:cd06641  242 SFRPTAKELLKHKFILRNAKK 262
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
77-334 3.07e-25

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 102.63  E-value: 3.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVlfksqIEKEGVEHQL-RREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKF-----VKVKGADQVLvKKEISILNIARHRNILRLHESFESHEELVMIFE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN--LLLGLKGELKIADFGWSVHA-PSLRRK 231
Cdd:cd14104   77 FISGVDIFERItTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENiiYCTRRGSYIKIIEFGQSRQLkPGDKFR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKL 307
Cdd:cd14104  157 LQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDeafkNISIEALDFVDRL 236
                        250       260
                 ....*....|....*....|....*..
gi 927602445 308 LRHNPSERLPLAQVSAHPWVRANSRRV 334
Cdd:cd14104  237 LVKERKSRMTAQEALNHPWLKQGMETV 263
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
83-278 3.16e-25

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


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 102.53  E-value: 3.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERK-ALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 yKELQKSCTFDEQRTAT--IMEELADALMYCHG--KKVIHRDIKPENLLLGLKGELKIADFGWSV-----HAPSLRRKT- 232
Cdd:cd13978   80 -KSLLEREIQDVPWSLRfrIIHEIALGMNFLHNmdPPLLHHDLKPENILLDNHFHVKISDFGLSKlgmksISANRRRGTe 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 927602445 233 -MCGTLDYLPPEMIE--GRMHNEKVDLWCIGVLCYELLVGNPPFESASH 278
Cdd:cd13978  159 nLGGTPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLTRKEPFENAIN 207
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
77-328 3.23e-25

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 102.23  E-value: 3.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEG-------VEHQLRREIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSklpgvnpVPNEVALLQSVGGGPGHRGVIRLLDWFEIPEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYA-PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG-ELKIADFGwsvhAPS 227
Cdd:cd14101   82 FLLVLERPqHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTgDIKLIDFG----SGA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMC----GTLDYLPPEMIE-GRMHNEKVDLWCIGVLCYELLVGNPPFESASHnetyrrIVKVDLKFPASVPMGAQD 302
Cdd:cd14101  158 TLKDSMYtdfdGTRVYSPPEWILyHQYHALPATVWSLGILLYDMVCGDIPFERDTD------ILKAKPSFNKRVSNDCRS 231
                        250       260
                 ....*....|....*....|....*.
gi 927602445 303 LISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd14101  232 LIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
81-337 4.68e-25

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 103.27  E-value: 4.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQI-EKEGVEH-QLRREIEIQAHlHHPNILRLYNYFYDRRRIYLILEYAP 158
Cdd:cd05588    1 RVIGRGSYAKVLMVELKKTKRIYAMKVIKKELVnDDEDIDWvQTEKHVFETAS-NHPFLVGLHSCFQTESRLFFVIEFVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA--PSLRRKTMCGT 236
Cdd:cd05588   80 GGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGlrPGDTTSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET---------YRRIVKVDLKFPASVPMGAQDLISKL 307
Cdd:cd05588  160 PNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDIVGSSDNpdqntedylFQVILEKPIRIPRSLSVKAASVLKGF 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 927602445 308 LRHNPSERL------PLAQVSAHP------WVRANSRRVLPP 337
Cdd:cd05588  240 LNKNPAERLgchpqtGFADIQSHPffrtidWEQLEQKQVTPP 281
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
81-329 5.53e-25

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 103.94  E-value: 5.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd05626    7 KTLGIGAFGEVCLACKVDTHALYAMKTLRKKDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------WSVHAP------SL 228
Cdd:cd05626   87 DMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGlctgfrWTHNSKyyqkgsHI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTM-------------------------------------CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNP 271
Cdd:cd05626  167 RQDSMepsdlwddvsncrcgdrlktleqratkqhqrclahslVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQP 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 272 PFESASHNETYRRIVKVD--LKFPASVPMG--AQDLISKLLrHNPSERL---PLAQVSAHPWVRA 329
Cdd:cd05626  247 PFLAPTPTETQLKVINWEntLHIPPQVKLSpeAVDLITKLC-CSAEERLgrnGADDIKAHPFFSE 310
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
83-335 5.56e-25

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 102.39  E-value: 5.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfksQIE-KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYaprge 161
Cdd:cd07873   10 LGEGTYATVYKGRSKLTDNLVALKEI---RLEhEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEY----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQK---SC--TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRRKTMCG- 235
Cdd:cd07873   82 LDKDLKQyldDCgnSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-RAKSIPTKTYSNe 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 --TLDYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-------------------DLKFP 293
Cdd:cd07873  161 vvTLWYRPPDILLGSTdYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRIlgtpteetwpgilsneefkSYNYP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 927602445 294 ASVPMGAQ-----------DLISKLLRHNPSERLPLAQVSAHPWVRANSRRVL 335
Cdd:cd07873  241 KYRADALHnhaprldsdgaDLLSKLLQFEGRKRISAEEAMKHPYFHSLGERIH 293
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
73-325 5.75e-25

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 102.62  E-value: 5.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKegvehqLRREIEIQAHLH-HPNILRLYNYFYD--RRR 149
Cdd:cd14132   16 SQDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKK------IKREIKILQNLRgGPNIVKLLDVVKDpqSKT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPrGELYKELQKSCTFDEQRtaTIMEELADALMYCHGKKVIHRDIKPEN-LLLGLKGELKIADFG-------- 220
Cdd:cd14132   90 PSLIFEYVN-NTDFKTLYPTLTDYDIR--YYMYELLKALDYCHSKGIMHRDVKPHNiMIDHEKRKLRLIDWGlaefyhpg 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 --WSVHAPSLRRKtmcgtldylPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN-ETYRRIVKV-------- 288
Cdd:cd14132  167 qeYNVRVASRYYK---------GPElLVDYQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDNyDQLVKIAKVlgtddlya 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927602445 289 -----DLKFPAS----------------VPMGAQ--------DLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd14132  238 yldkyGIELPPRlndilgrhskkpwerfVNSENQhlvtpealDLLDKLLRYDHQERITAKEAMQHP 303
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
74-315 6.08e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 105.97  E-value: 6.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDR--RRI 150
Cdd:PTZ00266   12 LNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAIsYRGLKERE--KSQLVIEVNVMRELKHKNIVRYIDRFLNKanQKL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  151 YLILEYAPRGELYKELQKsC-----TFDEQRTATIMEELADALMYCH-------GKKVIHRDIKPENLLLGL-------- 210
Cdd:PTZ00266   90 YILMEFCDAGDLSRNIQK-CykmfgKIEEHAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLSTgirhigki 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  211 ---------KGELKIADFGWSVHAPSLRRKTMC-GTLDYLPPEMI--EGRMHNEKVDLWCIGVLCYELLVGNPPFESASH 278
Cdd:PTZ00266  169 taqannlngRPIAKIGDFGLSKNIGIESMAHSCvGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANN 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 927602445  279 netYRRIVKvDLKFPASVPMGAQD-----LISKLLRHNPSER 315
Cdd:PTZ00266  249 ---FSQLIS-ELKRGPDLPIKGKSkelniLIKNLLNLSAKER 286
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
76-324 8.10e-25

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: 101.49  E-value: 8.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKegVEHQLRREIEIQAHLHHPNILRlynYFY---------- 145
Cdd:cd14048    7 DFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNEL--AREKVLREVRALAKLDHPGIVR---YFNawlerppegw 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 ----DRRRIYLILEYAPRGELYKELQKSCTFDEQRTAT---IMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIAD 218
Cdd:cd14048   82 qekmDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFVclnIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 219 FGWSVHA-------------PSLRRKT-MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVgnpPFESAShnETYRR 284
Cdd:cd14048  162 FGLVTAMdqgepeqtvltpmPAYAKHTgQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELIY---SFSTQM--ERIRT 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 927602445 285 IVKV-DLKFPA----SVPMgAQDLISKLLRHNPSERLPLAQVSAH 324
Cdd:cd14048  237 LTDVrKLKFPAlftnKYPE-ERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
77-329 8.53e-25

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 102.64  E-value: 8.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFK-------SQiekegvehqlR--REIE-IQAHLHHPNILRLYNYFY- 145
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDafrnatdAQ----------RtfREIMfLQELNDHPNIIKLLNVIRa 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 -DRRRIYLILEYAP-------RGELYKELQKSctfdeqrtaTIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA 217
Cdd:cd07852   79 eNDKDIYLVFEYMEtdlhaviRANILEDIHKQ---------YIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 218 DFGWSVHAPSLRRKTMCGTL-DYL------PPEMIEGRMHNEK-VDLWCIGVLCYELLVGNPPFESAS------------ 277
Cdd:cd07852  150 DFGLARSLSQLEEDDENPVLtDYVatrwyrAPEILLGSTRYTKgVDMWSVGCILGEMLLGKPLFPGTStlnqlekiievi 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927602445 278 --------------------HNETYRRIVKVDLKFPaSVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRA 329
Cdd:cd07852  230 grpsaediesiqspfaatmlESLPPSRPKSLDELFP-KASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ 300
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
123-315 8.99e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 104.33  E-value: 8.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 123 RREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYKE----LQKSCTFDEQRTATIMEELADALMYCHGKKVIH 198
Cdd:PTZ00267 113 RSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQikqrLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMH 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 199 RDIKPENLLLGLKGELKIADFGWSVH---APSLR-RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFE 274
Cdd:PTZ00267 193 RDLKSANIFLMPTGIIKLGDFGFSKQysdSVSLDvASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFK 272
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 927602445 275 SASHNETYRRIV--KVDlKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:PTZ00267 273 GPSQREIMQQVLygKYD-PFPCPVSSGMKALLDPLLSKNPALR 314
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
83-321 1.03e-24

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 100.80  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKVLfksqiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRriYLILEYAPRGEL 162
Cdd:cd14068    2 LGDGGFGSVYRAVYRGED--VAVKIF-----NKHTSFRLLRQELVVLSHLHHPSLVALLAAGTAPR--MLVMELAPKGSL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL-----LLGLKGELKIADFGWSVHAPSLRRKTMCGT 236
Cdd:cd14068   73 DALLQQdNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVllftlYPNCAIIAKIADYGIAQYCCRMGIKTSEGT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 LDYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNppfesashnetyRRIVKvDLKFP---------------------A 294
Cdd:cd14068  153 PGFRAPEVARGNViYNQQADVYSFGLLLYDILTCG------------ERIVE-GLKFPnefdelaiqgklpdpvkeygcA 219
                        250       260
                 ....*....|....*....|....*..
gi 927602445 295 SVPMgAQDLISKLLRHNPSERLPLAQV 321
Cdd:cd14068  220 PWPG-VEALIKDCLKENPQCRPTSAQV 245
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
83-273 1.10e-24

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 101.29  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06642   12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAEDE-IE-DIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YkELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLDYL 240
Cdd:cd06642   90 L-DLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAgqLTDTQIKRNTFVGTPFWM 168
                        170       180       190
                 ....*....|....*....|....*....|...
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd06642  169 APEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
83-328 1.22e-24

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


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 101.72  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06655   27 IGQGASGTVFTAIDVATGQEVAIKQI---NLQKQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTMCGTLDYL 240
Cdd:cd06655  104 TDVVTETC-MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFcaQITPEQSKRSTMVGTPYWM 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesasHNETYRRIVKV-------DLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd06655  183 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY----LNENPLRALYLiatngtpELQNPEKLSPIFRDFLNRCLEMDVE 258
                        250
                 ....*....|....*
gi 927602445 314 ERLPLAQVSAHPWVR 328
Cdd:cd06655  259 KRGSAKELLQHPFLK 273
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
81-329 1.49e-24

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


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 102.82  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd05625    7 KTLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------WSVHA--------- 225
Cdd:cd05625   87 DMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfrWTHDSkyyqsgdhl 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 ------------------------PSLRR----------KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNP 271
Cdd:cd05625  167 rqdsmdfsnewgdpencrcgdrlkPLERRaarqhqrclaHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGQP 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 272 PFESASHNETYRRIVK--VDLKFPASVPMG--AQDLISKLLRhNPSERL---PLAQVSAHPWVRA 329
Cdd:cd05625  247 PFLAQTPLETQMKVINwqTSLHIPPQAKLSpeASDLIIKLCR-GPEDRLgknGADEIKAHPFFKT 310
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
77-327 2.32e-24

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 100.43  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHL---HHPNILRLYN--YFYDRRR-- 149
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV-RVPLSEEGIPLSTIREIALLKQLesfEHPNVVRLLDvcHGPRTDRel 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 -IYLILEYAPRgELYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHA 225
Cdd:cd07838   80 kLTLVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLArIYS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYEL---------------------LVGNP-----PFESASHN 279
Cdd:cd07838  159 FEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELfnrrplfrgsseadqlgkifdVIGLPseeewPRNSALPR 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 280 ETYRRIVKVDLK--FPASVPMGAqDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07838  239 SSFPSYTPRPFKsfVPEIDEEGL-DLLKKMLTFNPHKRISAFEALQHPYF 287
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
76-325 2.95e-24

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 99.98  E-value: 2.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHfIVALKVLFKSQIEKEGVEHQLRrEIEIQAHL-HHPNILRLYNYFYDRRR--IYL 152
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVLNPKKK-IYALKRVDLEGADEQTLQSYKN-EIELLKKLkGSDRIIQLYDYEVTDEDdyLYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYaprGE--LYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIaDFGWS----VH 224
Cdd:cd14131   80 VMEC---GEidLATILKKkrPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRLKLI-DFGIAkaiqND 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTMCGTLDYLPPE-MIEGRMHNE---------KVDLWCIGVLCYELLVGNPPFESASH-NETYRRIV--KVDLK 291
Cdd:cd14131  156 TTSIVRDSQVGTLNYMSPEaIKDTSASGEgkpkskigrPSDVWSLGCILYQMVYGKTPFQHITNpIAKLQAIIdpNHEIE 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 292 FPASVPMGAQDLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd14131  236 FPDIPNPDLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
83-288 2.97e-24

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 100.47  E-value: 2.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfksQIE-KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYApRGE 161
Cdd:cd07871   13 LGEGTYATVFKGRSKLTENLVALKEI---RLEhEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFEYL-DSD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATI-MEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRRKTMCG---TL 237
Cdd:cd07871   89 LKQYLDNCGNLMSMHNVKIfMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLA-RAKSVPTKTYSNevvTL 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 238 DYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV 288
Cdd:cd07871  168 WYRPPDVLLGSTeYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRL 219
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
75-328 4.50e-24

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


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 100.83  E-value: 4.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIekegveHQLR--REIEIQAHLHHPNILRLYNYFY---- 145
Cdd:cd07851   15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLsrpFQSAI------HAKRtyRELRLLKHMKHENVIGLLDVFTpass 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 --DRRRIYLILEYAPRgELYKELqKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV 223
Cdd:cd07851   89 leDFQDVYLVTHLMGA-DLNNIV-KCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLrrktMCG---TLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----------- 288
Cdd:cd07851  167 HTDDE----MTGyvaTRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLvgtpdeellkk 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 289 -------------------DLK--FPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd07851  243 issesarnyiqslpqmpkkDFKevFSGANPL-AIDLLEKMLVLDPDKRITAAEALAHPYLA 302
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
83-326 4.50e-24

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 99.75  E-value: 4.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSqiEKEGVEHQLR-REIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd07847    9 IGEGSYGVVFKCRNRETGQIVAIKKFVES--EDDPVIKKIAlREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDHTV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYkELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLD 238
Cdd:cd07847   87 LN-ELEKNPRgVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAriLTGPGDDYTDYVATRW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNP--PFESA----------------------SHNETYRRI-------- 285
Cdd:cd07847  166 YRAPELLVGDTqYGPPVDVWAIGCVFAELLTGQPlwPGKSDvdqlylirktlgdliprhqqifSTNQFFKGLsipepetr 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 927602445 286 VKVDLKFPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07847  246 EPLESKFPNISSP-ALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
83-273 6.06e-24

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 99.65  E-value: 6.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfksQIEKEGVEHQLRR---EIEIQAHLHHPNILRLYNYFYDRRRI------YLI 153
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIK-----QCRQELSPKNRERwclEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYK---ELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWsvhAPS 227
Cdd:cd14038   77 MEYCQGGDLRKylnQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENivlQQGEQRLIHKIIDLGY---AKE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMC----GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd14038  154 LDQGSLCtsfvGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
76-326 6.87e-24

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


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 99.03  E-value: 6.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKI-RLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRgELYK---ELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRR 230
Cdd:cd07861   80 FLSM-DLKKyldSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLarAFGIPVRVY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----------------DLK-- 291
Cdd:cd07861  159 THEVVTLWYRAPEVLLGsPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRIlgtptediwpgvtslpDYKnt 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 927602445 292 FP--------ASVP---MGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07861  239 FPkwkkgslrTAVKnldEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
75-328 7.29e-24

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 99.43  E-value: 7.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKvLFKSQIeKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARK-LIHLEI-KPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTM 233
Cdd:cd06615   79 EHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVG---------------NPPFESASHNETYRRIVKVD--------- 289
Cdd:cd06615  159 VGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrypipppdakeleamFGRPVSEGEAKESHRPVSGHppdsprpma 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 927602445 290 ----LKF-----PASVPMGA-----QDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd06615  239 ifelLDYivnepPPKLPSGAfsdefQDFVDKCLKKNPKERADLKELTKHPFIK 291
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
77-327 7.97e-24

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 98.49  E-value: 7.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEI----QAHLHHPNILRLYNYfYDRRRIYL 152
Cdd:cd14102    2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMVPLEIvllkKVGSGFRGVIKLLDW-YERPDGFL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPR--GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG-ELKIADFGWSVHAPSLR 229
Cdd:cd14102   81 IVMERPEpvKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTgELKLIDFGSGALLKDTV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIE-GRMHNEKVDLWCIGVLCYELLVGNPPFESAshnetyRRIVKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd14102  161 YTDFDGTRVYSPPEWIRyHRYHGRSATVWSLGVLLYDMVCGDIPFEQD------EEILRGRLYFRRRVSPECQQLIKWCL 234
                        250
                 ....*....|....*....
gi 927602445 309 RHNPSERLPLAQVSAHPWV 327
Cdd:cd14102  235 SLRPSDRPTLEQIFDHPWM 253
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
79-326 8.38e-24

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 99.84  E-value: 8.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKE-----------GVEHQLRREIEIQAHLHHPNILRLYNYFYDR 147
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDvtkdrqlvgmcGIHFTTLRELKIMNEIKHENIMGLVDVYVEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS----- 222
Cdd:PTZ00024  93 DFINLVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLArrygy 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 --VHAPSLRRKTMCG---------TLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-- 288
Cdd:PTZ00024 172 ppYSDTLSKDETMQRreemtskvvTLWYRAPELLMGaEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFELlg 251
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 289 -------------------------DLK--FPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:PTZ00024 252 tpnednwpqakklplyteftprkpkDLKtiFPNASDD-AIDLLQSLLKLNPLERISAKEALKHEY 315
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
76-325 8.39e-24

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 98.22  E-value: 8.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHL-HHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKS-KKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGEL---YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSlRRK 231
Cdd:cd13997   80 ELCENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLET-SGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRiVKVDLKFPASVPMGAQDLISKLLRH 310
Cdd:cd13997  159 VEEGDSRYLAPELLnENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLRQ-GKLPLPPGLVLSQELTRLLKVMLDP 237
                        250
                 ....*....|....*
gi 927602445 311 NPSERLPLAQVSAHP 325
Cdd:cd13997  238 DPTRRPTADQLLAHD 252
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
81-324 8.57e-24

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 98.16  E-value: 8.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLG-----KGKFGNVYLAREKKSHFIVALKVLfksqiekeGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd13995    5 RNIGsdfipRGAFGKVYLAQDTKTKKRMACKLI--------PVEQFKPSDVEIQACFRHENIAELYGALLWEETVHLFME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIaDFGWSVHAPS--LRRKTM 233
Cdd:cd13995   77 AGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEdvYVPKDL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLK-------FPASVPMGAQDLISK 306
Cdd:cd13995  156 RGTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKqappledIAQDCSPAMRELLEA 235
                        250
                 ....*....|....*...
gi 927602445 307 LLRHNPSERLPLAQVSAH 324
Cdd:cd13995  236 ALERNPNHRSSAAELLKH 253
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
77-326 9.31e-24

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: 98.04  E-value: 9.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKegvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIpLRSSTRA-----RAFQERDILARLSHRRLTCLLDQFETRKTLILILE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL--KIADFGWSVHAPSLRRK-T 232
Cdd:cd14107   79 LCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREdiKICDFGFAQEITPSEHQfS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPA----SVPMGAQDLISKLL 308
Cdd:cd14107  159 KYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVSWDTpeitHLSEDAKDFIKRVL 238
                        250
                 ....*....|....*...
gi 927602445 309 RHNPSERLPLAQVSAHPW 326
Cdd:cd14107  239 QPDPEKRPSASECLSHEW 256
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
80-327 9.44e-24

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 98.47  E-value: 9.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiEKEGVEHQLRREIEI-QAHLHHPNILRLYNYFYDRRRIYLILEYAP 158
Cdd:cd14197   14 GRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRR-KGQDCRMEIIHEIAVlELAQANPWVINLHEVYETASEMILVLEYAA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKEL--QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL---KIADFGWS-VHAPSLRRKT 232
Cdd:cd14197   93 GGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgdiKIVDFGLSrILKNSEELRE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPAS----VPMGAQDLISKLL 308
Cdd:cd14197  173 IMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSEEefehLSESAIDFIKTLL 252
                        250
                 ....*....|....*....
gi 927602445 309 RHNPSERLPLAQVSAHPWV 327
Cdd:cd14197  253 IKKPENRATAEDCLKHPWL 271
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
83-273 9.77e-24

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 98.84  E-value: 9.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKV--LFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNY-----FYDRRRIYLILE 155
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKScrLELSVKNKD----RWCHEIQIMKKLNHPNVVKACDVpeemnFLVNDVPLLAME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKS---CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGL---KGELKIADFGWsvhAPSLR 229
Cdd:cd14039   77 YCSGGDLRKLLNKPencCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEingKIVHKIIDLGY---AKDLD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 927602445 230 RKTMC----GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd14039  154 QGSLCtsfvGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
77-327 9.78e-24

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 98.87  E-value: 9.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKE-----------------------GVEHQLRREIEIQAHLH 133
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplAPLERVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 134 HPNILRLYNYFYD--RRRIYLILEYAPRGELYkELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLK 211
Cdd:cd14200   82 HVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 212 GELKIADFGWS--VHAPSLRRKTMCGTLDYLPPEMIE--GRMHNEK-VDLWCIGVLCYELLVGNPPFESASHNETYRRIV 286
Cdd:cd14200  161 GHVKIADFGVSnqFEGNDALLSSTAGTPAFMAPETLSdsGQSFSGKaLDVWAMGVTLYCFVYGKCPFIDEFILALHNKIK 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 287 KVDLKFP--ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14200  241 NKPVEFPeePEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
81-334 1.18e-23

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 98.53  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd05631    6 RVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR-KTMCGTL 237
Cdd:cd05631   86 DLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETvRGRVGTV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd05631  166 GYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFrkrkERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNPK 245
                        250       260
                 ....*....|....*....|....*..
gi 927602445 314 ERLPL-----AQVSAHPWVRA-NSRRV 334
Cdd:cd05631  246 ERLGCrgngaAGVKQHPIFKNiNFKRL 272
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
83-328 2.55e-23

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 97.87  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06656   27 IGQGASGTVYTAIDIATGQEVAIKQM---NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTMCGTLDYL 240
Cdd:cd06656  104 TDVVTETC-MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcaQITPEQSKRSTMVGTPYWM 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesasHNETYRRIVKV-------DLKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd06656  183 APEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY----LNENPLRALYLiatngtpELQNPERLSAVFRDFLNRCLEMDVD 258
                        250
                 ....*....|....*
gi 927602445 314 ERLPLAQVSAHPWVR 328
Cdd:cd06656  259 RRGSAKELLQHPFLK 273
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
77-326 2.67e-23

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 98.37  E-value: 2.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIekegveHQLR--REIEIQAHLHHPNILRLYNYFYDRRR-- 149
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIsnvFDDLI------DAKRilREIKILRHLKHENIIGLLDILRPPSPee 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 ---IYLILEYAPrGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsvhap 226
Cdd:cd07834   76 fndVYIVTELME-TDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFG------ 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 sLRRKTMCGTLD-----------YLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASH---------------- 278
Cdd:cd07834  149 -LARGVDPDEDKgflteyvvtrwYRAPELLLSSKKyTKAIDIWSVGCIFAELLTRKPLFPGRDYidqlnlivevlgtpse 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 279 -------NETYRRIV-------KVDL--KFPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07834  228 edlkfisSEKARNYLkslpkkpKKPLseVFPGASPE-AIDLLEKMLVFNPKKRITADEALAHPY 290
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
76-337 3.07e-23

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: 97.64  E-value: 3.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFeigRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEK-EGVEHQLRrEIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05608    5 DF---RVLGKGGFGEVSACQMRATGKLYACKKLNKKRLKKrKGYEGAMV-EKRILAKVHSRFIVSLAYAFQTKTDLCLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGEL----YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR 230
Cdd:cd05608   81 TIMNGGDLryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KT--MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQDLI 304
Cdd:cd05608  161 KTkgYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFrargEKVENKELKQRILNDSVTYSEKFSPASKSIC 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 305 SKLLRHNPSERLPL-----AQVSAHPWVRANSRR-----VLPP 337
Cdd:cd05608  241 EALLAKDPEKRLGFrdgncDGLRTHPFFRDINWRkleagILPP 283
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
83-326 4.55e-23

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 97.44  E-value: 4.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALK-VLFKSqiEKEGVEHQLRREIEIQAHLHHPNILRLYN--------YFYDRRRIYLI 153
Cdd:cd07865   20 IGQGTFGEVFKARHRKTGQIVALKkVLMEN--EKEGFPITALREIKILQLLKHENVVNLIEicrtkatpYNRYKGSIYLV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRgELYKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRRKT 232
Cdd:cd07865   98 FEFCEH-DLAGLLSnKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLA-RAFSLAKNS 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCG-------TLDYLPPEMIEG-RMHNEKVDLWCIGVLCYEL------LVGN---------------------------P 271
Cdd:cd07865  176 QPNrytnrvvTLWYRPPELLLGeRDYGPPIDMWGAGCIMAEMwtrspiMQGNteqhqltlisqlcgsitpevwpgvdklE 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 272 PFESASHNETYRRIVKVDLKFPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07865  256 LFKKMELPQGQKRKVKERLKPYVKDPY-ALDLIDKLLVLDPAKRIDADTALNHDF 309
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
75-319 4.71e-23

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 97.43  E-value: 4.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksQIE-KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLI---HLEiKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT 232
Cdd:cd06650   82 MEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNP 312
Cdd:cd06650  162 FVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGM 241

                 ....*..
gi 927602445 313 SERLPLA 319
Cdd:cd06650  242 DSRPPMA 248
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
83-340 4.83e-23

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


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 97.03  E-value: 4.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVK---KMDLRKQQRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGAL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 yKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTMCGTLDYL 240
Cdd:cd06658  107 -TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFcaQVSKEVPKRKSLVGTPYWM 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRI-------VKvDLKFPASVPMGAQDLiskLLRHNPS 313
Cdd:cd06658  186 APEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIrdnlpprVK-DSHKVSSVLRGFLDL---MLVREPS 261
                        250       260
                 ....*....|....*....|....*..
gi 927602445 314 ERLPLAQVSAHPWVRANSrrvlPPSAL 340
Cdd:cd06658  262 QRATAQELLQHPFLKLAG----PPSCI 284
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
76-327 5.64e-23

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 96.25  E-value: 5.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALK-VLFKSQIEKEGVE-HQLRREIEIQAHLHHPNILRLYNYFYD--RRRIY 151
Cdd:cd06653    3 NWRLGKLLGRGAFGEVYLCYDADTGRELAVKqVPFDPDSQETSKEvNALECEIQLLKNLRHDRIVQYYGCLRDpeEKKLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR- 230
Cdd:cd06653   83 IFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTICMs 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 ----KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKVDLKfPAS--VPMGAQDLI 304
Cdd:cd06653  163 gtgiKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW---AEYEAMAAIFKIATQ-PTKpqLPDGVSDAC 238
                        250       260
                 ....*....|....*....|....*.
gi 927602445 305 SKLLRH--NPSERLPLAQ-VSAHPWV 327
Cdd:cd06653  239 RDFLRQifVEEKRRPTAEfLLRHPFV 264
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
83-273 1.31e-22

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


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 95.95  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVL-FKSQIEKEGVEHqlrrEIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd06654   28 IGQGASGTVYTAMDVATGQEVAIRQMnLQQQPKKELIIN----EILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTMCGTLDY 239
Cdd:cd06654  104 LTDVVTETC-MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcaQITPEQSKRSTMVGTPYW 182
                        170       180       190
                 ....*....|....*....|....*....|....
gi 927602445 240 LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd06654  183 MAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
68-274 1.40e-22

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 95.64  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  68 LTRHFTIDDF-EIGRPLGKGKFGNVYLAREKKSHfiVALKVLFK-SQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFY 145
Cdd:cd14158    7 MTNNFDERPIsVGGNKLGEGGFGVVFKGYINDKN--VAVKKLAAmVDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGELYKELqkSCTFDE-----QRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG 220
Cdd:cd14158   85 DGPQLCLVYTYMPNGSLLDRL--ACLNDTpplswHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 221 WSVHAP----SLRRKTMCGTLDYLPPEMIEGRMhNEKVDLWCIGVLCYELLVGNPPFE 274
Cdd:cd14158  163 LARASEkfsqTIMTERIVGTTAYMAPEALRGEI-TPKSDIFSFGVVLLEIITGLPPVD 219
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
75-332 1.64e-22

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 95.30  E-value: 1.64e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfksQIEKEGVEHQLR---REIEIQAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMK-----EIRLELDESKFNqiiMELDILHKAVSPYIVDFYGAFFIEGAVY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRG---ELYKELQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPS 227
Cdd:cd06622   76 MCMEYMDAGsldKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIEGRMHNE------KVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMG-- 299
Cdd:cd06622  156 SLAKTNIGCQSYMAPERIKSGGPNQnptytvQSDVWSLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTLPSGys 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 300 --AQDLISKLLRHNPSERLPLAQVSAHPWVRANSR 332
Cdd:cd06622  236 ddAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKN 270
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
84-321 2.01e-22

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 94.25  E-value: 2.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  84 GKGKFGNVYLAREKKSHFIVALKVLFKsqIEKEGvehqlrreiEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELY 163
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLLK--IEKEA---------EILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 164 KEL--QKSCTFDEQRTATIMEELADALMYCHGK---KVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLD 238
Cdd:cd14060   71 DYLnsNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLVGTFP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVD--LKFPASVPMGAQDLISKLLRHNPSERL 316
Cdd:cd14060  151 WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNerPTIPSSCPRSFAELMRRCWEADVKERP 230

                 ....*
gi 927602445 317 PLAQV 321
Cdd:cd14060  231 SFKQI 235
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
73-326 2.34e-22

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: 94.98  E-value: 2.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFY--DRRRI 150
Cdd:cd07843    3 SVDEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKL-KMEKEKEGFPITSLREINILLKLQHPNIVTVKEVVVgsNLDKI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRgELyKEL--QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG----WSVH 224
Cdd:cd07843   82 YMVMEYVEH-DL-KSLmeTMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGlareYGSP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTMcgTLDYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-------------DL 290
Cdd:cd07843  160 LKPYTQLVV--TLWYRAPELLLGaKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLlgtptekiwpgfsEL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 291 ------------------KFPASVPMGAQ-DLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07843  238 pgakkktftkypynqlrkKFPALSLSDNGfDLLNRLLTYDPAKRISAEDALKHPY 292
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
75-327 2.76e-22

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 94.12  E-value: 2.76e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIG-RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIekegvehqLRREIEIQAHLHHPNILRLYN-YFYDRRRIYL 152
Cdd:cd14109    3 ELYEIGeEDEKRAAQGAPFHVTERSTGRNFLAQLRYGDPF--------LMREVDIHNSLDHPNIVQMHDaYDDEKLAVTV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQKSCT--FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELkIADFGWSvhapslRR 230
Cdd:cd14109   75 IDNLASTIELVRDNLLPGKdyYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDKLK-LADFGQS------RR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 --KTMCGTLDY-----LPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASV----PMG 299
Cdd:cd14109  148 llRGKLTTLIYgspefVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWSFDSSPlgniSDD 227
                        250       260
                 ....*....|....*....|....*...
gi 927602445 300 AQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14109  228 ARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
76-308 2.77e-22

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 94.34  E-value: 2.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVE-----HQLRREIEIQAHLHHPNILRLYNYFYD--RR 148
Cdd:cd06652    3 NWRLGKLLGQGAFGRVYLCYDADTGRELAVK---QVQFDPESPEtskevNALECEIQLLKNLLHERIVQYYGCLRDpqER 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 RIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsvhaPSL 228
Cdd:cd06652   80 TLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFG-----ASK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMC----------GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKV-----DLKFP 293
Cdd:cd06652  155 RLQTIClsgtgmksvtGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPW---AEFEAMAAIFKIatqptNPQLP 231
                        250
                 ....*....|....*
gi 927602445 294 ASVPMGAQDLISKLL 308
Cdd:cd06652  232 AHVSDHCRDFLKRIF 246
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
74-279 3.54e-22

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 94.32  E-value: 3.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd08228    1 LANFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGEL---YKELQKSCTFDEQRTA-TIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPS 227
Cdd:cd08228   81 LELADAGDLsqmIKYFKKQKRLIPERTVwKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGrfFSSKT 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 228 LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN 279
Cdd:cd08228  161 TAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMN 212
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
76-327 4.85e-22

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 93.66  E-value: 4.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREK---KSHFIVALKVLFKSQIEKEGVEhqlrREIEIQAHLHHPNILRLYNYFYDRR-RIY 151
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKrdrKQYVIKKLNLKNASKRERKAAE----QEAKLLSKLKHPNIVSYKESFEGEDgFLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKEL--QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPS 227
Cdd:cd08223   77 IVMGFCEGGDLYTRLkeQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIArvLESSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVdlKFPasvPMGAQ------ 301
Cdd:cd08223  157 DMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEG--KLP---PMPKQyspelg 231
                        250       260
                 ....*....|....*....|....*.
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd08223  232 ELIKAMLHQDPEKRPSVKRILRQPYI 257
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
83-322 5.71e-22

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 93.57  E-value: 5.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHL-HHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd05047    3 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKS----------------CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA 225
Cdd:cd05047   83 LLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMcGTLD--YLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK-VDLKFPASVPMGAQ 301
Cdd:cd05047  163 EVYVKKTM-GRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYEKLPQgYRLEKPLNCDDEVY 241
                        250       260
                 ....*....|....*....|.
gi 927602445 302 DLISKLLRHNPSERLPLAQVS 322
Cdd:cd05047  242 DLMRQCWREKPYERPSFAQIL 262
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
75-273 6.65e-22

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 93.92  E-value: 6.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqiekeGVEHQLRREIE-----IQAHLHHPNILRLYNYFYDRR- 148
Cdd:cd06638   18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKIL--------DPIHDIDEEIEaeyniLKALSDHPNVVKFYGMYYKKDv 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 ----RIYLILEYAPRG---ELYKE-LQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG 220
Cdd:cd06638   90 kngdQLWLVLELCNGGsvtDLVKGfLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFG 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 WSVHAPS--LRRKTMCGTLDYLPPEMI--EGRM---HNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd06638  170 VSAQLTStrLRRNTSVGTPFWMAPEVIacEQQLdstYDARCDVWSLGITAIELGDGDPPL 229
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
83-324 9.61e-22

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


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 92.17  E-value: 9.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKvlfKSQIEKEGVEHQLRReieiqahLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14059    1 LGSGAQGAVFLGKFRGEE--VAVK---KVRDEKETDIKHLRK-------LNHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK-TMCGTLDYLP 241
Cdd:cd14059   69 YEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKmSFAGTVAWMA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 242 PEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesasHNETYRRIV------KVDLKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd14059  149 PEVIRNEPCSEKVDIWSFGVVLWELLTGEIPY----KDVDSSAIIwgvgsnSLQLPVPSTCPDGFKLLMKQCWNSKPRNR 224

                 ....*....
gi 927602445 316 LPLAQVSAH 324
Cdd:cd14059  225 PSFRQILMH 233
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
75-327 1.08e-21

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 93.26  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGvEHQLRREIEIQAH-LHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd06617    1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQE-QKRLLMDLDISMRsVDCPYTVTFYGALFREGDVWIC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRG--ELYKE-LQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR 229
Cdd:cd06617   79 MEVMDTSldKFYKKvYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTM-CGTLDYLPPEMIEGRM----HNEKVDLWCIGVLCYELLVGNPPFES-ASHNETYRRIVKvdlKFPASVPMGA--- 300
Cdd:cd06617  159 AKTIdAGCKPYMAPERINPELnqkgYDVKSDVWSLGITMIELATGRFPYDSwKTPFQQLKQVVE---EPSPQLPAEKfsp 235
                        250       260
                 ....*....|....*....|....*....
gi 927602445 301 --QDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06617  236 efQDFVNKCLKKNYKERPNYPELLQHPFF 264
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
75-328 1.44e-21

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 92.75  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiekeGVEHQLRREIEIQAHL-HHPNILRLYNYFYDRRR---- 149
Cdd:cd06639   22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPIS----DVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQyvgg 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 -IYLILEYAPRG---ELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH 224
Cdd:cd06639   98 qLWLVLELCNGGsvtELVKGLLKCGQrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQ 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APS--LRRKTMCGTLDYLPPEMIEGRM-----HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVK---VDLKFPA 294
Cdd:cd06639  178 LTSarLRRNTSVGTPFWMAPEVIACEQqydysYDARCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRnppPTLLNPE 257
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 295 SVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd06639  258 KWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
77-335 1.64e-21

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: 92.42  E-value: 1.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLVLTI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGEL----YKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR-K 231
Cdd:cd05605   82 MNGGDLkfhiYNMGNPG--FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETiR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQDLISKL 307
Cdd:cd05605  160 GRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFrarkEKVKREEVDRRVKEDQEEYSEKFSEEAKSICSQL 239
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 308 LRHNPSERLPL-----AQVSAHPWVRANSRRVL 335
Cdd:cd05605  240 LQKDPKTRLGCrgegaEDVKSHPFFKSINFKRL 272
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
82-326 1.67e-21

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 93.43  E-value: 1.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  82 PLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIekegVEHQLRREIEIQAHLHHPNILRL---------YNYFYDrrr 149
Cdd:cd07879   22 QVGSGAYGSVCSAIDKRTGEKVAIKKLsrpFQSEI----FAKRAYRELTLLKHMQHENVIGLldvftsavsGDEFQD--- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYaprgeLYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS 227
Cdd:cd07879   95 FYLVMPY-----MQTDLQKimGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 lrrkTMCG---TLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV--------------- 288
Cdd:cd07879  170 ----EMTGyvvTRWYRAPEVILNWMHyNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVtgvpgpefvqkledk 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 289 -----------------DLKFPASVPMGAqDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07879  246 aaksyikslpkyprkdfSTLFPKASPQAV-DLLEKMLELDVDKRLTATEALEHPY 299
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
81-316 1.78e-21

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 92.66  E-value: 1.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd05607    8 RVLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFETKTHLCLVMSLMNGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 EL----YKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTM-CG 235
Cdd:cd05607   88 DLkyhiYNVGERG--IEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQrAG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFP-ASVPMGAQDLISKLLRH 310
Cdd:cd05607  166 TNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFrdhkEKVSKEELKRRTLEDEVKFEhQNFTEEAKDICRLFLAK 245

                 ....*.
gi 927602445 311 NPSERL 316
Cdd:cd05607  246 KPENRL 251
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
83-326 1.81e-21

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 92.33  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVeHQLRreiEIQAHL---HHPNILRLYNYFYDRR--RIYLILE-- 155
Cdd:cd07831    7 IGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQV-NNLR---EIQALRrlsPHPNILRLIEVLFDRKtgRLALVFElm 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 ----YaprgELYKElQKSCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPENlLLGLKGELKIADFGwsvhapSLRrk 231
Cdd:cd07831   83 dmnlY----ELIKG-RKRP-LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPEN-ILIKDDILKLADFG------SCR-- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLD---------YLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFE------------------SASHNETYR 283
Cdd:cd07831  148 GIYSKPPyteyistrwYRAPEcLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPgtneldqiakihdvlgtpDAEVLKKFR 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 927602445 284 RIVKVDLKFPASVPMG-----------AQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07831  228 KSRHMNYNFPSKKGTGlrkllpnasaeGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
75-328 1.90e-21

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: 93.11  E-value: 1.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05632    2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKDALCLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQK--SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP---SLR 229
Cdd:cd05632   82 TIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPegeSIR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTmcGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLKFPASVPMGAQDLIS 305
Cdd:cd05632  162 GRV--GTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFrgrkEKVKREEVDRRVLETEEVYSAKFSEEAKSICK 239
                        250       260
                 ....*....|....*....|....*...
gi 927602445 306 KLLRHNPSERLPL-----AQVSAHPWVR 328
Cdd:cd05632  240 MLLTKDPKQRLGCqeegaGEVKRHPFFR 267
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
76-315 1.97e-21

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 92.17  E-value: 1.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVEhqlrREIEIQAHLHHPNILRLYNYFYD--------- 146
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKHRIDGKTYAIK---RVKLNNEKAE----REVKALAKLDHPNIVRYNGCWDGfdydpetss 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 147 -------RRRIYLILEYAPRGELYKELQKS--CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA 217
Cdd:cd14047   80 snssrskTKCLFIQMEFCEKGTLESWIEKRngEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 218 DFGW--SVHAPSLRRKTMcGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLvgnppFESASHNETYRRIVKV------- 288
Cdd:cd14047  160 DFGLvtSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELL-----HVCDSAFEKSKFWTDLrngilpd 233
                        250       260
                 ....*....|....*....|....*....
gi 927602445 289 --DLKFPASVPmgaqdLISKLLRHNPSER 315
Cdd:cd14047  234 ifDKRYKIEKT-----IIKKMLSKKPEDR 257
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
83-327 2.08e-21

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


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 92.09  E-value: 2.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfksQI-EKEGVEHQ-LRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIK-----EIpERDSREVQpLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELyKELQKS----CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG-ELKIADFGWSVHAPSLR--RKTM 233
Cdd:cd06624   91 SL-SALLRSkwgpLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYSgVVKISDFGTSKRLAGINpcTETF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGTLDYLPPEMIEG--RMHNEKVDLWCIGVLCYELLVGNPPF-ESASHNETYRRI--VKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd06624  170 TGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFiELGEPQAAMFKVgmFKIHPEIPESLSEEAKSFILRCF 249
                        250
                 ....*....|....*....
gi 927602445 309 RHNPSERLPLAQVSAHPWV 327
Cdd:cd06624  250 EPDPDKRATASDLLQDPFL 268
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
77-334 3.23e-21

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 92.09  E-value: 3.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRReieIQAHLHHPNILRLYNYFYDRR------RI 150
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQEINM---LKKYSHHRNIATYYGAFIKKNppgmddQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQ--KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSL 228
Cdd:cd06637   85 WLVMEFCGAGSVTDLIKntKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 --RRKTMCGTLDYLPPEMIE-----GRMHNEKVDLWCIGVLCYELLVGNPP----------FESASHNETYRRIVKVDLK 291
Cdd:cd06637  165 vgRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPlcdmhpmralFLIPRNPAPRLKSKKWSKK 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 927602445 292 FpasvpmgaQDLISKLLRHNPSERLPLAQVSAHPWVR--ANSRRV 334
Cdd:cd06637  245 F--------QSFIESCLVKNHSQRPSTEQLMKHPFIRdqPNERQV 281
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
83-340 3.34e-21

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 92.01  E-value: 3.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVK---KMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGAL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 yKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTMCGTLDYL 240
Cdd:cd06657  105 -TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcaQVSKEVPRRKSLVGTPYWM 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRI---VKVDLKFPASVPMGAQDLISKLLRHNPSERLP 317
Cdd:cd06657  184 APELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPKLKNLHKVSPSLKGFLDRLLVRDPAQRAT 263
                        250       260
                 ....*....|....*....|...
gi 927602445 318 LAQVSAHPWVransRRVLPPSAL 340
Cdd:cd06657  264 AAELLKHPFL----AKAGPPSCI 282
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
71-316 3.43e-21

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 92.82  E-value: 3.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIE-KEGVEHQLRREIEIQ--AHLHHPNILRLYNYFYDR 147
Cdd:cd05633    1 HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmKQGETLALNERIMLSlvSTGDCPFIVCMTYAFHTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS 227
Cdd:cd05633   81 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRRKTMCGTLDYLPPEMIE-GRMHNEKVDLWCIGVLCYELLVGNPPF---ESASHNETYRRIVKVDLKFPASVPMGAQDL 303
Cdd:cd05633  161 KKPHASVGTHGYMAPEVLQkGTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDSFSPELKSL 240
                        250
                 ....*....|...
gi 927602445 304 ISKLLRHNPSERL 316
Cdd:cd05633  241 LEGLLQRDVSKRL 253
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
77-327 4.90e-21

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 90.80  E-value: 4.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEG-VEHQLRREIEI----QAHLHHPNILRLYNYFYDRRRIY 151
Cdd:cd14100    2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGeLPNGTRVPMEIvllkKVGSGFRGVIRLLDWFERPDSFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYA-PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG-ELKIADFGwsvhAPSLR 229
Cdd:cd14100   82 LVLERPePVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTgELKLIDFG----SGALL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMC----GTLDYLPPEMIE-GRMHNEKVDLWCIGVLCYELLVGNPPFEsasHNEtyrRIVKVDLKFPASVPMGAQDLI 304
Cdd:cd14100  158 KDTVYtdfdGTRVYSPPEWIRfHRYHGRSAAVWSLGILLYDMVCGDIPFE---HDE---EIIRGQVFFRQRVSSECQHLI 231
                        250       260
                 ....*....|....*....|...
gi 927602445 305 SKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14100  232 KWCLALRPSDRPSFEDIQNHPWM 254
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
77-328 6.35e-21

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 90.59  E-value: 6.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfkSQIEKEGVE--HQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKM--SYSGKQSTEkwQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EY-----APRGELYKELQKsctfdEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG-WSVHAPSl 228
Cdd:cd06607   81 EYclgsaSDIVEVHKKPLQ-----EVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGsASLVCPA- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 rrKTMCGTLDYLPPEMI----EGRmHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDlkfPASVPMGA---- 300
Cdd:cd06607  155 --NSFVGTPYWMAPEVIlamdEGQ-YDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQND---SPTLSSGEwsdd 228
                        250       260
                 ....*....|....*....|....*....
gi 927602445 301 -QDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd06607  229 fRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
78-276 6.83e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 93.32  E-value: 6.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQ-------IEKegvehqLRREIEIQAHLHHPNILRLYNYFYDRRRI 150
Cdd:NF033483  10 EIGERIGRGGMAEVYLAKDTRLDRDVAVKVL-RPDlardpefVAR------FRREAQSAASLSHPNIVSVYDVGEDGGIP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPrGELYKE-LQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPS 227
Cdd:NF033483  83 YIVMEYVD-GRTLKDyIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIarALSSTT 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 228 LRRK-TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF--ESA 276
Cdd:NF033483 162 MTQTnSVLGTVHYLSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPFdgDSP 213
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
77-273 7.13e-21

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 90.84  E-value: 7.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvehQLRREIE-IQAHLHHPNILRLYNYFYDRR------R 149
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEE----EIKLEINmLKKYSHHRNIATYYGAFIKKSppghddQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRG---ELYKELQKSCtFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP 226
Cdd:cd06636   94 LWLVMEFCGAGsvtDLVKNTKGNA-LKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLD 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 927602445 227 SL--RRKTMCGTLDYLPPEMIE-----GRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd06636  173 RTvgRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPL 226
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
83-326 8.12e-21

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 89.98  E-value: 8.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVA---LKVLFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYD--RRRIYLILEYA 157
Cdd:cd13983    9 LGRGSFKTVYRAFDTEEGIEVAwneIKLRKLPKAERQ----RFKQEIEILKSLKHPNIIKFYDSWESksKKEVIFITELM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENL-LLGLKGELKIADFGWSVHAPSLRRKTMC 234
Cdd:cd13983   85 TSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIfINGNTGEVKIGDLGLATLLRQSFAKSVI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMIEGRmHNEKVDLWCIGVLCYELLVGNPPF-ESASHNETYRRIVKVdlKFPASV-----PMgAQDLISKLL 308
Cdd:cd13983  165 GTPEFMAPEMYEEH-YDEKVDIYAFGMCLLEMATGEYPYsECTNAAQIYKKVTSG--IKPESLskvkdPE-LKDFIEKCL 240
                        250
                 ....*....|....*...
gi 927602445 309 RHnPSERLPLAQVSAHPW 326
Cdd:cd13983  241 KP-PDERPSARELLEHPF 257
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
75-327 1.04e-20

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 89.90  E-value: 1.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKS--HFIVALKVLFKSQIEKEGVehqlrREIEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd14112    3 GRFSFGSEIFRGRFSVIVKAVDSTTetDAHCAVKIFEVSDEASEAV-----REFESLRTLQHENVQRLIAAFKPSNFAYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEyaprgELYKELQKSCTFD----EQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKI--ADFGWSVHAP 226
Cdd:cd14112   78 VME-----KLQEDVFTRFSSNdyysEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVklVDFGRAQKVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRKTMCGTLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHN--ETYRRIVKVDLKF---PASVPMGA 300
Cdd:cd14112  153 KLGKVPVDGDTDWASPEFHNPETPiTVQSDIWGLGVLTFCLLSGFHPFTSEYDDeeETKENVIFVKCRPnliFVEATQEA 232
                        250       260
                 ....*....|....*....|....*..
gi 927602445 301 QDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14112  233 LRFATWALKKSPTRRMRTDEALEHRWL 259
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
73-273 1.41e-20

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 90.09  E-value: 1.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  73 TIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd08229   22 TLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNI 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGEL---YKELQKSCTFDEQRTA-TIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAP 226
Cdd:cd08229  102 VLELADAGDLsrmIKHFKKQKRLIPEKTVwKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGrfFSSK 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 927602445 227 SLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd08229  182 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF 228
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
68-272 1.61e-20

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 89.72  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  68 LTRHFTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQlrrEIEIQAHLHHPNILRLYNYFYDR 147
Cdd:cd06645    4 LSRRNPQEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQ---EIIMMKDCKHSNIVAYFGSYLRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHA 225
Cdd:cd06645   81 DKLWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSaqITA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCGTLDYLPPEM--IEGR-MHNEKVDLWCIGVLCYELLVGNPP 272
Cdd:cd06645  161 TIAKRKSFIGTPYWMAPEVaaVERKgGYNQLCDIWAVGITAIELAELQPP 210
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
81-327 1.64e-20

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


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 90.71  E-value: 1.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSqIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYD-RRRIYLILEYapR 159
Cdd:cd07856   16 QPVGMGAFGLVCSARDQLTGQNVAVKKIMKP-FSTPVLAKRTYRELKLLKHLRHENIISLSDIFISpLEDIYFVTEL--L 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvhapSLRRKTMCG---T 236
Cdd:cd07856   93 GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLA----RIQDPQMTGyvsT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 LDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----------------DLKFPASVPM- 298
Cdd:cd07856  169 RYYRAPEiMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELlgtppddvinticsenTLRFVQSLPKr 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 299 --------------GAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07856  249 ervpfsekfknadpDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
75-322 1.76e-20

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 90.06  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHL-HHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05089    2 EDIKFEDVIGEGNFGQVIKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKS----------------CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA 217
Cdd:cd05089   82 IEYAPYGNLLDFLRKSrvletdpafakehgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 218 DFGWSVHAPSLRRKTMcGTLD--YLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK-VDLKFP 293
Cdd:cd05089  162 DFGLSRGEEVYVKKTM-GRLPvrWMAIESLNYSVYTTKSDVWSFGVLLWEIVsLGGTPYCGMTCAELYEKLPQgYRMEKP 240
                        250       260
                 ....*....|....*....|....*....
gi 927602445 294 ASVPMGAQDLISKLLRHNPSERLPLAQVS 322
Cdd:cd05089  241 RNCDDEVYELMRQCWRDRPYERPPFSQIS 269
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
78-322 1.78e-20

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 89.65  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRPLGKGKFGNVYLAREKKSHFIVALK-VLFKSqiekegvEHQL---RREIEIQAHLH-HPNILRLYNYFYDRRR--- 149
Cdd:cd14037    6 TIEKYLAEGGFAHVYLVKTSNGGNRAALKrVYVND-------EHDLnvcKREIEIMKRLSgHKNIVGYIDSSANRSGngv 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 --IYLILEYAPRGELYKELQK--SCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKGELKIADFGwSV 223
Cdd:cd14037   79 yeVLLLMEYCKGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFG-SA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTMCG------------TLDYLPPEMIE---GRMHNEKVDLWCIGVLCYELLVGNPPFEsashnETYR-RIVK 287
Cdd:cd14037  158 TTKILPPQTKQGvtyveedikkytTLQYRAPEMIDlyrGKPITEKSDIWALGCLLYKLCFYTTPFE-----ESGQlAILN 232
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 927602445 288 VDLKFPaSVPMGAQD---LISKLLRHNPSERLPLAQVS 322
Cdd:cd14037  233 GNFTFP-DNSRYSKRlhkLIRYMLEEDPEKRPNIYQVS 269
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
83-338 1.99e-20

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 90.05  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfksQIE-KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGe 161
Cdd:cd07872   14 LGEGTYATVFKGRSKLTENLVALKEI---RLEhEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKD- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 lYKELQKSC--TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRRKTMCG---T 236
Cdd:cd07872   90 -LKQYMDDCgnIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLA-RAKSVPTKTYSNevvT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 LDYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPFESAS---------------HNETYRRIVKVD----LKFPASV 296
Cdd:cd07872  168 LWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLFPGSTvedelhlifrllgtpTEETWPGISSNDefknYNFPKYK 247
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 297 PM-----------GAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRV--LPPS 338
Cdd:cd07872  248 PQplinhaprldtEGIELLTKFLQYESKKRISAEEAMKHAYFRSLGTRIhsLPES 302
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
75-315 2.44e-20

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 89.02  E-value: 2.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLA--REKKSHFI-VALKVlFKSQIEKEGVEHQLRrEIEIQAHLHHPNILRLYNYFYDRRrIY 151
Cdd:cd05056    6 EDITLGRCIGEGQFGDVYQGvyMSPENEKIaVAVKT-CKNCTSPSVREKFLQ-EAYIMRQFDHPHIVKLIGVITENP-VW 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIME-ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSL 228
Cdd:cd05056   83 IVMELAPLGELRSYLQVNKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSryMEDESY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMcGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKVD-LKFPASVPMGAQDLI 304
Cdd:cd05056  163 YKASK-GKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLM 241
                        250
                 ....*....|.
gi 927602445 305 SKLLRHNPSER 315
Cdd:cd05056  242 TKCWAYDPSKR 252
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
83-273 2.93e-20

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: 89.86  E-value: 2.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVlFKSQIEKEGVEHQlRREIEIQAHLHHPNILRLYNYFYDR--RRIYLILEYAPRG 160
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKV-FNNLSFMRPLDVQ-MREFEVLKKLNHKNIVKLFAIEEELttRHKVLVMELCPCG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQK---SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGlkgelkIADFGWSVH-------APSLRR 230
Cdd:cd13988   79 SLYTVLEEpsnAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRV------IGEDGQSVYkltdfgaARELED 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 231 K----TMCGTLDYLPPEMIE--------GRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd13988  153 DeqfvSLYGTEEYLHPDMYEravlrkdhQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
82-326 3.34e-20

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 88.98  E-value: 3.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  82 PLGKGKFGNVYLAREKKSHFIVALKVLfkSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRgE 161
Cdd:cd07844    7 KLGEGSYATVYKGRSKLTGQLVALKEI--RLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDT-D 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATI-MEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRRKTMCG---TL 237
Cdd:cd07844   84 LKQYMDDCGGGLSMHNVRLfLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLA-RAKSVPSKTYSNevvTL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMIEG-RMHNEKVDLWCIGVLCYELLVGNPPFESASH-NETYRRIVKV-------------------DLKFPASV 296
Cdd:cd07844  163 WYRPPDVLLGsTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDvEDQLHKIFRVlgtpteetwpgvssnpefkPYSFPFYP 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 297 P-------------MGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07844  243 PrplinhaprldriPHGEELALKFLQYEPKKRISAAEAMKHPY 285
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
77-326 3.72e-20

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 90.87  E-value: 3.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvehqlrREIEIQAHLHHPNILRLYNYFY------DRRRI 150
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKN-------RELLIMKNLNHINIIFLKDYYYtecfkkNEKNI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YL--ILEYAPRgELYKELQKSCTFDEQRTATIME----ELADALMYCHGKKVIHRDIKPENLLLG-LKGELKIADFGWSV 223
Cdd:PTZ00036 141 FLnvVMEFIPQ-TVHKYMKHYARNNHALPLFLVKlysyQLCRALAYIHSKFICHRDLKPQNLLIDpNTHTLKLCDFGSAK 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKT--MCGTLdYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV------------ 288
Cdd:PTZ00036 220 NLLAGQRSVsyICSRF-YRAPELMLGATnYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVlgtptedqlkem 298
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 289 ---------------DLK--FPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:PTZ00036 299 npnyadikfpdvkpkDLKkvFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPF 353
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
83-326 4.45e-20

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 88.86  E-value: 4.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfkSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd07870    8 LGEGSYATVYKGISRINGQLVALKVI--SMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvHAPSLRRKTMCG---TLDY 239
Cdd:cd07870   86 QYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLA-RAKSIPSQTYSSevvTLWY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPFESASH----------------NETYRRIVKVDLKFPA-------- 294
Cdd:cd07870  165 RPPDVLLGATdYSSALDIWGAGCIFIEMLQGQPAFPGVSDvfeqlekiwtvlgvptEDTWPGVSKLPNYKPEwflpckpq 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 927602445 295 ---------SVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07870  245 qlrvvwkrlSRPPKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
85-327 5.50e-20

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 87.67  E-value: 5.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  85 KGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVehqlRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELYK 164
Cdd:cd14110   13 RGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQLV----LREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 165 ELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYL---P 241
Cdd:cd14110   89 NLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVetmA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 242 PEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP---ASVPMGAQDLISKLLRHNPSERLPL 318
Cdd:cd14110  169 PELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSrcyAGLSGGAVNFLKSTLCAKPWGRPTA 248

                 ....*....
gi 927602445 319 AQVSAHPWV 327
Cdd:cd14110  249 SECLQNPWL 257
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
79-315 7.04e-20

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 90.31  E-value: 7.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNVYLAREKKSHFIVALKVlfksqIEKEGVEHQ--LRREIEIQAHLH--HPNILRLYNYFYDR------- 147
Cdd:PTZ00283  36 ISRVLGSGATGTVLCAKRVSDGEPFAVKV-----VDMEGMSEAdkNRAQAEVCCLLNcdFFSIVKCHEDFAKKdprnpen 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 -RRIYLILEYAPRGELYKELQK----SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS 222
Cdd:PTZ00283 111 vLMIALVLDYANAGDLRQEIKSraktNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFS 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRR----KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDlKFPASV 296
Cdd:PTZ00283 191 KMYAATVSddvgRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLagRYD-PLPPSI 269
                        250
                 ....*....|....*....
gi 927602445 297 PMGAQDLISKLLRHNPSER 315
Cdd:PTZ00283 270 SPEMQEIVTALLSSDPKRR 288
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
82-315 7.68e-20

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: 87.44  E-value: 7.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  82 PLGKGKFGNVYLAREKKSHfiVALKVLfKSQIEKEGVEHQLRREIEIqAHLHHPNILRLY--NYFYDRRRIYLIL-EYAP 158
Cdd:cd13979   10 PLGSGGFGSVYKATYKGET--VAVKIV-RRRRKNRASRQSFWAELNA-ARLRHENIVRVLaaETGTDFASLGLIImEYCG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RG-------ELYKELQKsctfdeQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSV-----HAP 226
Cdd:cd13979   86 NGtlqqliyEGSEPLPL------AHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVklgegNEV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYrRIVKVDLKfPASVPMG------- 299
Cdd:cd13979  160 GTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLY-AVVAKDLR-PDLSGLEdsefgqr 237
                        250
                 ....*....|....*.
gi 927602445 300 AQDLISKLLRHNPSER 315
Cdd:cd13979  238 LRSLISRCWSAQPAER 253
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
80-321 8.12e-20

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


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 87.83  E-value: 8.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKS-HFIVALKVLFKSQIEKEGVE-HQLRREIEIQAHLHHPNILRLYNYFYDR--RRIYLILE 155
Cdd:cd06651   12 GKLLGQGAFGRVYLCYDVDTgRELAAKQVQFDPESPETSKEvSALECEIQLLKNLQHERIVQYYGCLRDRaeKTLTIFME 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsvhaPSLRRKTMC- 234
Cdd:cd06651   92 YMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-----ASKRLQTICm 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 ---------GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVKV-----DLKFPASVPMGA 300
Cdd:cd06651  167 sgtgirsvtGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPW---AEYEAMAAIFKIatqptNPQLPSHISEHA 243
                        250       260
                 ....*....|....*....|....*...
gi 927602445 301 QDLISKLL---RHNPSE----RLPLAQV 321
Cdd:cd06651  244 RDFLGCIFveaRHRPSAeellRHPFAQL 271
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
71-344 9.35e-20

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 88.19  E-value: 9.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDD-FEIGRPLGKGKFGNVYLAREKKSHFIVALKV--LFKS--QIEKEGVEHQLRREIEIQAHLHHPNILRLYNYF- 144
Cdd:cd14041    1 HPTLNDrYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFs 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 145 YDRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKGE---LKIADF 219
Cdd:cd14041   81 LDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTAcgeIKITDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 220 GWS----------VHAPSLRRKTmCGTLDYLPPEMI----EGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRI 285
Cdd:cd14041  161 GLSkimdddsynsVDGMELTSQG-AGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFYQCLYGRKPF---GHNQSQQDI 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 286 VK-------VDLKFPAS--VPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSALQSVA 344
Cdd:cd14041  237 LQentilkaTEVQFPPKpvVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAA 304
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
76-325 1.00e-19

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 87.48  E-value: 1.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIV-ALKVLFKSQIEKEGVEHQLRrEIEIQAHLH---HPNILRLYNYFYDRRRIY 151
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYAGAKDRLRRLE-EVSILRELTldgHDNIVQLIDSWEYHGHLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGEL---YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSL 228
Cdd:cd14052   80 IQTELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMATVWPLI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-------GNP------------PFESASHNETYRRIVKVD 289
Cdd:cd14052  160 RGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLEAAAnvvlpdnGDAwqklrsgdlsdaPRLSSTDLHSASSPSSNP 239
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 927602445 290 LKFPASVPMGAQDL---ISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd14052  240 PPDPPNMPILSGSLdrvVRWMLSPEPDRRPTADDVLATP 278
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
76-315 1.04e-19

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 87.10  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKkSHFIVALKVLfKSqiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05148    7 EFTLERKLGSGYFGEVWEGLWK-NRVRVAIKIL-KS--DDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELyKELQKSCTFDEQRTATIME---ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW------SVHAP 226
Cdd:cd05148   83 LMEKGSL-LAFLRSPEGQVLPVASLIDmacQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLarlikeDVYLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRKTMCGTldylPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGAQDLI 304
Cdd:cd05148  162 SDKKIPYKWT----APEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAgYRMPCPAKCPQEIYKIM 237
                        250
                 ....*....|.
gi 927602445 305 SKLLRHNPSER 315
Cdd:cd05148  238 LECWAAEPEDR 248
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
81-288 1.10e-19

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: 88.47  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSqIEKEGVEHQLRREIEIQAHLHHPNILRLYNYF-----YDR-RRIYLIL 154
Cdd:cd07880   21 KQVGSGAYGTVCSALDRRTGAKVAIKKLYRP-FQSELFAKRAYRELRLLKHMKHENVIGLLDVFtpdlsLDRfHDFYLVM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAprGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSlrrkTMC 234
Cdd:cd07880  100 PFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDS----EMT 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 235 G---TLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV 288
Cdd:cd07880  174 GyvvTRWYRAPEVILNWMHyTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKV 231
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
82-326 1.28e-19

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: 88.17  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  82 PLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRR------IYL 152
Cdd:cd07877   24 PVGSGAYGSVCAAFDTKTGLRVAVKKLsrpFQSIIHAK----RTYRELRLLKHMKHENVIGLLDVFTPARSleefndVYL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAprGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPslrrKT 232
Cdd:cd07877  100 VTHLM--GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTD----DE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCG---TLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASH-----------------------NETYRRI 285
Cdd:cd07877  174 MTGyvaTRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLTGRTLFPGTDHidqlklilrlvgtpgaellkkisSESARNY 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 927602445 286 VKVDLKFP----ASVPMGAQ----DLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07877  254 IQSLTQMPkmnfANVFIGANplavDLLEKMLVLDSDKRITAAQALAHAY 302
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
83-328 1.64e-19

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 86.86  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEgVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd06619    9 LGHGNGGTVYKAYHLLTRRILAVKVI-PLDITVE-LQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 --YKELQksctfdEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYL 240
Cdd:cd06619   87 dvYRKIP------EHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYVGTNAYM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 241 PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHN-------ETYRRIVKVDlkfPASVPMGA-----QDLISKLL 308
Cdd:cd06619  161 APERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNqgslmplQLLQCIVDED---PPVLPVGQfsekfVHFITQCM 237
                        250       260
                 ....*....|....*....|
gi 927602445 309 RHNPSERLPLAQVSAHPWVR 328
Cdd:cd06619  238 RKQPKERPAPENLMDHPFIV 257
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
83-311 1.75e-19

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 87.40  E-value: 1.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY--APRG 160
Cdd:cd06633   29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYclGSAS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG-WSVHAPSlrrKTMCGTLDY 239
Cdd:cd06633  109 DLLEVHKKP--LQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGsASIASPA---NSFVGTPYW 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 240 LPPEMI----EGRmHNEKVDLWCIGVLCYELLVGNPP--------------------FESASHNETYRRIVKVDL-KFPA 294
Cdd:cd06633  184 MAPEVIlamdEGQ-YDGKVDIWSLGITCIELAERKPPlfnmnamsalyhiaqndsptLQSNEWTDSFRGFVDYCLqKIPQ 262
                        250
                 ....*....|....*..
gi 927602445 295 SVPMGAQdliskLLRHN 311
Cdd:cd06633  263 ERPSSAE-----LLRHD 274
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
83-333 2.39e-19

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 87.03  E-value: 2.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKV--LFKS--QIEKEGVEHQLRREIEIQAHLHHPNILRLYNYF-YDRRRIYLILEYA 157
Cdd:cd14040   14 LGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKGE---LKIADFGWS---------V 223
Cdd:cd14040   94 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSkimdddsygV 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTmCGTLDYLPPEMI----EGRMHNEKVDLWCIGVLCYELLVGNPPFesaSHNETYRRIVK-------VDLKF 292
Cdd:cd14040  174 DGMDLTSQG-AGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF---GHNQSQQDILQentilkaTEVQF 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 293 PAS--VPMGAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRR 333
Cdd:cd14040  250 PVKpvVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRR 292
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
103-320 2.55e-19

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: 89.13  E-value: 2.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   103 VALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLynyfYDR-----RRIYLILEYAPRGELYKELQKSCTFDEQRT 177
Cdd:TIGR03903    6 VAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVAL----LDSgeappGLLFAVFEYVPGRTLREVLAADGALPAGET 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   178 ATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAP--------SLRRKT-MCGTLDYLPPEMI 245
Cdd:TIGR03903   82 GRLMLQVLDALACAHNQGIVHRDLKPQNimvSQTGVRPHAKVLDFGIGTLLPgvrdadvaTLTRTTeVLGTPTYCAPEQL 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445   246 EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNET-YRRIVKVDLKFP---ASVPMGaqDLISKLLRHNPSERLPLAQ 320
Cdd:TIGR03903  162 RGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEIlYQQLSPVDVSLPpwiAGHPLG--QVLRKALNKDPRQRAASAP 238
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
81-326 2.85e-19

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: 87.41  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIekegveHQLR--REIEIQAHLHHPNILRLYNYFY------DRRR 149
Cdd:cd07878   21 TPVGSGAYGSVCSAYDTRLRQKVAVKKLsrpFQSLI------HARRtyRELRLLKHMKHENVIGLLDVFTpatsieNFNE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAprGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsvhapsLR 229
Cdd:cd07878   95 VYLVTNLM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFG-------LA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKT---MCG---TLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-------------- 288
Cdd:cd07878  166 RQAddeMTGyvaTRWYRAPEIMLNWMHyNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVvgtpspevlkkiss 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 927602445 289 ----------------DLK--FPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07878  246 eharkyiqslphmpqqDLKkiFRGANPL-AIDLLEKMLVLDSDKRISASEALAHPY 300
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
77-239 4.51e-19

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 85.20  E-value: 4.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfksqIEKEGVEH-QLRREIEIQAHLH-HPNILRLYNYFYDRRRIYLIL 154
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIK------IEKKDSKHpQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVMVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYaprgeLYKELQ---KSC--TFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL---LLGLKGELKIADFGWS---- 222
Cdd:cd14016   76 DL-----LGPSLEdlfNKCgrKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFlmgLGKNSNKVYLIDFGLAkkyr 150
                        170       180
                 ....*....|....*....|..
gi 927602445 223 -----VHAPSLRRKTMCGTLDY 239
Cdd:cd14016  151 dprtgKHIPYREGKSLTGTARY 172
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
81-317 4.91e-19

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 85.51  E-value: 4.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAR----EKKSHFIVALKVLFKSQieKEGVEHQLRREIEIQAHLHHPNILRLYNYFYD--RRRIYLIL 154
Cdd:cd05038   10 KQLGEGHFGSVELCRydplGDNTGEQVAVKSLQPSG--EEQHMSDFKREIEILRTLDHEYIVKYKGVCESpgRRSLRLIM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKscTFDEQRTATIM---EELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK 231
Cdd:cd05038   88 EYLPSGSLRDYLQR--HRDQIDLKRLLlfaSQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEDKEY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLP-----PEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETyrrivkvDLKFPASVPMGAQDLISK 306
Cdd:cd05038  166 YYVKEPGESPifwyaPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPALFL-------RMIGIAQGQMIVTRLLEL 238
                        250
                 ....*....|.
gi 927602445 307 LlrhNPSERLP 317
Cdd:cd05038  239 L---KSGERLP 246
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
83-267 6.59e-19

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 85.01  E-value: 6.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQiekEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFD---EETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 ---YKELQKSCTFDEQrtATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS----------VHAPSLR 229
Cdd:cd14221   78 rgiIKSMDSHYPWSQR--VSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdektqpEGLRSLK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 927602445 230 RK------TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:cd14221  156 KPdrkkryTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
83-263 7.70e-19

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 84.87  E-value: 7.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQiekEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFD---EEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHAPSLR---------- 229
Cdd:cd14154   78 KDVLKdMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArlIVEERLPsgnmspsetl 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 927602445 230 ----------RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIG-VLC 263
Cdd:cd14154  158 rhlkspdrkkRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGiVLC 202
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
83-267 1.02e-18

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 84.61  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQiekEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIRCD---EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-------VHAPSLR------ 229
Cdd:cd14222   78 KDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveekKKPPPDKpttkkr 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 927602445 230 ---------RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:cd14222  158 tlrkndrkkRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
83-267 1.26e-18

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 84.08  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKvlfksqIEKEGVEH-QLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMK------ELKRFDEQrSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LyKELQKSctFDEQ----RTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAPSLRRK--- 231
Cdd:cd14065   75 L-EELLKS--MDEQlpwsQRVSLAKDIASGMAYLHSKNIIHRDLNSKNclvREANRGRNAVVADFGLAREMPDEKTKkpd 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 927602445 232 -----TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:cd14065  152 rkkrlTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
83-319 1.57e-18

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 84.20  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKVLFKSQIEKEGVEH------------------QLRREIEIQAHLHHPNILRLYNYF 144
Cdd:cd14000    2 LGDGGFGSVYRASYKGEP--VAVKIFNKHTSSNFANVPadtmlrhlratdamknfrLLRQELTVLSHLHHPSIVYLLGIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 145 YDRRriYLILEYAPRGELYKELQKS----CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL-----LLGLKGELK 215
Cdd:cd14000   80 IHPL--MLVLELAPLGSLDHLLQQDsrsfASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVlvwtlYPNSAIIIK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 216 IADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGR-MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVK---VDLK 291
Cdd:cd14000  158 IADYGISRQCCRMGAKGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHGglrPPLK 237
                        250       260
                 ....*....|....*....|....*....
gi 927602445 292 FPASVPMG-AQDLISKLLRHNPSERlPLA 319
Cdd:cd14000  238 QYECAPWPeVEVLMKKCWKENPQQR-PTA 265
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
66-272 1.69e-18

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 83.92  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  66 DILTRHfTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFY 145
Cdd:cd06646    1 DILRRN-PQHDYELIQRVGSGTYGDVYKARNLHTGELAAVKII---KLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--V 223
Cdd:cd06646   77 SREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAakI 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 224 HAPSLRRKTMCGTLDYLPPEMI---EGRMHNEKVDLWCIGVLCYELLVGNPP 272
Cdd:cd06646  157 TATIAKRKSFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPP 208
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
83-321 1.98e-18

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


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 83.53  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYlarEKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILrLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14150    8 IGTGSFGTVF---RGKWHGDVAVKILKVTEPTPEQLQ-AFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGSSL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG-------WS----VHAPSlrr 230
Cdd:cd14150   83 YRHLHVTETrFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGlatvktrWSgsqqVEQPS--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 ktmcGTLDYLPPEMIegRMHNE-----KVDLWCIGVLCYELLVGNPPFESASHNETY-----RRIVKVDL-KFPASVPMG 299
Cdd:cd14150  160 ----GSILWMAPEVI--RMQDTnpysfQSDVYAYGVVLYELMSGTLPYSNINNRDQIifmvgRGYLSPDLsKLSSNCPKA 233
                        250       260
                 ....*....|....*....|..
gi 927602445 300 AQDLISKLLRHNPSERLPLAQV 321
Cdd:cd14150  234 MKRLLIDCLKFKREERPLFPQI 255
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
80-327 2.66e-18

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: 83.25  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIvALKVLFKSQIEKEGVEHQ---LRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd06631    6 GNVLGKGAYGTVYCGLTSTGQLI-AVKQVELDTSDKEKAEKEyekLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG--------WSVHAPSL 228
Cdd:cd06631   85 VPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrlcinLSSGSQSQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPP----------FESASHnetyRRIVKvdlKFPASVPM 298
Cdd:cd06631  165 LLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPwadmnpmaaiFAIGSG----RKPVP---RLPDKFSP 237
                        250       260
                 ....*....|....*....|....*....
gi 927602445 299 GAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd06631  238 EARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
83-326 2.72e-18

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 83.86  E-value: 2.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQ---AHLHHPNILRLYNYFYDRR-----RIYLIL 154
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSV-RVQTNEDGLPLSTVREVALLkrlEAFDHPNIVRLMDVCATSRtdretKVTLVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRgELYKELQKSCT--FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHAPSLRRK 231
Cdd:cd07863   87 EHVDQ-DLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLArIYSCQMALT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV-----------DLKFPAS----- 295
Cdd:cd07863  166 PVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLiglppeddwprDVTLPRGafspr 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 296 --------VP----MGAqDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07863  246 gprpvqsvVPeieeSGA-QLLLEMLTFNPHKRISAFRALQHPF 287
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
83-276 3.14e-18

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 83.31  E-value: 3.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAReKKSHFIVALKVLFKSQieKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE- 161
Cdd:cd14664    1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEG--TQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSl 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 ---LYKELQKSCTFDEQRTATIMEELADALMYCH---GKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLRRKT 232
Cdd:cd14664   78 gelLHSRPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAklmDDKDSHVMSS 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESA 276
Cdd:cd14664  158 VAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEA 201
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
83-282 3.17e-18

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 83.72  E-value: 3.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVAlKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14159    1 IGEGGFGCVYQAVMRNTEYAVK-RLKEDSELDWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKSCTFD----EQRTaTIMEELADALMYCHGKK--VIHRDIKPENLLLGLKGELKIADFGW-----SVHAPSL--- 228
Cdd:cd14159   80 EDRLHCQVSCPclswSQRL-HVLLGTARAIQYLHSDSpsLIHGDVKSSNILLDAALNPKLGDFGLarfsrRPKQPGMsst 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 927602445 229 --RRKTMCGTLDYLPPEMIE-GRMHNEkVDLWCIGVLCYELLVGNPPFESASHNETY 282
Cdd:cd14159  159 laRTQTVRGTLAYLPEEYVKtGTLSVE-IDVYSFGVVLLELLTGRRAMEVDSCSPTK 214
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
83-315 3.43e-18

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 83.28  E-value: 3.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKS-----HFIVALKVLfkSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd05046   13 LGRGEFGEVFLAKAKGIeeeggETLVLVKAL--QKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREAEPHYMILEYT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDE----------QRTAtIMEELADALMYCHGKKVIHRDIKPENLLLGlkgelkiADFGWSVHAPS 227
Cdd:cd05046   91 DLGDLKQFLRATKSKDEklkppplstkQKVA-LCTQIALGMDHLSNARFVHRDLAARNCLVS-------SQREVKVSLLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRR----------KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKVDLKFPasV 296
Cdd:cd05046  163 LSKdvynseyyklRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELP--V 240
                        250       260
                 ....*....|....*....|...
gi 927602445 297 PMGAQDLISKLLRH----NPSER 315
Cdd:cd05046  241 PEGCPSRLYKLMTRcwavNPKDR 263
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
109-325 4.06e-18

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


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 82.41  E-value: 4.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 109 FKSQIEkegvehQLRREIEIQAHLHHPNILRLYNYFYDRR------RIYLILEYAPRGELYKELQKSCTFDEQRTATIME 182
Cdd:cd14012   38 GKKQIQ------LLEKELESLKKLRHPNLVSYLAFSIERRgrsdgwKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 183 ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLD------YLPPEMIEGRM-HNEKVD 255
Cdd:cd14012  112 QLLEALEYLHRNGVVHKSLHAGNVLLDRDAGTGIVKLTDYSLGKTLLDMCSRGSLDefkqtyWLPPELAQGSKsPTRKTD 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 256 LWCIGVLCYELLVGNPPFEsashNETYRRIVKVDLKFPASVpmgaQDLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd14012  192 VWDLGLLFLQMLFGLDVLE----KYTSPNPVLVSLDLSASL----QDFLSKCLSLDPKKRPTALELLPHE 253
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
74-315 6.27e-18

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 82.11  E-value: 6.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEI--GRPLGKGKFGNVYLArEKKSHFIVALKVLfksqieKEGV--EHQLRREIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd05059    1 IDPSELtfLKELGSGQFGVVHLG-KWRGKIDVAIKMI------KEGSmsEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQKSctFDEQRTATIME---ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP 226
Cdd:cd05059   74 IFIVTEYMANGCLLNYLRER--RGKFQTEQLLEmckDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRKTMCGT---LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGAQ 301
Cdd:cd05059  152 DDEYTSSVGTkfpVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQgYRLYRPHLAPTEVY 231
                        250
                 ....*....|....
gi 927602445 302 DLISKLLRHNPSER 315
Cdd:cd05059  232 TIMYSCWHEKPEER 245
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
65-273 6.61e-18

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 83.18  E-value: 6.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  65 PDILTRHFTIDD---FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLY 141
Cdd:cd06635   12 PDIAELFFKEDPeklFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 142 NYFYDRRRIYLILEY--APRGELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADF 219
Cdd:cd06635   92 GCYLREHTAWLVMEYclGSASDLLEVHKKP--LQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADF 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 220 G-WSVHAPSlrrKTMCGTLDYLPPEMI----EGRmHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd06635  170 GsASIASPA---NSFVGTPYWMAPEVIlamdEGQ-YDGKVDVWSLGITCIELAERKPPL 224
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
72-283 8.73e-18

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


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 82.76  E-value: 8.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLA------REK-KSHFIVALKVLFKSQIEKEGVEhqLRREIEIQAHL-HHPNILRLYNY 143
Cdd:cd05101   21 FPRDKLTLGKPLGEGCFGQVVMAeavgidKDKpKEAVTVAVKMLKDDATEKDLSD--LVSEMEMMKMIgKHKNIINLLGA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 144 FYDRRRIYLILEYAPRGELYKELQK------------SCTFDEQRT----ATIMEELADALMYCHGKKVIHRDIKPENLL 207
Cdd:cd05101   99 CTQDGPLYVIVEYASKGNLREYLRArrppgmeysydiNRVPEEQMTfkdlVSCTYQLARGMEYLASQKCIHRDLAARNVL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 208 LGLKGELKIADFGWS--VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETY 282
Cdd:cd05101  179 VTENNVMKIADFGLArdINNIDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLMWEIFtLGGSPYPGIPVEELF 258

                 .
gi 927602445 283 R 283
Cdd:cd05101  259 K 259
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
75-326 9.58e-18

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 81.49  E-value: 9.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVehqlRREIEIQAHLHHPNILRLYNYFyDRRRIYLIL 154
Cdd:cd14108    2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTSA----RRELALLAELDHKSIVRFHDAF-EKRRVVIIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN--LLLGLKGELKIADFGWSVH-APSLRRK 231
Cdd:cd14108   77 TELCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENllMADQKTDQVRICDFGNAQElTPNEPQY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMG----AQDLISKL 307
Cdd:cd14108  157 CKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESMFKDlcreAKGFIIKV 236
                        250       260
                 ....*....|....*....|.
gi 927602445 308 LRHNpseRL-PLA-QVSAHPW 326
Cdd:cd14108  237 LVSD---RLrPDAeETLEHPW 254
pknD PRK13184
serine/threonine-protein kinase PknD;
77-315 9.69e-18

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 84.44  E-value: 9.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 ApRGELYKELQKSC--------TFDEQRTA----TIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH 224
Cdd:PRK13184  84 I-EGYTLKSLLKSVwqkeslskELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 ---------APSLRRKTMC-----------GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFEsashNETYRR 284
Cdd:PRK13184 163 kkleeedllDIDVDERNICyssmtipgkivGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYR----RKKGRK 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 927602445 285 IVKVD-LKFPASV------PMGAQDLISKLLRHNPSER 315
Cdd:PRK13184 239 ISYRDvILSPIEVapyreiPPFLSQIAMKALAVDPAER 276
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
76-316 1.07e-17

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 82.40  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIE-KEGVEHQLRREIEIQ--AHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmKQGETLALNERIMLSlvSTGDCPFIVCMSYAFHTPDKLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT 232
Cdd:cd14223   81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIE-GRMHNEKVDLWCIGVLCYELLVGNPPF---ESASHNETYRRIVKVDLKFPASVPMGAQDLISKLL 308
Cdd:cd14223  161 SVGTHGYMAPEVLQkGVAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTMAVELPDSFSPELRSLLEGLL 240

                 ....*...
gi 927602445 309 RHNPSERL 316
Cdd:cd14223  241 QRDVNRRL 248
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
81-273 1.14e-17

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


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 82.38  E-value: 1.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY--AP 158
Cdd:cd06634   21 REIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYclGS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG-WSVHAPSlrrKTMCGTL 237
Cdd:cd06634  101 ASDLLEVHKKP--LQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGsASIMAPA---NSFVGTP 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 927602445 238 DYLPPEMI----EGRmHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd06634  176 YWMAPEVIlamdEGQ-YDGKVDVWSLGITCIELAERKPPL 214
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
83-323 1.71e-17

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 81.24  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKVLFKSQIEK-EGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14146    2 IGVGGFGKVYRATWKGQE--VAVKAARQDPDEDiKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKSCTFDEQRTATIME---------ELADALMYCHGKKV---IHRDIKPENLLLGLK--------GELKIADFGW 221
Cdd:cd14146   80 LNRALAAANAAPGPRRARRIPphilvnwavQIARGMLYLHEEAVvpiLHRDLKSSNILLLEKiehddicnKTLKITDFGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 222 SVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPASVPMG 299
Cdd:cd14146  160 AREWHRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAvnKLTLPIPSTCPEP 239
                        250       260
                 ....*....|....*....|....*...
gi 927602445 300 AQDLISKLLRHNPSER----LPLAQVSA 323
Cdd:cd14146  240 FAKLMKECWEQDPHIRpsfaLILEQLTA 267
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
75-283 2.53e-17

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 81.21  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLA------REKKSHFI-VALKVLFKSQIEKEGVEhqLRREIEIQAHL-HHPNILRLYNYFYD 146
Cdd:cd05098   13 DRLVLGKPLGEGCFGQVVLAeaigldKDKPNRVTkVAVKMLKSDATEKDLSD--LISEMEMMKMIgKHKNIINLLGACTQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 147 RRRIYLILEYAPRGELYKELQ------------KSCTFDEQRT----ATIMEELADALMYCHGKKVIHRDIKPENLLLGL 210
Cdd:cd05098   91 DGPLYVIVEYASKGNLREYLQarrppgmeycynPSHNPEEQLSskdlVSCAYQVARGMEYLASKKCIHRDLAARNVLVTE 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 211 KGELKIADFGWS--VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYR 283
Cdd:cd05098  171 DNVMKIADFGLArdIHHIDYYKKTTNGRLpvKWMAPEALFDRIYTHQSDVWSFGVLLWEIFtLGGSPYPGVPVEELFK 248
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
83-315 2.72e-17

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 80.18  E-value: 2.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKV----LFKSQIEKegvehqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAP 158
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTcretLPPDLKRK------FLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKELQKSCtfDEQRTATIMEELADA---LMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS------VHAPSLR 229
Cdd:cd05041   77 GGSLLTFLRKKG--ARLTVKQLLQMCLDAaagMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSreeedgEYTVSDG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMcgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETyRRIVKVDLKFPAsvPMGAQDLISKLL 308
Cdd:cd05041  155 LKQI--PIKWTAPEALNYGRYTSESDVWSFGILLWEIFsLGATPYPGMSNQQT-REQIESGYRMPA--PELCPEAVYRLM 229
                        250
                 ....*....|.
gi 927602445 309 RH----NPSER 315
Cdd:cd05041  230 LQcwayDPENR 240
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
75-272 3.61e-17

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 81.25  E-value: 3.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksQIE-KEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLI---HLEiKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT 232
Cdd:cd06649   82 MEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPP 272
Cdd:cd06649  162 FVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYP 201
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
82-321 4.42e-17

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 80.01  E-value: 4.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  82 PLGKGKFGNVYLAREKKShfIVALKVLFKSQiekegvEHQLRREIEI--QAHLHHPNILRlynyFY--DRR------RIY 151
Cdd:cd14056    2 TIGKGRYGEVWLGKYRGE--KVAVKIFSSRD------EDSWFRETEIyqTVMLRHENILG----FIaaDIKstgswtQLW 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKsCTFDEQRTATIMEELADALMYCH-------GKKVI-HRDIKPENLLLGLKGELKIADFGWSV 223
Cdd:cd14056   70 LITEYHEHGSLYDYLQR-NTLDTEEALRLAYSAASGLAHLHteivgtqGKPAIaHRDLKSKNILVKRDGTCCIADLGLAV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKT------MCGTLDYLPPEMIEGRMHNE------KVDLWCIGVLCYELL----VGN------PPFESASHN-- 279
Cdd:cd14056  149 RYDSDTNTIdippnpRVGTKRYMAPEVLDDSINPKsfesfkMADIYSFGLVLWEIArrceIGGiaeeyqLPYFGMVPSdp 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 927602445 280 --ETYRRIVKVDLKFPA------SVPMGAQdlISKLLR----HNPSERLPLAQV 321
Cdd:cd14056  229 sfEEMRKVVCVEKLRPPipnrwkSDPVLRS--MVKLMQecwsENPHARLTALRV 280
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
83-288 5.10e-17

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


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 80.08  E-value: 5.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLARE-KKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLH---HPNILRLYNYFYDRR-----RIYLI 153
Cdd:cd07862    9 IGEGAYGKVFKARDlKNGGRFVALKRV-RVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVSRtdretKLTLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRgELYKELQKSCT--FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-VHAPSLRR 230
Cdd:cd07862   88 FEHVDQ-DLTTYLDKVPEpgVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLArIYSFQMAL 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV 288
Cdd:cd07862  167 TSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDV 224
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
83-328 6.00e-17

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


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 79.79  E-value: 6.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIE-KEGVEHQLRREIEIQA---HLHHPNILRLYNYFYDRRRIYLILEYAP 158
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmKQGETLALNERIMLSLvstGGDCPFIVCMTYAFQTPDKLCFILDLMN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLD 238
Cdd:cd05606   82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHASVGTHG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 239 YLPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPFESAS---HNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSE 314
Cdd:cd05606  162 YMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKtkdKHEIDRMTLTMNVELPDSFSPELKSLLEGLLQRDVSK 241
                        250
                 ....*....|....*....
gi 927602445 315 RL-----PLAQVSAHPWVR 328
Cdd:cd05606  242 RLgclgrGATEVKEHPFFK 260
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
75-327 6.46e-17

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 80.43  E-value: 6.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqiekEGVEHQ---LR--REIEIQAHLHHPNILRLYNY-----F 144
Cdd:cd07849    5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKI-------SPFEHQtycLRtlREIKILLRFKHENIIGILDIqrpptF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 145 YDRRRIYLILEYAPRgELYKeLQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-V 223
Cdd:cd07849   78 ESFKDVYIVQELMET-DLYK-LIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLArI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTM----CGTLDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFE---------------SASHNETYR 283
Cdd:cd07849  156 ADPEHDHTGFlteyVATRWYRAPEiMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPgkdylhqlnlilgilGTPSQEDLN 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 284 RIVKV-------DLKFPASVPMG---------AQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07849  236 CIISLkarnyikSLPFKPKVPWNklfpnadpkALDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
77-273 1.25e-16

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 79.25  E-value: 1.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHF--IVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYD--RRRIYL 152
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAKRKNGKDgkEYAIKKFKGDKEQYTGISQSACREIALLRELKHENVVSLVEVFLEhaDKSVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRgELYKELQ-----KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWS- 222
Cdd:cd07842   82 LFDYAEH-DLWQIIKfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANilvmGEGPERGVVKIGDLGLAr 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 223 -VHAPSlrrKTMCG------TLDYLPPEMIEGRMHNEK-VDLWCIGVLCYELLVGNPPF 273
Cdd:cd07842  161 lFNAPL---KPLADldpvvvTIWYRAPELLLGARHYTKaIDIWAIGCIFAELLTLEPIF 216
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
80-321 1.30e-16

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 78.12  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLA--REKKShfiVALKVLfksqieKEGVEHQLR----REIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05085    1 GELLGKGNFGEVYKGtlKDKTP---VAVKTC------KEDLPQELKikflSEARILKQYDHPNIVKLIGVCTQRQPIYIV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCtfDEQRTATIMEELADA---LMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS------VH 224
Cdd:cd05085   72 MELVPGGDFLSFLRKKK--DELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSrqeddgVY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTmcgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESAShNETYRRivKVDLKFPASVPMGAQDL 303
Cdd:cd05085  150 SSSGLKQI---PIKWTAPEALNYGRYSSESDVWSFGILLWETFsLGVCPYPGMT-NQQARE--QVEKGYRMSAPQRCPED 223
                        250       260
                 ....*....|....*....|..
gi 927602445 304 ISKLLR----HNPSERLPLAQV 321
Cdd:cd05085  224 IYKIMQrcwdYNPENRPKFSEL 245
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
83-274 1.41e-16

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 78.20  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKVLFKSQIEKEGV-EHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14061    2 IGVGGFGKVYRGIWRGEE--VAVKAARQDPDEDISVtLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKScTFDEQRTATIMEELADALMYCHGKK---VIHRDIK--------PENLLLGLKGELKIADFGWSVHAPSLRR 230
Cdd:cd14061   80 LNRVLAGR-KIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKssnilileAIENEDLENKTLKITDFGLAREWHKTTR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFE 274
Cdd:cd14061  159 MSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYK 202
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
75-321 1.48e-16

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 78.89  E-value: 1.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHL-HHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05088    7 NDIKFQDVIGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKS----------------CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA 217
Cdd:cd05088   87 IEYAPHGNLLDFLRKSrvletdpafaianstaSTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 218 DFGWSVHAPSLRRKTMcGTLD--YLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRrivKVDLKFPA 294
Cdd:cd05088  167 DFGLSRGQEVYVKKTM-GRLPvrWMAIESLNYSVYTTNSDVWSYGVLLWEIVsLGGTPYCGMTCAELYE---KLPQGYRL 242
                        250       260       270
                 ....*....|....*....|....*....|.
gi 927602445 295 SVPMGAQDLISKLL----RHNPSERLPLAQV 321
Cdd:cd05088  243 EKPLNCDDEVYDLMrqcwREKPYERPSFAQI 273
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
83-274 1.62e-16

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 78.52  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAR----EKKSHFIVALKVLfksqieKEGVEHQLR---REIEIQAHLHHPNILRLYNYFYD--RRRIYLI 153
Cdd:cd14205   12 LGKGNFGSVEMCRydplQDNTGEVVAVKKL------QHSTEEHLRdfeREIEILKSLQHDNIVKYKGVCYSagRRNLRLI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP------ 226
Cdd:cd14205   86 MEYLPYGSLRDYLQKHKErIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPqdkeyy 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 927602445 227 SLRRKTMCGTLDYLPPEMIEGRMhNEKVDLWCIGVLCYELLV-----GNPPFE 274
Cdd:cd14205  166 KVKEPGESPIFWYAPESLTESKF-SVASDVWSFGVVLYELFTyieksKSPPAE 217
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
71-323 1.62e-16

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 78.47  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEIGRPLGKGKFGNVYLAR-----EKKSHFIVALKVLFKSQiekEGVEHQLRREIEIQAHLHHPNILRLYNYFY 145
Cdd:cd05092    1 HIKRRDIVLKWELGEGAFGKVFLAEchnllPEQDKMLVAVKALKEAT---ESARQDFQREAELLTVLQHQHIVRFYGVCT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGELYKELQK----SCTFDEQRTAT-----------IMEELADALMYCHGKKVIHRDIKPENLLLGL 210
Cdd:cd05092   78 EGEPLIMVFEYMRHGDLNRFLRShgpdAKILDGGEGQApgqltlgqmlqIASQIASGMVYLASLHFVHRDLATRNCLVGQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 211 KGELKIADFGWS--VHAPSLRR---KTMCgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRR 284
Cdd:cd05092  158 GLVVKIGDFGMSrdIYSTDYYRvggRTML-PIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIEC 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 927602445 285 IVK-VDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSA 323
Cdd:cd05092  237 ITQgRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHS 276
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
134-326 1.87e-16

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 77.77  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 134 HPNILRLYNYFYDRRRIYLILEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKP-----ENLLL 208
Cdd:cd14022   44 HSNINQITEIILGETKAYVFFERS-YGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLrkfvfKDEER 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 209 GLKGELKIAD-FGWSVHAPSLRRKTMCGTldYLPPEMI--EGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRI 285
Cdd:cd14022  123 TRVKLESLEDaYILRGHDDSLSDKHGCPA--YVSPEILntSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 927602445 286 VKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14022  201 RRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 241
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
72-283 2.31e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 78.47  E-value: 2.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLA------REKKSHFI-VALKVLFKSQIEKEGVEhqLRREIEIQAHL-HHPNILRLYNY 143
Cdd:cd05099    9 FPRDRLVLGKPLGEGCFGQVVRAeaygidKSRPDQTVtVAVKMLKDNATDKDLAD--LISEMELMKLIgKHKNIINLLGV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 144 FYDRRRIYLILEYAPRGELYKELQK------SCTFDEQRT----------ATIMEELADALMYCHGKKVIHRDIKPENLL 207
Cdd:cd05099   87 CTQEGPLYVIVEYAAKGNLREFLRArrppgpDYTFDITKVpeeqlsfkdlVSCAYQVARGMEYLESRRCIHRDLAARNVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 208 LGLKGELKIADFGWS--VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETY 282
Cdd:cd05099  167 VTEDNVMKIADFGLArgVHDIDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILMWEIFtLGGSPYPGIPVEELF 246

                 .
gi 927602445 283 R 283
Cdd:cd05099  247 K 247
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
78-315 4.20e-16

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: 77.55  E-value: 4.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRpLGKGKFGNVYLAREKKSHFIVALK-VLFKSQIEKEGVEHQlrREIEIQAHLHHPNILRLYNYFYDRRRIYL---- 152
Cdd:cd14049   10 EIAR-LGKGGYGKVYKVRNKLDGQYYAIKkILIKKVTKRDCMKVL--REVKVLAGLQHPNIVGYHTAWMEHVQLMLyiqm 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ----------ILEYAPRGELYKELQKSCTF-DEQRTATIMEELADALMYCHGKKVIHRDIKPENL-LLGLKGELKIADFG 220
Cdd:cd14049   87 qlcelslwdwIVERNKRPCEEEFKSAPYTPvDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIfLHGSDIHVRIGDFG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 ------------WSVHAP--SLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVgnpPFESashnETYRRIV 286
Cdd:cd14049  167 lacpdilqdgndSTTMSRlnGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELFQ---PFGT----EMERAEV 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 927602445 287 KVDLK---FPASV----PMGAQdLISKLLRHNPSER 315
Cdd:cd14049  240 LTQLRngqIPKSLckrwPVQAK-YIKLLTSTEPSER 274
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
75-294 4.94e-16

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 77.80  E-value: 4.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEI-GRPLGKGKFGNVYLAREK--KSHFIVALKvlfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYF--YDRRR 149
Cdd:cd07867    1 DLFEYeGCKVGRGTYGHVYKAKRKdgKDEKEYALK-----QIEGTGISMSACREIALLRELKHPNVIALQKVFlsHSDRK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELY--------KELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLG----LKGELKIA 217
Cdd:cd07867   76 VWLLFDYAEHDLWHiikfhrasKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 218 DFGW-----SVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEK-VDLWCIGVLCYELLVGNPPFESAS---------HNETY 282
Cdd:cd07867  156 DMGFarlfnSPLKPLADLDPVVVTFWYRAPELLLGARHYTKaIDIWAIGCIFAELLTSEPIFHCRQediktsnpfHHDQL 235
                        250
                 ....*....|..
gi 927602445 283 RRIVKVdLKFPA 294
Cdd:cd07867  236 DRIFSV-MGFPA 246
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
81-285 5.18e-16

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 76.82  E-value: 5.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLArEKKSHFIVALKVLfksqieKEGV--EHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAP 158
Cdd:cd05114   10 KELGSGLFGVVRLG-KWRAQYKVAIKAI------REGAmsEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGT- 236
Cdd:cd05114   83 NGCLLNYLrQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAk 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 237 --LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRI 285
Cdd:cd05114  163 fpVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMV 214
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
71-321 5.64e-16

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 76.91  E-value: 5.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEigrpLGKGKFGNVY--LAREKKSHFIVALKVLfKSQIEKeGVEHQLRREIEIQAHLHHPNILRLYNyFYDRR 148
Cdd:cd05115    4 NLLIDEVE----LGSGNFGCVKkgVYKMRKKQIDVAIKVL-KQGNEK-AVRDEMMREAQIMHQLDNPYIVRMIG-VCEAE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 RIYLILEYAPRGELYKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VHA 225
Cdd:cd05115   77 ALMLVMEMASGGPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSkaLGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCG---TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVD-LKFPASVPMGA 300
Cdd:cd05115  157 DDSYYKARSAgkwPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFsYGQKPYKKMKGPEVMSFIEQGKrMDCPAECPPEM 236
                        250       260
                 ....*....|....*....|.
gi 927602445 301 QDLISKLLRHNPSERLPLAQV 321
Cdd:cd05115  237 YALMSDCWIYKWEDRPNFLTV 257
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
81-321 6.14e-16

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 76.66  E-value: 6.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLA-----REKKSHFIVALKVLfkSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05036   12 RALGQGAFGEVYEGtvsgmPGDPSPLQVAVKTL--PELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEEL-------ADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWS--V 223
Cdd:cd05036   90 LMAGGDLKSFLRENRPRPEQPSSLTMLDLlqlaqdvAKGCRYLEENHFIHRDIAARNcllTCKGPGRVAKIGDFGMArdI 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVD-LKFPASVPMG 299
Cdd:cd05036  170 YRADYYRKGGKAMLpvKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFsLGYMPYPGKSNQEVMEFVTSGGrMDPPKNCPGP 249
                        250       260
                 ....*....|....*....|..
gi 927602445 300 AQDLISKLLRHNPSERLPLAQV 321
Cdd:cd05036  250 VYRIMTQCWQHIPEDRPNFSTI 271
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
72-271 6.86e-16

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 77.07  E-value: 6.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLA--------REKKShfIVALKVLFKSQIEKEGVEhqLRREIEIQAHL-HHPNILRLYN 142
Cdd:cd05053    9 LPRDRLTLGKPLGEGAFGQVVKAeavgldnkPNEVV--TVAVKMLKDDATEKDLSD--LVSEMEMMKMIgKHKNIINLLG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 143 YFYDRRRIYLILEYAPRGELYKELQKS------CTFDEQRTAT-------IME---ELADALMYCHGKKVIHRDIKPENL 206
Cdd:cd05053   85 ACTQDGPLYVVVEYASKGNLREFLRARrppgeeASPDDPRVPEeqltqkdLVSfayQVARGMEYLASKKCIHRDLAARNV 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 207 LLGLKGELKIADFGWS--VHAPSLRRKTMCGTLDY--LPPEMIEGRMHNEKVDLWCIGVLCYEL--LVGNP 271
Cdd:cd05053  165 LVTEDNVMKIADFGLArdIHHIDYYRKTTNGRLPVkwMAPEALFDRVYTHQSDVWSFGVLLWEIftLGGSP 235
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
75-321 7.62e-16

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 76.61  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVY--LAR--EKKSHFI-VALKVLFKSQIEKEgvehqlRREIEIQA----HLHHPNILRLYNYFY 145
Cdd:cd05032    6 EKITLIRELGQGSFGMVYegLAKgvVKGEPETrVAIKTVNENASMRE------RIEFLNEAsvmkEFNCHHVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGELyKELQKSCTFDEQRTATIME-----------ELADALMYCHGKKVIHRDIKPENLLLGLKGEL 214
Cdd:cd05032   80 TGQPTLVVMELMAKGDL-KSYLRSRRPEAENNPGLGPptlqkfiqmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 215 KIADFGWS--VHAPSLRRKTMCGTLD--YLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVD 289
Cdd:cd05032  159 KIGDFGMTrdIYETDYYRKGGKGLLPvrWMAPESLKDGVFTTKSDVWSFGVVLWEMAtLAEQPYQGLSNEEVLKFVIDGG 238
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 290 -LKFPASVPMGAQDLISKLLRHNPSERLPLAQV 321
Cdd:cd05032  239 hLDLPENCPDKLLELMRMCWQYNPKMRPTFLEI 271
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
83-321 1.02e-15

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 75.77  E-value: 1.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVY--LAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNyFYDRRRIYLILEYAPRG 160
Cdd:cd05116    3 LGSGNFGTVKkgYYQMKKVVKTVAVKIL-KNEANDPALKDELLREANVMQQLDNPYIVRMIG-ICEAESWMLVMEMAELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGT---- 236
Cdd:cd05116   81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADENYYKAQThgkw 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 -LDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVD-LKFPASVPMGAQDLISKLLRHNPS 313
Cdd:cd05116  161 pVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFsYGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCWTYDVD 240

                 ....*...
gi 927602445 314 ERLPLAQV 321
Cdd:cd05116  241 ERPGFAAV 248
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
75-315 1.22e-15

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 75.76  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLArekksHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05112    4 SELTFVQEIGSGQFGLVHLG-----YWLNKDKVAIKTIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTM 233
Cdd:cd05112   79 EFMEHGCLSDYLRtQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGT---LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIvkvDLKFPASVPMGAQDLISKLLR 309
Cdd:cd05112  159 TGTkfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDI---NAGFRLYKPRLASTHVYEIMN 235

                 ....*.
gi 927602445 310 HNPSER 315
Cdd:cd05112  236 HCWKER 241
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
71-327 1.23e-15

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: 76.43  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDD-----FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqIEKEGVEHQLRREIEIQAHL------HHPNILR 139
Cdd:cd14210    4 KVVLGDhiayrYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII----RNKKRFHQQALVEVKILKHLndndpdDKHNIVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 140 LYNYFYDRRRIYLILEYAPRgELYkELQKSCTF-----DEQRTATImeELADALMYCHGKKVIHRDIKPENLLLGLKGEL 214
Cdd:cd14210   80 YKDSFIFRGHLCIVFELLSI-NLY-ELLKSNNFqglslSLIRKFAK--QILQALQFLHKLNIIHCDLKPENILLKQPSKS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 215 KIA--DFGWS--VHAPSL-----RRktmcgtldYLPPEMIEGRMHNEKVDLWCIG-VLCyELLVGNPPFESAshNET--- 281
Cdd:cd14210  156 SIKviDFGSScfEGEKVYtyiqsRF--------YRAPEVILGLPYDTAIDMWSLGcILA-ELYTGYPLFPGE--NEEeql 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 282 ----------------------------------------YRRIVKVDLKFPASV-PMGAQDLISKLLRHNPSERLPLAQ 320
Cdd:cd14210  225 acimevlgvppkslidkasrrkkffdsngkprpttnskgkKRRPGSKSLAQVLKCdDPSFLDFLKKCLRWDPSERMTPEE 304

                 ....*..
gi 927602445 321 VSAHPWV 327
Cdd:cd14210  305 ALQHPWI 311
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
77-315 1.69e-15

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 75.72  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNV---YLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRR---RI 150
Cdd:cd05074   11 FTLGRMLGKGEFGSVreaQLKSEDGSFQKVAVKML-KADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRSRakgRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 ---YLILEYAPRGELYKELQKSCTFDE------QRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW 221
Cdd:cd05074   90 pipMVILPFMKHGDLHTFLLMSRIGEEpftlplQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 222 S--VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKVD-LKFPAS 295
Cdd:cd05074  170 SkkIYSGDYYRQGCASKLpvKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNYLIKGNrLKQPPD 249
                        250       260
                 ....*....|....*....|
gi 927602445 296 VPMGAQDLISKLLRHNPSER 315
Cdd:cd05074  250 CLEDVYELMCQCWSPEPKCR 269
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
71-316 1.75e-15

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 75.58  E-value: 1.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEIGRPLGKGKFGNVYLAR-----EKKSHFIVALKVLfksqieKEGVEHQLR----REIEIQAHLHHPNILRLY 141
Cdd:cd05049    1 HIKRDTIVLKRELGEGAFGKVFLGEcynlePEQDKMLVAVKTL------KDASSPDARkdfeREAELLTNLQHENIVKFY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 142 NYFYDRRRIYLILEYAPRGELYKEL--------------QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL 207
Cdd:cd05049   75 GVCTEGDPLLMVFEYMEHGDLNKFLrshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 208 LGLKGELKIADFGWS--VHAPSLRR---KTMCgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNET 281
Cdd:cd05049  155 VGTNLVVKIGDFGMSrdIYSTDYYRvggHTML-PIRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTEV 233
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 927602445 282 YRRIVK-VDLKFPASVPMGAQDLISKLLRHNPSERL 316
Cdd:cd05049  234 IECITQgRLLQRPRTCPSEVYAVMLGCWKREPQQRL 269
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
81-315 1.82e-15

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


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 75.01  E-value: 1.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKsHFIVALKVLFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd05034    1 KKLGAGQFGEVWMGVWNG-TTKVAVKTLKPGTMSPE----AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKsctfDEQRTATI------MEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsvhapsLRRKTMC 234
Cdd:cd05034   76 SLLDYLRT----GEGRALRLpqlidmAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFG-------LARLIED 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTldYLP------------PEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETyrrIVKVDLKFPASVPMGAQ 301
Cdd:cd05034  145 DE--YTAregakfpikwtaPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREV---LEQVERGYRMPKPPGCP 219
                        250
                 ....*....|....*...
gi 927602445 302 DLISKLL----RHNPSER 315
Cdd:cd05034  220 DELYDIMlqcwKKEPEER 237
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
75-273 2.08e-15

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


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 75.50  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSqiEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQ--EEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYApRGELYKELQK-SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRK 231
Cdd:cd07869   83 EYV-HTDLCQYMDKhPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLarAKSVPSHTYS 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 927602445 232 TMCGTLDYLPPEMIEGRM-HNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd07869  162 NEVVTLWYRPPDVLLGSTeYSTCLDMWGVGCIFVEMIQGVAAF 204
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
71-321 2.11e-15

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 75.46  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEIGRPLGKGKFGNVYLAR-----EKKSHFIVALKVLFKSQiekEGVEHQLRREIEIQAHLHHPNILRLYNYFY 145
Cdd:cd05093    1 HIKRHNIVLKRELGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDAS---DNARKDFHREAELLTNLQHEHIVKFYGVCV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGELYKEL-------------QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKG 212
Cdd:cd05093   78 EGDPLIMVFEYMKHGDLNKFLrahgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 213 ELKIADFGWSVHAPSLRRKTMCG----TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK 287
Cdd:cd05093  158 LVKIGDFGMSRDVYSTDYYRVGGhtmlPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQ 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 288 VD-LKFPASVPMGAQDLISKLLRHNPSERLPLAQV 321
Cdd:cd05093  238 GRvLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEI 272
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
79-321 2.36e-15

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 75.24  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgveHQLRREIEIQAHLH-HPNILRLYNYFYDRRRI------- 150
Cdd:cd14036    4 IKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKN---KAIIQEINFMKKLSgHPNIVQFCSAASIGKEEsdqgqae 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGEL---YKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKGELKIADFG----- 220
Cdd:cd14036   81 YLLLTELCKGQLvdfVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGsatte 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 -------WSVHAPSL-----RRKTmcgTLDYLPPEMIEGRMH---NEKVDLWCIGVLCYELLVGNPPFESASHnetyRRI 285
Cdd:cd14036  161 ahypdysWSAQKRSLvedeiTRNT---TPMYRTPEMIDLYSNypiGEKQDIWALGCILYLLCFRKHPFEDGAK----LRI 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 927602445 286 VKVDLKFPasvPMGAQ-----DLISKLLRHNPSERLPLAQV 321
Cdd:cd14036  234 INAKYTIP---PNDTQytvfhDLIRSTLKVNPEERLSITEI 271
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
77-275 2.58e-15

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 75.14  E-value: 2.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYlarekKSHFI---------VALKVLFKSQIEKEGVEhqLRREIEIQAHLHHPNILRLYNYFYDR 147
Cdd:cd05057    9 LEKGKVLGSGAFGTVY-----KGVWIpegekvkipVAIKVLREETGPKANEE--ILDEAYVMASVDHPHLVRLLGICLSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RrIYLILEYAPRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG----WS 222
Cdd:cd05057   82 Q-VQLITQLMPLGCLLDYVrNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGlaklLD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 927602445 223 VHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFES 275
Cdd:cd05057  161 VDEKEYHAEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEG 214
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
83-321 3.14e-15

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 74.69  E-value: 3.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKVLFKSQIE--KEGVEHqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd14145   14 IGIGGFGKVYRAIWIGDE--VAVKAARHDPDEdiSQTIEN-VRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQ-KSCTFDEQRTATImeELADALMYCHGKK---VIHRDIKPENLLLGLK--------GELKIADFGWSVHAPSL 228
Cdd:cd14145   91 PLNRVLSgKRIPPDILVNWAV--QIARGMNYLHCEAivpVIHRDLKSSNILILEKvengdlsnKILKITDFGLAREWHRT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPASVPMGAQDLISK 306
Cdd:cd14145  169 TKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAmnKLSLPIPSTCPEPFARLMED 248
                        250
                 ....*....|....*
gi 927602445 307 LLRHNPSERLPLAQV 321
Cdd:cd14145  249 CWNPDPHSRPPFTNI 263
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
75-294 3.33e-15

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 75.48  E-value: 3.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEI-GRPLGKGKFGNVYLAREK--KSHFIVALKvlfksQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDR--RR 149
Cdd:cd07868   16 DLFEYeGCKVGRGTYGHVYKAKRKdgKDDKDYALK-----QIEGTGISMSACREIALLRELKHPNVISLQKVFLSHadRK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELY--------KELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLG----LKGELKIA 217
Cdd:cd07868   91 VWLLFDYAEHDLWHiikfhrasKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 218 DFGW-----SVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEK-VDLWCIGVLCYELLVGNPPFE---------SASHNETY 282
Cdd:cd07868  171 DMGFarlfnSPLKPLADLDPVVVTFWYRAPELLLGARHYTKaIDIWAIGCIFAELLTSEPIFHcrqediktsNPYHHDQL 250
                        250
                 ....*....|..
gi 927602445 283 RRIVKVdLKFPA 294
Cdd:cd07868  251 DRIFNV-MGFPA 261
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
72-326 4.05e-15

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 75.09  E-value: 4.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDD-FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRrEIEIQAHLHHPNILRLYNYFY----- 145
Cdd:cd07855    1 FDVGDrYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLR-ELKILRHFKHDNIIAIRDILRpkvpy 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 -DRRRIYLILEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-- 222
Cdd:cd07855   80 aDFKDVYVVLDLM-ESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMArg 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRRKTM----CGTLDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV--------- 288
Cdd:cd07855  159 LCTSPEEHKYFmteyVATRWYRAPElMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVlgtpsqavi 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927602445 289 ------------------------DLKFPASVPmgAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07855  239 naigadrvrryiqnlpnkqpvpweTLYPKADQQ--ALDLLSQMLRFDPSERITVAEALQHPF 298
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
83-321 4.31e-15

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


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 74.30  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKShfIVALKVLFKSQIEKEGVEHQ-LRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGE 161
Cdd:cd14147   11 IGIGGFGKVYRGSWRGE--LVAVKAARQDPDEDISVTAEsVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKELQKScTFDEQRTATIMEELADALMYCHGKK---VIHRDIKPENLLLGLK--------GELKIADFGWSVHAPSLRR 230
Cdd:cd14147   89 LSRALAGR-RVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPienddmehKTLKITDFGLAREWHKTTQ 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIV--KVDLKFPASVPMGAQDLISKLL 308
Cdd:cd14147  168 MSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAvnKLTLPIPSTCPEPFAQLMADCW 247
                        250
                 ....*....|...
gi 927602445 309 RHNPSERLPLAQV 321
Cdd:cd14147  248 AQDPHRRPDFASI 260
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
83-326 4.69e-15

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 74.37  E-value: 4.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKeGVEHQLRREIEIQAHLHHPNILRLYNYFYD----RRRIYLILEYAP 158
Cdd:cd14031   18 LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTK-AEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELMT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKG-ELKIADFGWSVHAPSLRRKTMCG 235
Cdd:cd14031   97 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLMRTSFAKSVIG 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 236 TLDYLPPEMIEgRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKfPAS----VPMGAQDLISKLLRHN 311
Cdd:cd14031  177 TPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIK-PASfnkvTDPEVKEIIEGCIRQN 254
                        250
                 ....*....|....*
gi 927602445 312 PSERLPLAQVSAHPW 326
Cdd:cd14031  255 KSERLSIKDLLNHAF 269
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
75-323 4.74e-15

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 74.33  E-value: 4.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEI-------GRPLGKGKFGNVYlarEKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILrLYNYFYDR 147
Cdd:cd14151    1 DDWEIpdgqitvGQRIGSGSFGTVY---KGKWHGDVAVKMLNVTAPTPQQLQ-AFKNEVGVLRKTRHVNIL-LFMGYSTK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------ 220
Cdd:cd14151   76 PQLAIVTQWCEGSSLYHHLHIIETkFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGlatvks 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 -WSvhaPSLRRKTMCGTLDYLPPEMIEGRMHNE---KVDLWCIGVLCYELLVGNPPFESASHNETY-----RRIVKVDL- 290
Cdd:cd14151  156 rWS---GSHQFEQLSGSILWMAPEVIRMQDKNPysfQSDVYAFGIVLYELMTGQLPYSNINNRDQIifmvgRGYLSPDLs 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 291 KFPASVPMGAQDLISKLLRHNPSERLPLAQVSA 323
Cdd:cd14151  233 KVRSNCPKAMKRLMAECLKKKRDERPLFPQILA 265
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
75-326 4.94e-15

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 74.49  E-value: 4.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHH-PNILRLYNYFY----DRRR 149
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKT-RLEMEEEGVPSTALREVSLLQMLSQsIYIVRLLDVEHveenGKPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYaprgeLYKELQK---------SCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLL-GLKGELKIADF 219
Cdd:cd07837   80 LYLVFEY-----LDTDLKKfidsygrgpHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVdKQKGLLKIADL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 220 G----WSVHAPSLRRKTMcgTLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV------ 288
Cdd:cd07837  155 GlgraFTIPIKSYTHEIV--TLWYRAPEVLLGSTHySTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLlgtpne 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 289 ---------------------DLK--FPASVPMGAqDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07837  233 evwpgvsklrdwheypqwkpqDLSraVPDLEPEGV-DLLTKMLAYDPAKRISAKAALQHPY 292
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
81-316 5.17e-15

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 74.44  E-value: 5.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHfiVALKVLFKSQiekegvEHQLRREIEI--QAHLHHPNILRLYNYfyDRR------RIYL 152
Cdd:cd14144    1 RSVGKGRYGEVWKGKWRGEK--VAVKIFFTTE------EASWFRETEIyqTVLMRHENILGFIAA--DIKgtgswtQLYL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKELQKScTFDEQRTATIMEELADALMYCH-------GKKVI-HRDIKPENLLLGLKGELKIADFGWSVH 224
Cdd:cd14144   71 ITDYHENGSLYDFLRGN-TLDTQSMLKLAYSAACGLAHLHteifgtqGKPAIaHRDIKSKNILVKKNGTCCIADLGLAVK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APS------LRRKTMCGTLDYLPPEMIEGRMHNEKVD-------------LWCIGVLC--------YELlvgnPPFESAS 277
Cdd:cd14144  150 FISetnevdLPPNTRVGTKRYMAPEVLDESLNRNHFDaykmadmysfglvLWEIARRCisggiveeYQL----PYYDAVP 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 927602445 278 HNETY---RRIVKVDlKFPASVPMGAQD-----LISKLLR----HNPSERL 316
Cdd:cd14144  226 SDPSYedmRRVVCVE-RRRPSIPNRWSSdevlrTMSKLMSecwaHNPAARL 275
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
83-322 6.09e-15

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 73.54  E-value: 6.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLA--REKKSHFI-VALKVLFKSQIEkeGVEHQLRREIEIQAHLHHPNILRLYNyFYDRRRIYLILEYAPR 159
Cdd:cd05060    3 LGHGNFGSVRKGvyLMKSGKEVeVAVKTLKQEHEK--AGKKEFLREASVMAQLDHPCIVRLIG-VCKGEPLMLVMELAPL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvhaPSLR------RKTM 233
Cdd:cd05060   80 GPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMS---RALGagsdyyRATT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 234 CGT--LDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETyrrIVKVD----LKFPASVPMGAQDLISK 306
Cdd:cd05060  157 AGRwpLKWYAPECINYGKFSSKSDVWSYGVTLWEAFsYGAKPYGEMKGPEV---IAMLEsgerLPRPEECPQEIYSIMLS 233
                        250
                 ....*....|....*.
gi 927602445 307 LLRHNPSERLPLAQVS 322
Cdd:cd05060  234 CWKYRPEDRPTFSELE 249
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
83-315 6.45e-15

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 73.69  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKkSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14027    1 LDSGGFGKVSLCFHR-TQGLVVLKTVYTGPNCIEHNE-ALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQKsCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG------WSV----HAPSLRR-- 230
Cdd:cd14027   79 MHVLKK-VSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmWSKltkeEHNEQREvd 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 ---KTMCGTLDYLPPEMIE--GRMHNEKVDLWCIGVLCYELLVGNPPFESA-SHNETYRRIVK-----VDLkFPASVPMG 299
Cdd:cd14027  158 gtaKKNAGTLYYMAPEHLNdvNAKPTEKSDVYSFAIVLWAIFANKEPYENAiNEDQIIMCIKSgnrpdVDD-ITEYCPRE 236
                        250
                 ....*....|....*.
gi 927602445 300 AQDLISKLLRHNPSER 315
Cdd:cd14027  237 IIDLMKLCWEANPEAR 252
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
123-325 7.25e-15

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 73.46  E-value: 7.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 123 RREIE-IQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG--ELYKELQKSCTFDEQ--RTATIMEELADALMYCHGKKVI 197
Cdd:cd13982   42 DREVQlLRESDEHPNVIRYFCTEKDRQFLYIALELCAASlqDLVESPRESKLFLRPglEPVRLLRQIASGLAHLHSLNIV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 198 HRDIKPEN-----LLLGLKGELKIADFGWS----VHAPSLRRKT-MCGTLDYLPPEMIEGRMHNE---KVDLWCIGVLCY 264
Cdd:cd13982  122 HRDLKPQNilistPNAHGNVRAMISDFGLCkkldVGRSSFSRRSgVAGTSGWIAPEMLSGSTKRRqtrAVDIFSLGCVFY 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 265 ELLV-GNPPFESashneTYRR---IVKVDLKFPASVPMG-----AQDLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd13982  202 YVLSgGSHPFGD-----KLEReanILKGKYSLDKLLSLGehgpeAQDLIERMIDFDPEKRPSAEEVLNHP 266
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
81-287 7.36e-15

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 73.38  E-value: 7.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHfIVALKVLfksqieKEGV--EHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAP 158
Cdd:cd05113   10 KELGTGQFGVVKYGKWRGQY-DVAIKMI------KEGSmsEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 159 RGELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGT- 236
Cdd:cd05113   83 NGCLLNYLREMRKrFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSk 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 927602445 237 --LDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK 287
Cdd:cd05113  163 fpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYsLGKMPYERFTNSETVEHVSQ 216
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
77-326 9.32e-15

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 74.14  E-value: 9.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVehqlRREIEIQAHLHH------PNILRLYNYFYDRRRI 150
Cdd:cd14134   14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREAA----KIEIDVLETLAEkdpngkSHCVQLRDWFDYRGHM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILE-YAPrgELYKELQKSC--TFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN-------------------LLL 208
Cdd:cd14134   90 CIVFElLGP--SLYDFLKKNNygPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENillvdsdyvkvynpkkkrqIRV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 209 GLKGELKIADFG----WSVHapslrRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF----------- 273
Cdd:cd14134  168 PKSTDIKLIDFGsatfDDEY-----HSSIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFqthdnlehlam 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 274 ---------------------------------ESASHNETYRRIVKVDLKFPASVPMGAQ---DLISKLLRHNPSERLP 317
Cdd:cd14134  243 merilgplpkrmirrakkgakyfyfyhgrldwpEGSSSGRSIKRVCKPLKRLMLLVDPEHRllfDLIRKMLEYDPSKRIT 322

                 ....*....
gi 927602445 318 LAQVSAHPW 326
Cdd:cd14134  323 AKEALKHPF 331
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
72-283 1.09e-14

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 73.90  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLA------REKKSHFI-VALKVLFKSQIEKEGVEhqLRREIEIQAHL-HHPNILRLYNY 143
Cdd:cd05100    9 LSRTRLTLGKPLGEGCFGQVVMAeaigidKDKPNKPVtVAVKMLKDDATDKDLSD--LVSEMEMMKMIgKHKNIINLLGA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 144 FYDRRRIYLILEYAPRGELYKELQ-----------KSCTFDEQRTA-----TIMEELADALMYCHGKKVIHRDIKPENLL 207
Cdd:cd05100   87 CTQDGPLYVLVEYASKGNLREYLRarrppgmdysfDTCKLPEEQLTfkdlvSCAYQVARGMEYLASQKCIHRDLAARNVL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 208 LGLKGELKIADFGWS--VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETY 282
Cdd:cd05100  167 VTEDNVMKIADFGLArdVHNIDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLWEIFtLGGSPYPGIPVEELF 246

                 .
gi 927602445 283 R 283
Cdd:cd05100  247 K 247
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
80-315 1.09e-14

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 72.66  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  80 GRPLGKGKFGNVYLAREKKSHFIVALKvlfkSQIEKEGVEHQLR--REIEIQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd05084    1 GERIGRGNFGEVFSGRLRADNTPVAVK----SCRETLPPDLKAKflQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS------VHAPSLRR 230
Cdd:cd05084   77 QGGDFLTFLRtEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSreeedgVYAATGGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMcgTLDYLPPEMIE-GRMHNEKvDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK-VDLKFPASVPMGAQDLISKL 307
Cdd:cd05084  157 KQI--PVKWTAPEALNyGRYSSES-DVWSFGILLWETFsLGAVPYANLSNQQTREAVEQgVRLPCPENCPDEVYRLMEQC 233

                 ....*...
gi 927602445 308 LRHNPSER 315
Cdd:cd05084  234 WEYDPRKR 241
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
77-267 1.14e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 74.14  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVehQLRReieiqahLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKIGQKGTTLIEAM--LLQN-------VNHPSVIRMKDTLVSGAITCMVLPH 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 ApRGELYKELQKSCTFDEQRTA-TIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG---WSVHAPSLRrkT 232
Cdd:PHA03209 139 Y-SSDLYTYLTKRSRPLPIDQAlIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGaaqFPVVAPAFL--G 215
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:PHA03209 216 LAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
77-315 1.61e-14

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 72.57  E-value: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVY---LAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQaHLHHPNILRLYNYFY---DRRRI 150
Cdd:cd05035    1 LKLGKILGEGEFGSVMeaqLKQDDGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMK-DFDHPNVMRLIGVCFtasDLNKP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 ---YLILEYAPRGELYKELQKSCT------FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGW 221
Cdd:cd05035   80 pspMVILPFMKHGDLHSYLLYSRLgglpekLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 222 S--VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKVD-LKFPAS 295
Cdd:cd05035  160 SrkIYSGDYYRQGRISKMpvKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGNrLKQPED 239
                        250       260
                 ....*....|....*....|
gi 927602445 296 VPMGAQDLISKLLRHNPSER 315
Cdd:cd05035  240 CLDEVYFLMYFCWTVDPKDR 259
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
72-328 1.62e-14

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 72.79  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHH-PNILRLYNYFYDRRRI 150
Cdd:cd06618   12 ADLNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKEE--NKRILMDLDVVLKSHDcPYIVKCYGYFITDSDV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEY--APRGELYKELQKSctFDEQRTATIMEELADALMYC---HGkkVIHRDIKPENLLLGLKGELKIADFGWSVHA 225
Cdd:cd06618   90 FICMELmsTCLDKLLKRIQGP--IPEDILGKMTVSIVKALHYLkekHG--VIHRDVKPSNILLDESGNVKLCDFGISGRL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKT-MCGTLDYLPPEMIEGRMHNE---KVDLWCIGVLCYELLVGNPPFESASHN-ETYRRIVKVDlkfPASVPMGA 300
Cdd:cd06618  166 VDSKAKTrSAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILNEE---PPSLPPNE 242
                        250       260       270
                 ....*....|....*....|....*....|....
gi 927602445 301 ------QDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd06618  243 gfspdfCSFVDLCLTKDHRYRPKYRELLQHPFIR 276
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
83-267 2.26e-14

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 72.23  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREK----KSHFIVALKvlfksQIEKEGVEHQ--LRREIEIQAHLHHPNILRLYNYFYD--RRRIYLIL 154
Cdd:cd05081   12 LGKGNFGSVELCRYDplgdNTGALVAVK-----QLQHSGPDQQrdFQREIQILKALHSDFIVKYRGVSYGpgRRSLRLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKS-CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR---- 229
Cdd:cd05081   87 EYLPSGCLRDFLQRHrARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDKdyyv 166
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 927602445 230 -RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:cd05081  167 vREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELF 205
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
76-324 3.12e-14

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 71.57  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRplgkGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGvEHQLRREIEIQAHLHHPNILRLYNYFYDRRR----IY 151
Cdd:cd14033    6 NIEIGR----GSFKTVYRGLDTETTVEVAWCELQTRKLSKGE-RQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcII 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKsctFDEQRTATIME---ELADALMYCHGK--KVIHRDIKPENLLLG-LKGELKIADFGWSVHA 225
Cdd:cd14033   81 LVTELMTSGTLKTYLKR---FREMKLKLLQRwsrQILKGLHFLHSRcpPILHRDLKCDNIFITgPTGSVKIGDLGLATLK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 226 PSLRRKTMCGTLDYLPPEMIEGRmHNEKVDLWCIGVLCYELLVGNPPF-ESASHNETYRRI---VKVDLKFPASVPMgAQ 301
Cdd:cd14033  158 RASFAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYsECQNAAQIYRKVtsgIKPDSFYKVKVPE-LK 235
                        250       260
                 ....*....|....*....|...
gi 927602445 302 DLISKLLRHNPSERLPLAQVSAH 324
Cdd:cd14033  236 EIIEGCIRTDKDERFTIQDLLEH 258
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
83-323 3.32e-14

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 71.41  E-value: 3.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKShfIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNY-FYDRRRIYLILEYAPRGE 161
Cdd:cd14064    1 IGSGSFGKVYKGRCRNK--IVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQYVSGGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 162 LYKEL--QKScTFDEQRTATIMEELADALMYCHG--KKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMC--- 234
Cdd:cd14064   79 LFSLLheQKR-VIDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTkqp 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPFE-----SASHNETYRRIVKvdlKFPASVPMGAQDLISKLL 308
Cdd:cd14064  158 GNLRWMAPEVFtQCTRYSIKADVFSYALCLWELLTGEIPFAhlkpaAAAADMAYHHIRP---PIGYSIPKPISSLLMRGW 234
                        250
                 ....*....|....*
gi 927602445 309 RHNPSERLPLAQVSA 323
Cdd:cd14064  235 NAEPESRPSFVEIVA 249
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
81-328 3.34e-14

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 72.45  E-value: 3.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVEHQLR--REIEIQAHLHHPNILRLYNYFY------DRRRIYL 152
Cdd:cd07850    6 KPIGSGAQGIVCAAYDTVTGQNVAIK---KLSRPFQNVTHAKRayRELVLMKLVNHKNIIGLLNVFTpqksleEFQDVYL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPrGELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA-PSLRRK 231
Cdd:cd07850   83 VMELMD-ANLCQVIQMD--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAgTSFMMT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV----------------------- 288
Cdd:cd07850  160 PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQlgtpsdefmsrlqptvrnyvenr 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 289 -------------DLKFPASV-------PMGAQDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd07850  240 pkyagysfeelfpDVLFPPDSeehnklkASQARDLLSKMLVIDPEKRISVDDALQHPYIN 299
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
71-321 3.71e-14

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 71.97  E-value: 3.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEIGRPLGKGKFGNVYLAR-----EKKSHFIVALKVLFKSQIekeGVEHQLRREIEIQAHLHHPNILRLYNYFY 145
Cdd:cd05094    1 HIKRRDIVLKRELGEGAFGKVFLAEcynlsPTKDKMLVAVKTLKDPTL---AARKDFQREAELLTNLQHDHIVKFYGVCG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGELYK----------------ELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLG 209
Cdd:cd05094   78 DGDPLIMVFEYMKHGDLNKflrahgpdamilvdgqPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 210 LKGELKIADFGWS--VHAPSLRR---KTMCgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYR 283
Cdd:cd05094  158 ANLLVKIGDFGMSrdVYSTDYYRvggHTML-PIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIE 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 927602445 284 RIVKVD-LKFPASVPMGAQDLISKLLRHNPSERLPLAQV 321
Cdd:cd05094  237 CITQGRvLERPRVCPKEVYDIMLGCWQREPQQRLNIKEI 275
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
81-327 3.86e-14

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 72.37  E-value: 3.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRR------IY 151
Cdd:cd07876   27 KPIGSGAQGIVCAAFDTVLGINVAVKKLsrpFQNQTHAK----RAYRELVLLKCVNHKNIISLLNVFTPQKSleefqdVY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPrGELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPS-LRR 230
Cdd:cd07876  103 LVMELMD-ANLCQVIHME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTnFMM 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV---------------------- 288
Cdd:cd07876  180 TPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQlgtpsaefmnrlqptvrnyven 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 289 --------------DLKFPASVPMG------AQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07876  260 rpqypgisfeelfpDWIFPSESERDklktsqARDLLSKMLVIDPDKRISVDEALRHPYI 318
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
83-321 4.84e-14

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 71.70  E-value: 4.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKVlFKSQIEKegvehQLRREIEI--QAHLHHPNILRLYNYFYDRR----RIYLILEY 156
Cdd:cd14142   13 IGKGRYGEVWRGQWQGES--VAVKI-FSSRDEK-----SWFRETEIynTVLLRHENILGFIASDMTSRnsctQLWLITHY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKScTFDEQRTATIMEELADALMYCH-------GKKVI-HRDIKPENLLLGLKGELKIADFGWSV-HAPS 227
Cdd:cd14142   85 HENGSLYDYLQRT-TLDHQEMLRLALSAASGLVHLHteifgtqGKPAIaHRDLKSKNILVKSNGQCCIADLGLAVtHSQE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 -----LRRKTMCGTLDYLPPEMIEGRMHNE------KVDLWCIGVLCYEL----LVG------NPPFESASHN----ETY 282
Cdd:cd14142  164 tnqldVGNNPRVGTKRYMAPEVLDETINTDcfesykRVDIYAFGLVLWEVarrcVSGgiveeyKPPFYDVVPSdpsfEDM 243
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 927602445 283 RRIVKVDLKFPASVPMGAQD----LISKLLR----HNPSERLPLAQV 321
Cdd:cd14142  244 RKVVCVDQQRPNIPNRWSSDptltAMAKLMKecwyQNPSARLTALRI 290
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
134-327 5.22e-14

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 70.68  E-value: 5.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 134 HPNILRLYNYFYDRRRIYLILEyAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGE 213
Cdd:cd14024   44 HEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELR 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 214 LKIADFGWSVHAP------SLRRKTMCGTldYLPPEMIEGR--MHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRI 285
Cdd:cd14024  123 TKLVLVNLEDSCPlngdddSLTDKHGCPA--YVGPEILSSRrsYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKI 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 927602445 286 VKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd14024  201 RRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
76-321 6.43e-14

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 70.46  E-value: 6.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLA--REKKshfiVALKVLFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLI 153
Cdd:cd05039    7 DLKLGELIGKGEFGDVMLGdyRGQK----VAVKCLKDDSTAAQ----AFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRGELYKELQKS----CTFDEQRTATImeELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSvhapslr 229
Cdd:cd05039   79 TEYMAKGSLVDYLRSRgravITRKDQLGFAL--DVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLA------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 rKTMCGTLD--YLP-----PEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK-VDLKFPASVPMGA 300
Cdd:cd05039  150 -KEASSNQDggKLPikwtaPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPLKDVVPHVEKgYRMEAPEGCPPEV 228
                        250       260
                 ....*....|....*....|.
gi 927602445 301 QDLISKLLRHNPSERLPLAQV 321
Cdd:cd05039  229 YKVMKNCWELDPAKRPTFKQL 249
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
83-326 7.61e-14

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 70.49  E-value: 7.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKegVEHQ-LRREIEIQAHLHHPNILRLYNYFYD----RRRIYLILEYA 157
Cdd:cd14032    9 LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTK--VERQrFKEEAEMLKGLQHPNIVRFYDFWEScakgKRCIVLVTELM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKG-ELKIADFGWSVHAPSLRRKTMC 234
Cdd:cd14032   87 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLKRASFAKSVI 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMIEgRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKfPASVPM----GAQDLISKLLRH 310
Cdd:cd14032  167 GTPEFMAPEMYE-EHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTCGIK-PASFEKvtdpEIKEIIGECICK 244
                        250
                 ....*....|....*.
gi 927602445 311 NPSERLPLAQVSAHPW 326
Cdd:cd14032  245 NKEERYEIKDLLSHAF 260
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
75-315 7.83e-14

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 70.84  E-value: 7.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHfIVALKVLFKSQIEKEGvehqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd05072    7 ESIKLVKKLGAGQFGEVWMGYYNNST-KVAVKTLKPGTMSVQA----FLEEANLMKTLQHDKLVRLYAVVTKEEPIYIIT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQ----------KSCTFDEQrtatimeeLADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH 224
Cdd:cd05072   82 EYMAKGSLLDFLKsdeggkvllpKLIDFSAQ--------IAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTMCGT---LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMG 299
Cdd:cd05072  154 IEDNEYTAREGAkfpIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRgYRMPRMENCPDE 233
                        250
                 ....*....|....*.
gi 927602445 300 AQDLISKLLRHNPSER 315
Cdd:cd05072  234 LYDIMKTCWKEKAEER 249
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
76-273 9.28e-14

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 70.46  E-value: 9.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLARekkSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14063    1 ELEIKEVIGKGRFGRVHRGR---WHGDVAIKLLNIDYLNEEQLE-AFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKEL--QKScTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENlLLGLKGELKIADFG-WSVHAPSLRRKT 232
Cdd:cd14063   77 LCKGRTLYSLIheRKE-KFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKN-IFLENGRVVITDFGlFSLSGLLQPGRR 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 927602445 233 MC------GTLDYLPPEMIEGRMHN----------EKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd14063  155 EDtlvipnGWLCYLAPEIIRALSPDldfeeslpftKASDVYAFGTVWYELLAGRWPF 211
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
83-220 1.02e-13

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 67.47  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVlfkSQIEKEGVEHQLRREIEIQAHL--HHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKI---GDDVNNEEGEDLESEMDILRRLkgLELNIPKVLVTEDVDGPNILLMELVKGG 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTfDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG 220
Cdd:cd13968   78 TLIAYTQEEEL-DEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
75-318 1.22e-13

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 70.89  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqIEKEGVEHQLRREIEIQAHLHHPN-----ILRLYNYFYDRRR 149
Cdd:cd14228   15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKIL----KNHPSYARQGQIEVSILSRLSSENadeynFVRSYECFQHKNH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRgELYKELQ--KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL----LGLKGELKIADFGWSV 223
Cdd:cd14228   91 TCLVFEMLEQ-NLYDFLKqnKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSAS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDlKFPASVPMGAQDL 303
Cdd:cd14228  170 HVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEYLLSAGTK 248
                        250
                 ....*....|....*
gi 927602445 304 ISKLLRHNPSERLPL 318
Cdd:cd14228  249 TSRFFNRDPNLGYPL 263
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
83-273 1.38e-13

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 69.63  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVY--LAREKKshfiVALKVLFKSQIEKEGVE-HQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd14148    2 IGVGGFGKVYkgLWRGEE----VAVKAARQDPDEDIAVTaENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKScTFDEQRTATIMEELADALMYCHGKK---VIHRDIKPEN--------LLLGLKGELKIADFGWSVHAPSL 228
Cdd:cd14148   78 GALNRALAGK-KVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNililepieNDDLSGKTLKITDFGLAREWHKT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd14148  157 TKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
77-325 1.56e-13

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


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 69.26  E-value: 1.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVlFKSQIEKEGVEHQLRREIEIQAHLH-HPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKR-SRSRFRGEKDRKRKLEEVERHEKLGeHPNCVRFIKAWEEKGILYIQTE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 Y-APRGELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVhapSLRRKTMC 234
Cdd:cd14050   82 LcDTSLQQYCEETHS--LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVV---ELDKEDIH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 ----GTLDYLPPEMIEGRMHNeKVDLWCIGVLCYELLVGnppFESASHNETYRRIVKVDL--KFPASVPMGAQDLISKLL 308
Cdd:cd14050  157 daqeGDPRYMAPELLQGSFTK-AADIFSLGITILELACN---LELPSGGDGWHQLRQGYLpeEFTAGLSPELRSIIKLMM 232
                        250
                 ....*....|....*..
gi 927602445 309 RHNPSERLPLAQVSAHP 325
Cdd:cd14050  233 DPDPERRPTAEDLLALP 249
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
118-326 1.93e-13

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 68.92  E-value: 1.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 118 VEHQLRREIEIQAHLH---HPNILRLYNYFYDRRRIYLILEyAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGK 194
Cdd:cd14023   25 VFPLKHYQDKIRPYIQlpsHRNITGIVEVILGDTKAYVFFE-KDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 195 KVIHRDIKPE-----NLLLGLKGELKIADfgwsVHA-----PSLRRKTMCGTldYLPPEMIE--GRMHNEKVDLWCIGVL 262
Cdd:cd14023  104 AIVLGDLKLRkfvfsDEERTQLRLESLED----THImkgedDALSDKHGCPA--YVSPEILNttGTYSGKSADVWSLGVM 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 263 CYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd14023  178 LYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
81-331 2.15e-13

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: 70.19  E-value: 2.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQieKEGVEHQLRrEIEIQAHLHHPNILRLYNYFYDR------------- 147
Cdd:cd07854   11 RPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTD--PQSVKHALR-EIKIIRRLDHDNIVKVYEVLGPSgsdltedvgslte 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 -RRIYLILEYApRGELYKELQKScTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL-LLGLKGELKIADFGWS--- 222
Cdd:cd07854   88 lNSVYIVQEYM-ETDLANVLEQG-PLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVfINTEDLVLKIGDFGLAriv 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 ----VHAPSLRRKTMcgTLDYLPPEMI-EGRMHNEKVDLWCIGVLCYELLVGNPPFESA---------------SHNETY 282
Cdd:cd07854  166 dphySHKGYLSEGLV--TKWYRSPRLLlSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAheleqmqlilesvpvVREEDR 243
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 283 RRIVKVDLKF----------------PASVPMgAQDLISKLLRHNPSERLPLAQVSAHPWVRANS 331
Cdd:cd07854  244 NELLNVIPSFvrndggeprrplrdllPGVNPE-ALDFLEQILTFNPMDRLTAEEALMHPYMSCYS 307
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
77-285 3.01e-13

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 69.67  E-value: 3.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqIEKEGVEHQLRREIEIQAHLHHPN-----ILRLYNYFYDRRRIY 151
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKIL----KNHPSYARQGQIEVGILARLSNENadefnFVRAYECFQHRNHTC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRgELYKELQ--KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL----LGLKGELKIADFGWSVHA 225
Cdd:cd14229   78 LVFEMLEQ-NLYDFLKqnKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSASHV 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 226 pslrRKTMCGTL----DYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRI 285
Cdd:cd14229  157 ----SKTVCSTYlqsrYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYI 216
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
75-318 3.58e-13

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 69.73  E-value: 3.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqIEKEGVEHQLRREIEIQAHLHHP-----NILRLYNYFYDRRR 149
Cdd:cd14227   15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIL----KNHPSYARQGQIEVSILARLSTEsaddyNFVRAYECFQHKNH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRgELYKELQ--KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLL----LGLKGELKIADFGWSV 223
Cdd:cd14227   91 TCLVFEMLEQ-NLYDFLKqnKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMlvdpSRQPYRVKVIDFGSAS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDlKFPASVPMGAQDL 303
Cdd:cd14227  170 HVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEYLLSAGTK 248
                        250
                 ....*....|....*
gi 927602445 304 ISKLLRHNPSERLPL 318
Cdd:cd14227  249 TTRFFNRDTDSPYPL 263
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
75-321 3.90e-13

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 68.71  E-value: 3.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLARE-----KKSHFIVALKVLfksqieKEGVEHQLR----REIEIQAHLHHPNILRLYNYFY 145
Cdd:cd05050    5 NNIEYVRDIGQGAFGRVFQARApgllpYEPFTMVAVKML------KEEASADMQadfqREAALMAEFDHPNIVKLLGVCA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGEL----------------------YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKP 203
Cdd:cd05050   79 VGKPMCLLFEYMAYGDLneflrhrspraqcslshstssaRKCGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLAT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 204 ENLLLGLKGELKIADFGWS--VHAPSLRRKTMCGTLD--YLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASH 278
Cdd:cd05050  159 RNCLVGENMVVKIADFGLSrnIYSADYYKASENDAIPirWMPPESIFYNRYTTESDVWAYGVVLWEIFsYGMQPYYGMAH 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 927602445 279 NET--YRRIVKVdLKFPASVPMGAQDLISKLLRHNPSERLPLAQV 321
Cdd:cd05050  239 EEViyYVRDGNV-LSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
83-321 6.39e-13

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


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 67.80  E-value: 6.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLARekkSHFIVALKVLFKSQIEKEgvehQL---RREIEIQAHLHHPNILrLYNYFYDRRRIYLILEYAPR 159
Cdd:cd14062    1 IGSGSFGTVYKGR---WHGDVAVKKLNVTDPTPS----QLqafKNEVAVLRKTRHVNIL-LFMGYMTKPQLAIVTQWCEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG-------WSVhAPSLRRK 231
Cdd:cd14062   73 SSLYKHLHVLETkFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGlatvktrWSG-SQQFEQP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 232 TmcGTLDYLPPEMIegRMHNE-----KVDLWCIGVLCYELLVGNPPFESASHNETY-----RRIVKVDL-KFPASVPMGA 300
Cdd:cd14062  152 T--GSILWMAPEVI--RMQDEnpysfQSDVYAFGIVLYELLTGQLPYSHINNRDQIlfmvgRGYLRPDLsKVRSDTPKAL 227
                        250       260
                 ....*....|....*....|.
gi 927602445 301 QDLISKLLRHNPSERLPLAQV 321
Cdd:cd14062  228 RRLMEDCIKFQRDERPLFPQI 248
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
84-266 7.57e-13

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


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 67.85  E-value: 7.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  84 GKGKFGNVYLAReKKSHFiVALKVlFKSQIEKegvehQLRREIEI--QAHLHHPNILRL----YNYFYDRRRIYLILEYA 157
Cdd:cd13998    4 GKGRFGEVWKAS-LKNEP-VAVKI-FSSRDKQ-----SWFREKEIyrTPMLKHENILQFiaadERDTALRTELWLVTAFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKScTFDEQRTATIMEELADALMYCH--------GKKVI-HRDIKPENLLLGLKGELKIADFGWSV-HAPS 227
Cdd:cd13998   76 PNGSL*DYLSLH-TIDWVSLCRLALSVARGLAHLHseipgctqGKPAIaHRDLKSKNILVKNDGTCCIADFGLAVrLSPS 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 LRR-----KTMCGTLDYLPPEMIEGRMHNE------KVDLWCIGVLCYEL 266
Cdd:cd13998  155 TGEednanNGQVGTKRYMAPEVLEGAINLRdfesfkRVDIYAMGLVLWEM 204
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
91-328 1.06e-12

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 67.35  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  91 VYLAREKKSHFIVALKVLFKSQIEKEGV---EHQ---LRREIEIQAHLHHPNILR----------------------LYN 142
Cdd:cd14011   12 IYNGSKKSTKQEVSVFVFEKKQLEEYSKrdrEQIlelLKRGVKQLTRLRHPRILTvqhpleesreslafatepvfasLAN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 143 YFYDRRRIylileyaprGELYKELQKSCTFDEQRTATIMEeLADALMYCHG-KKVIHRDIKPENLLLGLKGELKIADFGW 221
Cdd:cd14011   92 VLGERDNM---------PSPPPELQDYKLYDVEIKYGLLQ-ISEALSFLHNdVKLVHGNICPESVVINSNGEWKLAGFDF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 222 SVHAPSLRRKTMCG-------------TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK 287
Cdd:cd14011  162 CISSEQATDQFPYFreydpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNkGKPLFDCVNNLLSYKKNSN 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 927602445 288 V--DLKFP--ASVPMGAQDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd14011  242 QlrQLSLSllEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPFFD 286
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
77-327 1.15e-12

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


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 67.81  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAR--EKKSHFIVALK----VLFKSQIEKEGVehqlrREIEIQAHLH-HPNILRLY---NYFYD 146
Cdd:cd07857    2 YELIKELGQGAYGIVCSARnaETSEEETVAIKkitnVFSKKILAKRAL-----RELKLLRHFRgHKNITCLYdmdIVFPG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 147 R-RRIYLILEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--- 222
Cdd:cd07857   77 NfNELYLYEELM-EADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLArgf 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 -----VHAPSLrrKTMCGTLDYLPPE-MIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASH---------------NET 281
Cdd:cd07857  156 senpgENAGFM--TEYVATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYvdqlnqilqvlgtpdEET 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927602445 282 YRRI-------------VKVDLKFPASVPMG---AQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07857  234 LSRIgspkaqnyirslpNIPKKPFESIFPNAnplALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
81-327 1.31e-12

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 67.76  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRR------IY 151
Cdd:cd07875   30 KPIGSGAQGIVCAAYDAILERNVAIKKLsrpFQNQTHAK----RAYRELVLMKCVNHKNIIGLLNVFTPQKSleefqdVY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPrGELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA-PSLRR 230
Cdd:cd07875  106 IVMELMD-ANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAgTSFMM 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKV---------------------- 288
Cdd:cd07875  183 TPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQlgtpcpefmkklqptvrtyven 262
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 289 --------------DLKFPASVPMG------AQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07875  263 rpkyagysfeklfpDVLFPADSEHNklkasqARDLLSKMLVIDASKRISVDEALQHPYI 321
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
77-287 1.60e-12

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 67.47  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVL-----FKSQIEKE-GVEHQLRREieiQAHLHhpNILRLYNYFYDRRRI 150
Cdd:cd14211    1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILknhpsYARQGQIEvSILSRLSQE---NADEF--NFVRAYECFQHKNHT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRgELYkELQKSCTFDE---QRTATIMEELADALMYCHGKKVIHRDIKPENLL----LGLKGELKIADFGWSV 223
Cdd:cd14211   76 CLVFEMLEQ-NLY-DFLKQNKFSPlplKYIRPILQQVLTALLKLKSLGLIHADLKPENIMlvdpVRQPYRVKVIDFGSAS 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 224 HAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVK 287
Cdd:cd14211  154 HVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQ 217
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
83-267 1.60e-12

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 66.39  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVlFKSQIEkegvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKI-YKNDVD----QHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAPSL------RRKT 232
Cdd:cd14156   76 EELLaREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNcliRVTPRGREAVVTDFGLAREVGEMpandpeRKLS 155
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 927602445 233 MCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:cd14156  156 LVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
76-271 1.78e-12

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 66.91  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLA-----REKKSHFIVALKVLFKSQIEKEGVEhqLRREIEIQAHLHHPNILRLYNYFYDRRRI 150
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVKAtafrlKGRAGYTTVAVKMLKENASSSELRD--LLSEFNLLKQVNHPHVIKLYGACSQDGPL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKS----CTF--------------DEQRTATIMEELADALMYCHGK------KVIHRDIKPENL 206
Cdd:cd05045   79 LLIVEYAKYGSLRSFLRESrkvgPSYlgsdgnrnssyldnPDERALTMGDLISFAWQISRGMqylaemKLVHRDLAARNV 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 207 LLGLKGELKIADFGWS--VHAPS--LRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYEL--LVGNP 271
Cdd:cd05045  159 LVAEGRKMKISDFGLSrdVYEEDsyVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIvtLGGNP 229
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
83-321 1.90e-12

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 66.59  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYlarEKKSHFIVALKVLFKSQIEKEGVEhQLRREIEIQAHLHHPNILrLYNYFYDRRRIYLILEYAPRGEL 162
Cdd:cd14149   20 IGSGSFGTVY---KGKWHGDVAVKILKVVDPTPEQFQ-AFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 163 YKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG-------WSvhaPSLRRKTMC 234
Cdd:cd14149   95 YKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGlatvksrWS---GSQQVEQPT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 235 GTLDYLPPEMIEGRMHNE---KVDLWCIGVLCYELLVGNPPFESASHNETY-----RRIVKVDL-KFPASVPMGAQDLIS 305
Cdd:cd14149  172 GSILWMAPEVIRMQDNNPfsfQSDVYSYGIVLYELMTGELPYSHINNRDQIifmvgRGYASPDLsKLYKNCPKAMKRLVA 251
                        250
                 ....*....|....*.
gi 927602445 306 KLLRHNPSERLPLAQV 321
Cdd:cd14149  252 DCIKKVKEERPLFPQI 267
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
83-315 1.93e-12

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 66.21  E-value: 1.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKS---HFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRrIYLILEYAPR 159
Cdd:cd05040    3 LGDGSFGVVRRGEWTTPsgkVIQVAVKCLKSDVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSP-LMMVTELAPL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR--------R 230
Cdd:cd05040   82 GSLLDRLRKDQGhFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEdhyvmqehR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTmcgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKVD--LKFPASVPMGAQDLISKL 307
Cdd:cd05040  162 KV---PFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKEGerLERPDDCPQDIYNVMLQC 238

                 ....*...
gi 927602445 308 LRHNPSER 315
Cdd:cd05040  239 WAHKPADR 246
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
81-327 2.15e-12

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 67.42  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRR------IY 151
Cdd:cd07874   23 KPIGSGAQGIVCAAYDAVLDRNVAIKKLsrpFQNQTHAK----RAYRELVLMKCVNHKNIISLLNVFTPQKSleefqdVY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPrGELYKELQKSctFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHA-PSLRR 230
Cdd:cd07874   99 LVMELMD-ANLCQVIQME--LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAgTSFMM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVK----------------------- 287
Cdd:cd07874  176 TPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEqlgtpcpefmkklqptvrnyven 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 288 ----VDLKFPASVP---------------MGAQDLISKLLRHNPSERLPLAQVSAHPWV 327
Cdd:cd07874  256 rpkyAGLTFPKLFPdslfpadsehnklkaSQARDLLSKMLVIDPAKRISVDEALQHPYI 314
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
83-321 2.21e-12

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 66.29  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVY------LAREKKSHFIVALKVLFKSQIEKEGVEhqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd05044    3 LGSGAFGEVFegtakdILGDGSGETKVAVKTLRKGATDQEKAE--FLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSCTFDEQRTA-TIMEELADALMYCHGKK------VIHRDIKPEN----LLLGLKGELKIADFGWS--V 223
Cdd:cd05044   81 MEGGDLLSYLRAARPTAFTPPLlTLKDLLSICVDVAKGCVyledmhFVHRDLAARNclvsSKDYRERVVKIGDFGLArdI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HAPSLRRKTMCGTLD--YLPPE-MIEGRMHNEKvDLWCIGVLCYELL-VGNPPFESASHNETYrRIVKVD--LKFPASVP 297
Cdd:cd05044  161 YKNDYYRKEGEGLLPvrWMAPEsLVDGVFTTQS-DVWAFGVLMWEILtLGQQPYPARNNLEVL-HFVRAGgrLDQPDNCP 238
                        250       260
                 ....*....|....*....|....
gi 927602445 298 MGAQDLISKLLRHNPSERLPLAQV 321
Cdd:cd05044  239 DDLYELMLRCWSTDPEERPSFARI 262
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
79-315 2.36e-12

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 66.57  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNVYLAREKKSHFI--VALKVLFKSQIEKEGVEHQLRREIEIQaHLHHPNILRLYNYFYD--RRRIY--- 151
Cdd:cd05075    4 LGKTLGEGEFGSVMEGQLNQDDSVlkVAVKTMKIAICTRSEMEDFLSEAVCMK-EFDHPNVMRLIGVCLQntESEGYpsp 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 -LILEYAPRGELYKELQKSCTFDE------QRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-- 222
Cdd:cd05075   83 vVILPFMKHGDLHSFLLYSRLGDCpvylptQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLSkk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKVD-LKFPASVPM 298
Cdd:cd05075  163 IYNGDYYRQGRISKMpvKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQGNrLKQPPDCLD 242
                        250
                 ....*....|....*..
gi 927602445 299 GAQDLISKLLRHNPSER 315
Cdd:cd05075  243 GLYELMSSCWLLNPKDR 259
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
77-315 2.37e-12

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 66.20  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKsHFIVALKVLFKSQIEKEGvehqLRREIEIQAHLHHPNILRLyNYFYDRRRIYLILEY 156
Cdd:cd05073   13 LKLEKKLGAGQFGEVWMATYNK-HTKVAVKTMKPGSMSVEA----FLAEANVMKTLQHDKLVKL-HAVVTKEPIYIITEF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELqKSCTFDEQRTATIME---ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLRR 230
Cdd:cd05073   87 MAKGSLLDFL-KSDEGSKQPLPKLIDfsaQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLArviEDNEYTAR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGAQDLISKLL 308
Cdd:cd05073  166 EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRALERgYRMPRPENCPEELYNIMMRCW 245

                 ....*..
gi 927602445 309 RHNPSER 315
Cdd:cd05073  246 KNRPEER 252
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
83-308 3.12e-12

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


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 65.77  E-value: 3.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVY---LAREKKSHFIVALKVLFKSQIEKEGVEhqLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPR 159
Cdd:cd05063   13 IGAGEFGEVFrgiLKMPGRKEVAVAIKTLKPGYTEKQRQD--FLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMEN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 160 GELYKELQ-KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGTLD 238
Cdd:cd05063   91 GALDKYLRdHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPEGTYTTSGG 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 927602445 239 YLP-----PEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKvDLKFPAsvPMGAQDLISKLL 308
Cdd:cd05063  171 KIPirwtaPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAIND-GFRLPA--PMDCPSAVYQLM 243
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
77-293 3.32e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 66.79  E-value: 3.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLA--REKKSHFIVALKVLFKSQiekegvehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:PHA03207  94 YNILSSLTPGSEGEVFVCtkHGDEQRKKVIVKAVTGGK--------TPGREIDILKTISHRAIINLIHAYRWKSTVCMVM 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMC 234
Cdd:PHA03207 166 PKY-KCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPQC 244
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927602445 235 ----GTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF-----ESASHNetYRRIVKV----DLKFP 293
Cdd:PHA03207 245 ygwsGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLfgkqvKSSSSQ--LRSIIRCmqvhPLEFP 314
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
75-315 4.06e-12

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 65.68  E-value: 4.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAReKKSHFIVALKVLFKSQIEKEGvehqLRREIEIQAHLHHPNILRLYNYFyDRRRIYLIL 154
Cdd:cd05067    7 ETLKLVERLGAGQFGEVWMGY-YNGHTKVAIKSLKQGSMSPDA----FLAEANLMKQLQHQRLVRLYAVV-TQEPIYIIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCTFDEQRTATI--MEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLR 229
Cdd:cd05067   81 EYMENGSLVDFLKTPSGIKLTINKLLdmAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLArliEDNEYTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGAQDLISKL 307
Cdd:cd05067  161 REGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNLERgYRMPRPDNCPEELYQLMRLC 240

                 ....*...
gi 927602445 308 LRHNPSER 315
Cdd:cd05067  241 WKERPEDR 248
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
77-339 4.51e-12

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 65.96  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFY--DRRR---IY 151
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKI-NDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLppSRREfkdIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG----------- 220
Cdd:cd07859   81 VVFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGlarvafndtpt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 221 ---WS--VHAPSLRRKTMCGTL--DYLPpemiegrmhneKVDLWCIGVLCYELLVGNPPFE------------------- 274
Cdd:cd07859  160 aifWTdyVATRWYRAPELCGSFfsKYTP-----------AIDIWSIGCIFAEVLTGKPLFPgknvvhqldlitdllgtps 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 275 ----SASHNETYRRI---------VKVDLKFPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPWVRANSRRVLPPSA 339
Cdd:cd07859  229 petiSRVRNEKARRYlssmrkkqpVPFSQKFPNADPL-ALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVEREPSA 305
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
85-267 6.51e-12

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 65.04  E-value: 6.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  85 KGKFGNVYLAREKKShfIVALKVLFKSqiEKEGVEHQlrREIEIQAHLHHPNILrlyNYFYDRRRI-------YLILEYA 157
Cdd:cd14053    5 RGRFGAVWKAQYLNR--LVAVKIFPLQ--EKQSWLTE--REIYSLPGMKHENIL---QFIGAEKHGesleaeyWLITEFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYkELQKSCTFDEQRTATIMEELADALMYCH--------GKK--VIHRDIKPENLLLGLKGELKIADFGWSVH--- 224
Cdd:cd14053   76 ERGSLC-DYLKGNVISWNELCKIAESMARGLAYLHedipatngGHKpsIAHRDFKSKNVLLKSDLTACIADFGLALKfep 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 927602445 225 -APSLRRKTMCGTLDYLPPEMIEGRMHNEK-----VDLWCIGVLCYELL 267
Cdd:cd14053  155 gKSCGDTHGQVGTRRYMAPEVLEGAINFTRdaflrIDMYAMGLVLWELL 203
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
81-315 6.73e-12

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 64.95  E-value: 6.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEH--QLRREIEIQAHLHHPNILRLYNYFYDR--RRIYLILEY 156
Cdd:cd05079   10 RDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHiaDLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELQKSctfdeQRTATIMEELADALMYCHG------KKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRR 230
Cdd:cd05079   90 LPSGSLKEYLPRN-----KNKINLKQQLKYAVQICKGmdylgsRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 -KTMCGTLD-----YLPPEMIEGRMHNEKvDLWCIGVLCYELLV----GNPPFE------SASHNE-TYRRIVKV----- 288
Cdd:cd05079  165 yYTVKDDLDspvfwYAPECLIQSKFYIAS-DVWSFGVTLYELLTycdsESSPMTlflkmiGPTHGQmTVTRLVRVleegk 243
                        250       260
                 ....*....|....*....|....*..
gi 927602445 289 DLKFPASVPMGAQDLISKLLRHNPSER 315
Cdd:cd05079  244 RLPRPPNCPEEVYQLMRKCWEFQPSKR 270
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
76-331 7.65e-12

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 65.07  E-value: 7.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRplgkGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGvEHQLRREIEIQAHLHHPNILRLYNYFYD----RRRIY 151
Cdd:cd14030   30 DIEIGR----GSFKTVYKGLDTETTVEVAWCELQDRKLSKSE-RQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIV 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 152 LILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKG-ELKIADFGWSVHAPSL 228
Cdd:cd14030  105 LVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLKRAS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLDYLPPEMIEGRmHNEKVDLWCIGVLCYELLVGNPPF-ESASHNETYRRIVKvDLKfPASVPMGA----QDL 303
Cdd:cd14030  185 FAKSVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYsECQNAAQIYRRVTS-GVK-PASFDKVAipevKEI 261
                        250       260
                 ....*....|....*....|....*...
gi 927602445 304 ISKLLRHNPSERLPLAQVSAHPWVRANS 331
Cdd:cd14030  262 IEGCIRQNKDERYAIKDLLNHAFFQEET 289
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
78-315 8.35e-12

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 65.03  E-value: 8.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGR-PLGKGKFGNVYLAREKKSHfIVALKVLFKSQIEKEGVEHQlrREIEIQAHLHHPNILRLYNYFYDRRRIYLILEY 156
Cdd:cd05090   12 ELGEcAFGKIYKGHLYLPGMDHAQ-LVAIKTLKDYNNPQQWNEFQ--QEASLMTELHHPNIVCLLGVVTQEQPVCMLFEF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKEL-------QKSCTFDEQRTAT----------IMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADF 219
Cdd:cd05090   89 MNQGDLHEFLimrsphsDVGCSSDEDGTVKssldhgdflhIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 220 GWSVHAPS-----LRRKTMCgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVD-LKF 292
Cdd:cd05090  169 GLSREIYSsdyyrVQNKSLL-PIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFsFGLQPYYGFSNQEVIEMVRKRQlLPC 247
                        250       260
                 ....*....|....*....|...
gi 927602445 293 PASVPMGAQDLISKLLRHNPSER 315
Cdd:cd05090  248 SEDCPPRMYSLMTECWQEIPSRR 270
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
76-315 1.74e-11

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 63.46  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLA--REKKshfiVALKVlfksqIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFY-DRRRIYL 152
Cdd:cd05082    7 ELKLLQTIGKGEFGDVMLGdyRGNK----VAVKC-----IKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVeEKGGLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGEL--YKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLrR 230
Cdd:cd05082   78 VTEYMAKGSLvdYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASST-Q 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 231 KTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK-VDLKFPASVPMGAQDLISKLL 308
Cdd:cd05082  157 DTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYsFGRVPYPRIPLKDVVPRVEKgYKMDAPDGCPPAVYDVMKNCW 236

                 ....*..
gi 927602445 309 RHNPSER 315
Cdd:cd05082  237 HLDAAMR 243
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
77-273 1.78e-11

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 64.34  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVLfksqIEKEGVEHQLRREIEIQAHLHHP------NILRLYNYFYDRRRI 150
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKII----RNKKRFHHQALVEVKILDALRRKdrdnshNVIHMKEYFYFRNHL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRgELYkELQKSCTFdEQRTATIMEELADALMYC----HGKKVIHRDIKPENLLLGLKGELKIA--DFGWSVH 224
Cdd:cd14225  121 CITFELLGM-NLY-ELIKKNNF-QGFSLSLIRRFAISLLQClrllYRERIIHCDLKPENILLRQRGQSSIKviDFGSSCY 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 927602445 225 APSlRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd14225  198 EHQ-RVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLF 245
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
70-257 1.89e-11

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 63.68  E-value: 1.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  70 RHFTIDDFEIGRplgkGKFGNVYLAREKKSHFIVALKvlfKSQIEKEGVEhqlrrEIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd13991    5 VHWATHQLRIGR----GSFGEVHRMEDKQTGFQCAVK---KVRLEVFRAE-----ELMACAGLTSPRVVPLYGAVREGPW 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLK-GELKIADFGWSVHA-PS 227
Cdd:cd13991   73 VNIFMDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDgSDAFLCDFGHAECLdPD 152
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 927602445 228 ------LRRKTMCGTLDYLPPEMIEGRMHNEKVDLW 257
Cdd:cd13991  153 glgkslFTGDYIPGTETHMAPEVVLGKPCDAKVDVW 188
PHA02988 PHA02988
hypothetical protein; Provisional
85-315 2.25e-11

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 63.61  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  85 KGKFGNVylarekkshfIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRR----RIYLILEYAPRG 160
Cdd:PHA02988  38 KGIFNNK----------EVIIRTFKKFHKGHKVLIDITENEIKNLRRIDSNNILKIYGFIIDIVddlpRLSLILEYCTRG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIMEELADAL--MYCHGKKViHRDIKPENLLLGLKGELKIADFGW--SVHAPSLRRKTMcgt 236
Cdd:PHA02988 108 YLREVLDKEKDLSFKTKLDMAIDCCKGLynLYKYTNKP-YKNLTSVSFLVTENYKLKIICHGLekILSSPPFKNVNF--- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 LDYLPPEMIEG--RMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVK--VDLKFPASVPMGAQDLISKLLRHNP 312
Cdd:PHA02988 184 MVYFSYKMLNDifSEYTIKDDIYSLGVVLWEIFTGKIPFENLTTKEIYDLIINknNSLKLPLDCPLEIKCIVEACTSHDS 263

                 ...
gi 927602445 313 SER 315
Cdd:PHA02988 264 IKR 266
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
74-321 2.27e-11

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 63.16  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  74 IDDFEIGRPLGKGKFGNVYLAREK---KSHFIVALKVLFKSQIEKEGVEhqLRREIEIQAHLHHPNILRLYNYFYDRRRI 150
Cdd:cd05033    3 ASYVTIEKVIGGGEFGEVCSGSLKlpgKKEIDVAIKTLKSGYSDKQRLD--FLTEASIMGQFDHPNVIRLEGVVTKSRPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKSctfDEQRTAT----IMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS--VH 224
Cdd:cd05033   81 MIVTEYMENGSLDKFLREN---DGKFTVTqlvgMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSrrLE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTMCG--TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGA 300
Cdd:cd05033  158 DSEATYTTKGGkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAVEDgYRLPPPMDCPSAL 237
                        250       260
                 ....*....|....*....|.
gi 927602445 301 QDLISKLLRHNPSERLPLAQV 321
Cdd:cd05033  238 YQLMLDCWQKDRNERPTFSQI 258
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
72-273 2.32e-11

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 63.54  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvEHQLRREIE-IQAHLHHPNILRLYNYFYDRRRI 150
Cdd:cd06616    3 FTAEDLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKE--QKRLLMDLDvVMRSSDCPYIVKFYGALFREGDC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRG--ELYK---ELQKSCtFDEQRTATIMEELADALMYCHGK-KVIHRDIKPENLLLGLKGELKIADFGWSVH 224
Cdd:cd06616   81 WICMELMDISldKFYKyvyEVLDSV-IPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQ 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 927602445 225 APSLRRKTM-CGTLDYLPPEMIEGRMHNE----KVDLWCIGVLCYELLVGNPPF 273
Cdd:cd06616  160 LVDSIAKTRdAGCRPYMAPERIDPSASRDgydvRSDVWSLGITLYEVATGKFPY 213
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
79-310 4.06e-11

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 62.58  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNVYLAREK---KSHFIVALKVLFKSQIEKEgvEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05066    8 IEKVIGAGEFGEVCSGRLKlpgKREIPVAIKTLKAGYTEKQ--RRDFLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSctfDEQRTAT----IMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSL 228
Cdd:cd05066   86 YMENGSLDAFLRKH---DGQFTVIqlvgMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSrvlEDDPEA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 229 RRKTMCGTLD--YLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESAShNETYRRIVKVDLKFPAsvPMGAQDLIS 305
Cdd:cd05066  163 AYTTRGGKIPirWTAPEAIAYRKFTSASDVWSYGIVMWEVMsYGERPYWEMS-NQDVIKAIEEGYRLPA--PMDCPAALH 239

                 ....*
gi 927602445 306 KLLRH 310
Cdd:cd05066  240 QLMLD 244
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
77-273 4.18e-11

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: 63.61  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKVlfksqIEKEGVEH-QLRREIEIQAHLHHP------NILRLYNYFYDRRR 149
Cdd:cd14224   67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKM-----VRNEKRFHrQAAEEIRILEHLKKQdkdntmNVIHMLESFTFRNH 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRgELYkELQKSCTFdEQRTATIMEELADALMYC----HGKKVIHRDIKPENLLLGLKGELKIA--DFGWSV 223
Cdd:cd14224  142 ICMTFELLSM-NLY-ELIKKNKF-QGFSLQLVRKFAHSILQCldalHRNKIIHCDLKPENILLKQQGRSGIKviDFGSSC 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 HApSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd14224  219 YE-HQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLF 267
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
83-285 6.12e-11

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 62.65  E-value: 6.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVLfKSqieKEGVEHQLRREIEIQAHL---------HHpnILRLYNYFYDRRRIYLI 153
Cdd:cd14212    7 LGQGTFGQVVKCQDLKTNKLVAVKVL-KN---KPAYFRQAMLEIAILTLLntkydpedkHH--IVRLLDHFMHHGHLCIV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 154 LEYAPRgELYkELQKSCTF---DEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA--DFGWSVHapsl 228
Cdd:cd14212   81 FELLGV-NLY-ELLKQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIKliDFGSACF---- 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 927602445 229 RRKTMCGTLD---YLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESAS-HNETYRRI 285
Cdd:cd14212  155 ENYTLYTYIQsrfYRSPEVLLGLPYSTAIDMWSLGCIAAELFLGLPLFPGNSeYNQLSRII 215
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
92-321 1.06e-10

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 61.65  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  92 YLAREKKSHFIVALKVLfksQIEKEGVEHQLRREIEIQAH--------LH-HPNILRLYNYFYD---------------- 146
Cdd:cd13974   15 CLARKEGTDDFYTLKIL---TLEEKGEETQEDRQGKMLLHteysllslLHdQDGVVHHHGLFQDraceikedkssnvytg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 147 --RRRIYLIL------EYAPRGELYKELQ----KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGEL 214
Cdd:cd13974   92 rvRKRLCLVLdclcahDFSDKTADLINLQhyviREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 215 -KIADFGWSVHAPSLRR--KTMCGTLDYLPPEMIEGRMHNEK-VDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDL 290
Cdd:cd13974  172 iTITNFCLGKHLVSEDDllKDQRGSPAYISPDVLSGKPYLGKpSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEY 251
                        250       260       270
                 ....*....|....*....|....*....|...
gi 927602445 291 KFPASVPMGAQ--DLISKLLRHNPSERLPLAQV 321
Cdd:cd13974  252 TIPEDGRVSENtvCLIRKLLVLNPQKRLTASEV 284
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
75-325 1.28e-10

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 61.08  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLAREKKSHF-------IVALKVLFK----SQIEkegvehqlrREIEIqahLH----HPNILR 139
Cdd:cd14019    1 NKYRIIEKIGEGTFSSVYKAEDKLHDLydrnkgrLVALKHIYPtsspSRIL---------NELEC---LErlggSNNVSG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 140 LYNYFYDRRRIYLILEYAPRGElYKELQKSCTFDEQRTatIMEELADALMYCHGKKVIHRDIKPEN-LLLGLKGELKIAD 218
Cdd:cd14019   69 LITAFRNEDQVVAVLPYIEHDD-FRDFYRKMSLTDIRI--YLRNLFKALKHVHSFGIIHRDVKPGNfLYNRETGKGVLVD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 219 FGWS--VHAPSLRRKTMCGTLDYLPPEMIEgRMHNE--KVDLWCIGVLCYELLVGN-PPFESASHNETYRRIVKVdlkfp 293
Cdd:cd14019  146 FGLAqrEEDRPEQRAPRAGTRGFRAPEVLF-KCPHQttAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATI----- 219
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 927602445 294 asvpMG---AQDLISKLLRHNPSERLPLAQVSAHP 325
Cdd:cd14019  220 ----FGsdeAYDLLDKLLELDPSKRITAEEALKHP 250
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
77-315 1.52e-10

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 60.90  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRP-------LGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDRRR 149
Cdd:cd05052    1 WEIERTditmkhkLGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVE----EFLKEAAVMKEIKHPNLVQLLGVCTREPP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 150 IYLILEYAPRGELYKELqKSCTFDEQRTATIM---EELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAP 226
Cdd:cd05052   77 FYIITEFMPYGNLLDYL-RECNREELNAVVLLymaTQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 SLRRKTMCGT---LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGAQ 301
Cdd:cd05052  156 GDTYTAHAGAkfpIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKgYRMERPEGCPPKVY 235
                        250
                 ....*....|....
gi 927602445 302 DLISKLLRHNPSER 315
Cdd:cd05052  236 ELMRACWQWNPSDR 249
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
71-285 1.53e-10

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 61.24  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  71 HFTIDDFEIGRPLGKGKFGNVY-----LAREKKSHFIVALKVLFKSQIEKegVEHQLRREIEIQAHLHHPNILRLYNYFY 145
Cdd:cd05048    1 EIPLSAVRFLEELGEGAFGKVYkgellGPSSEESAISVAIKTLKENASPK--TQQDFRREAELMSDLQHPNIVCLLGVCT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 146 DRRRIYLILEYAPRGELYKEL-------QKSCTFDEQRTATIME---------ELADALMYCHGKKVIHRDIKPENLLLG 209
Cdd:cd05048   79 KEQPQCMLFEYMAHGDLHEFLvrhsphsDVGVSSDDDGTASSLDqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 210 LKGELKIADFGWS--VHAPSLRR---KTMCgTLDYLPPEMI-EGRMHNEKvDLWCIGVLCYELL-VGNPPFESASHNETY 282
Cdd:cd05048  159 DGLTVKISDFGLSrdIYSSDYYRvqsKSLL-PVRWMPPEAIlYGKFTTES-DVWSFGVVLWEIFsYGLQPYYGYSNQEVI 236

                 ...
gi 927602445 283 RRI 285
Cdd:cd05048  237 EMI 239
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
121-267 1.53e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 62.02  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 121 QLRREIEIQAHLHHPNILRL--------YNYFYDRRRIYLILEYAPRGELykELQKSCTFDEQRTatIMEELADALMYCH 192
Cdd:PHA03210 209 QLENEILALGRLNHENILKIeeilrseaNTYMITQKYDFDLYSFMYDEAF--DWKDRPLLKQTRA--IMKQLLCAVEYIH 284
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 927602445 193 GKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK---TMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:PHA03210 285 DKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAfdyGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDML 362
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
83-269 1.54e-10

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 61.05  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALkvlFKSQIEKEGVEHQLR--REIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd14160    1 IGEGEIFEVYRVRIGNRSYAVKL---FKQEKKMQWKKHWKRflSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQksCTFDE-----QRTATIMEELADALMYCHGKK---VIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT 232
Cdd:cd14160   78 TLFDRLQ--CHGVTkplswHERINILIGIAKAIHYLHNSQpctVICGNISSANILLDDQMQPKLTDFALAHFRPHLEDQS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 927602445 233 ----MCGT----LDYLPPEMI-EGRMhNEKVDLWCIGVLCYELLVG 269
Cdd:cd14160  156 ctinMTTAlhkhLWYMPEEYIrQGKL-SVKTDVYSFGIVIMEVLTG 200
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
77-326 1.61e-10

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 61.62  E-value: 1.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGR------PLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIEKegvehqLR--REIEIQAHLHHPNILRL----- 140
Cdd:cd07858    1 FEVDTkyvpikPIGRGAYGIVCSAKNSETNEKVAIKKIanaFDNRIDA------KRtlREIKLLRHLDHENVIAIkdimp 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 141 ---YNYFYDrrrIYLILEYAPRgELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIA 217
Cdd:cd07858   75 pphREAFND---VYIVYELMDT-DLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKIC 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 218 DFGwsvhapsLRRkTMCGTLDYL-----------PPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASH-------- 278
Cdd:cd07858  151 DFG-------LAR-TTSEKGDFMteyvvtrwyraPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYvhqlklit 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 927602445 279 ---------------NETYRRIVK-------VDL--KFPASVPMgAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd07858  223 ellgspseedlgfirNEKARRYIRslpytprQSFarLFPHANPL-AIDLLEKMLVFDPSKRITVEEALAHPY 293
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
76-328 1.97e-10

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 61.30  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  76 DFEIGRPLGKGKFGNVYLAREKKSHFIVALKVL---FKSQIEKEGVehqlRREIEIQAHLHHPNILR--------LYNYF 144
Cdd:cd07853    1 DVEPDRPIGYGAFGVVWSVTDPRDGKRVALKKMpnvFQNLVSCKRV----FRELKMLCFFKHDNVLSaldilqppHIDPF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 145 ydrRRIYLILEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH 224
Cdd:cd07853   77 ---EEIYVVTELM-QSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTMCG---TLDYLPPEMIEGRMH-NEKVDLWCIGVLCYELL---------------------VGNPPFE----- 274
Cdd:cd07853  153 EEPDESKHMTQevvTQYYRAPEILMGSRHyTSAVDIWSVGCIFAELLgrrilfqaqspiqqldlitdlLGTPSLEamrsa 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 275 -SASHNETYRRIVK---VDLKFPASVPMG--AQDLISKLLRHNPSERLPLAQVSAHPWVR 328
Cdd:cd07853  233 cEGARAHILRGPHKppsLPVLYTLSSQATheAVHLLCRMLVFDPDKRISAADALAHPYLD 292
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
78-273 2.53e-10

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 60.77  E-value: 2.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRPLGKGKFGN--VYLAREKKSHFIVALK-VLFKSQIEKEGVehQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLIL 154
Cdd:cd08216    1 ELLYEIGKCFKGGgvVHLAKHKPTNTLVAVKkINLESDSKEDLK--FLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQKSCT--FDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVH--APSLRR 230
Cdd:cd08216   79 PLMAYGSCRDLLKTHFPegLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSmvKHGKRQ 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 927602445 231 KTMCG-------TLDYLPPEMIEGRMH--NEKVDLWCIGVLCYELLVGNPPF 273
Cdd:cd08216  159 RVVHDfpkssekNLPWLSPEVLQQNLLgyNEKSDIYSVGITACELANGVVPF 210
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
72-287 3.33e-10

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 60.20  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLA-----REKKSHFIVALKVLfksqieKEGVEHQLRR----EIEIQAHL-HHPNILRLY 141
Cdd:cd05054    4 FPRDRLKLGKPLGRGAFGKVIQAsafgiDKSATCRTVAVKML------KEGATASEHKalmtELKILIHIgHHLNVVNLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 142 NYFYDRRR-IYLILEYAPRGEL--YKELQKSCTFDEQRTATI-----------------MEEL-------ADALMYCHGK 194
Cdd:cd05054   78 GACTKPGGpLMVIVEFCKFGNLsnYLRSKREEFVPYRDKGARdveeeedddelykepltLEDLicysfqvARGMEFLASR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 195 KVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLRRKTMCG-TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VG 269
Cdd:cd05054  158 KCIHRDLAARNILLSENNVVKICDFGLArdiYKDPDYVRKGDARlPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFsLG 237
                        250
                 ....*....|....*...
gi 927602445 270 NPPFESASHNETYRRIVK 287
Cdd:cd05054  238 ASPYPGVQMDEEFCRRLK 255
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
81-321 3.34e-10

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 60.05  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHfiVALKVLFKSQiekegvEHQLRREIEI--QAHLHHPNILRLY----NYFYDRRRIYLIL 154
Cdd:cd14220    1 RQIGKGRYGEVWMGKWRGEK--VAVKVFFTTE------EASWFRETEIyqTVLMRHENILGFIaadiKGTGSWTQLYLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELqKSCTFDEQRTATIMEELADALMYCH-------GKKVI-HRDIKPENLLLGLKGELKIADFGWSV--- 223
Cdd:cd14220   73 DYHENGSLYDFL-KCTTLDTRALLKLAYSAACGLCHLHteiygtqGKPAIaHRDLKSKNILIKKNGTCCIADLGLAVkfn 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 224 ---HAPSLRRKTMCGTLDYLPPEMIEGRMHNEK------VDLWCIGVLCYEL----LVGN-------PPFESASHNETY- 282
Cdd:cd14220  152 sdtNEVDVPLNTRVGTKRYMAPEVLDESLNKNHfqayimADIYSFGLIIWEMarrcVTGGiveeyqlPYYDMVPSDPSYe 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 927602445 283 --RRIVKVDLKFPASVPMGAQD--------LISKLLRHNPSERLPLAQV 321
Cdd:cd14220  232 dmREVVCVKRLRPTVSNRWNSDeclravlkLMSECWAHNPASRLTALRI 280
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
135-326 3.43e-10

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


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 59.87  E-value: 3.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 135 PNILRLYNYFYDRRRIYLILEYAPRGELYKELQK-------SCTFDE-------QRTATIME--------ELADALMYCH 192
Cdd:cd05576   51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKflndkeiHQLFADlderlaaASRFYIPEeciqrwaaEMVVALDALH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 193 GKKVIHRDIKPENLLLGLKGELKIADFG-WSVHAPSLRRKTMCGTldYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNP 271
Cdd:cd05576  131 REGIVCRDLNPNNILLNDRGHIQLTYFSrWSEVEDSCDSDAIENM--YCAPEVGGISEETEACDWWSLGALLFELLTGKA 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 272 PFEsaSHNETYRRivKVDLKFPASVPMGAQDLISKLLRHNPSERL-----PLAQVSAHPW 326
Cdd:cd05576  209 LVE--CHPAGINT--HTTLNIPEWVSEEARSLLQQLLQFNPTERLgagvaGVEDIKSHPF 264
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
128-326 3.54e-10

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 59.36  E-value: 3.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 128 IQAHLH---HPNILRLYNYFYDRRRIYLILEYApRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKpe 204
Cdd:cd13976   35 LRAYFRlpsHPNISGVHEVIAGETKAYVFFERD-HGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLK-- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 205 nlllglkgelkIADFgwsVHAPSLRRKTMCGTLD--------------------YLPPEMIEGRMH--NEKVDLWCIGVL 262
Cdd:cd13976  112 -----------LRKF---VFADEERTKLRLESLEdavilegeddslsdkhgcpaYVSPEILNSGATysGKAADVWSLGVI 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 263 CYELLVGNPPFESASHNETYRRIVKVDLKFPASVPMGAQDLISKLLRHNPSERLPLAQVSAHPW 326
Cdd:cd13976  178 LYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDILLHPW 241
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
81-275 3.74e-10

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 59.91  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSH----FIVALKVLfksqieKEGVEHQLR----REIEIQAHLHHPNILRLYNYFYDR--RRI 150
Cdd:cd05080   10 RDLGEGHFGKVSLYCYDPTNdgtgEMVAVKAL------KADCGPQHRsgwkQEIDILKTLYHENIVKYKGCCSEQggKSL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKScTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLR- 229
Cdd:cd05080   84 QLIMEYVPLGSLRDYLPKH-SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHe 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 ----RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFES 275
Cdd:cd05080  163 yyrvREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQS 212
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
83-267 5.74e-10

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


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 59.68  E-value: 5.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKShfIVALKVLFKSQIEKegveHQLRREIEIQAHLHHPNILRLYNY----FYDRRRIYLI-LEYA 157
Cdd:cd14054    3 IGQGRYGTVWKGSLDER--PVAVKVFPARHRQN----FQNEKDIYELPLMEHSNILRFIGAderpTADGRMEYLLvLEYA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKScTFDeQRTATIM-EELADALMYCHGKK---------VIHRDIKPENLLLGLKGELKIADFGWSVHAPS 227
Cdd:cd14054   77 PKGSLCSYLREN-TLD-WMSSCRMaLSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADGSCVICDFGLAMVLRG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 228 LRRK------------TMCGTLDYLPPEMIEG--RMHN-----EKVDLWCIGVLCYELL 267
Cdd:cd14054  155 SSLVrgrpgaaenasiSEVGTLRYMAPEVLEGavNLRDcesalKQVDVYALGLVLWEIA 213
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
83-267 6.18e-10

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 59.03  E-value: 6.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHFIVALKVlfksqiekegveHQLR-------REIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM------------NTLSsnranmlREVQLMNRLSHPNILRFMGVCVHQGQLHALTE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN---LLLGLKGELKIADFGWSVHAPSLR--- 229
Cdd:cd14155   69 YINGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNcliKRDENGYTAVVGDFGLAEKIPDYSdgk 148
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 927602445 230 -RKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:cd14155  149 eKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
81-315 7.39e-10

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 59.16  E-value: 7.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRG 160
Cdd:cd14026    3 RYLSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQR---TATIMEELADALMYCHGKK--VIHRDIKPENLLLGLKGELKIADFG---WSVHAPSLRRKT 232
Cdd:cd14026   83 SLNELLHEKDIYPDVAwplRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGlskWRQLSISQSRSS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 ----MCGTLDYLPPEMIE---GRMHNEKVDLWCIGVLCYELLVGNPPFESA--------SHNETYRRIVKVDlKFPASVP 297
Cdd:cd14026  163 ksapEGGTIIYMPPEEYEpsqKRRASVKHDIYSYAIIMWEVLSRKIPFEEVtnplqimySVSQGHRPDTGED-SLPVDIP 241
                        250       260
                 ....*....|....*....|
gi 927602445 298 MGAQ--DLISKLLRHNPSER 315
Cdd:cd14026  242 HRATliNLIESGWAQNPDER 261
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
72-315 8.72e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 59.25  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLARE---KKS--HFIVALKVLfksqieKEGV---EHQ-LRREIEIQAHL-HHPNILRLY 141
Cdd:cd14207    4 FARERLKLGKSLGRGAFGKVVQASAfgiKKSptCRVVAVKML------KEGAtasEYKaLMTELKILIHIgHHLNVVNLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 142 -----------------------NYFYDRRRIYLI-LEYAPRGELYKELQK---------------------SCTFDEQR 176
Cdd:cd14207   78 gactksggplmviveyckygnlsNYLKSKRDFFVTnKDTSLQEELIKEKKEaeptggkkkrlesvtssesfaSSGFQEDK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 177 TATIMEE------------------------LADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLR 229
Cdd:cd14207  158 SLSDVEEeeedsgdfykrpltmedlisysfqVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLArdiYKNPDYV 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 230 RKTMCG-TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVKVDLKFPAsvPMGAQDLISKL 307
Cdd:cd14207  238 RKGDARlPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFsLGASPYPGVQIDEDFCSKLKEGIRMRA--PEFATSEIYQI 315
                        330
                 ....*....|..
gi 927602445 308 L----RHNPSER 315
Cdd:cd14207  316 MldcwQGDPNER 327
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
81-315 8.95e-10

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 58.89  E-value: 8.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREK-----KSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHpnILRLYNYFYDRRRIYLILE 155
Cdd:cd05062   12 RELGQGSFGMVYEGIAKgvvkdEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHH--VVRLLGVVSQGQPTLVIME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELyKELQKSCTFDEQRTAT-----------IMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-- 222
Cdd:cd05062   90 LMTRGDL-KSYLRSLRPEMENNPVqappslkkmiqMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTrd 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRRKTMCGTLD--YLPPEMIEGRMHNEKVDLWCIGVLCYEL-LVGNPPFESASHNETYRRIVKVD-LKFPASVPM 298
Cdd:cd05062  169 IYETDYYRKGGKGLLPvrWMSPESLKDGVFTTYSDVWSFGVVLWEIaTLAEQPYQGMSNEQVLRFVMEGGlLDKPDNCPD 248
                        250
                 ....*....|....*..
gi 927602445 299 GAQDLISKLLRHNPSER 315
Cdd:cd05062  249 MLFELMRMCWQYNPKMR 265
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
83-308 1.10e-09

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 58.34  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREK---KSHFIVALKVLfksqieKEGVEHQLRR----EIEIQAHLHHPNILRLYNYFYDRRRIYLILE 155
Cdd:cd05065   12 IGAGEFGEVCRGRLKlpgKREIFVAIKTL------KSGYTEKQRRdflsEASIMGQFDHPNIIHLEGVVTKSRPVMIITE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS----------VH 224
Cdd:cd05065   86 FMENGALDSFLrQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSrfleddtsdpTY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 APSLRRKTmcgTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESAShNETYRRIVKVDLKFPAsvPMGAQDL 303
Cdd:cd05065  166 TSSLGGKI---PIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMsYGERPYWDMS-NQDVINAIEQDYRLPP--PMDCPTA 239

                 ....*
gi 927602445 304 ISKLL 308
Cdd:cd05065  240 LHQLM 244
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
81-273 1.91e-09

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 57.48  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVY---LAREKKSHFIVALKVLfkSQIEK-EGVEHQLRREIeIQAHLHHPNILRLYNYFYDRRRIYLI-LE 155
Cdd:cd05058    1 EVIGKGHFGCVYhgtLIDSDGQKIHCAVKSL--NRITDiEEVEQFLKEGI-IMKDFSHPNVLSLLGICLPSEGSPLVvLP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELYKELQksctfDEQRTATIME------ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFG--------- 220
Cdd:cd05058   78 YMKHGDLRNFIR-----SETHNPTVKDligfglQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGlardiydke 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 221 -WSVHapslRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPF 273
Cdd:cd05058  153 yYSVH----NHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPPY 203
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
134-323 2.10e-09

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 57.89  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 134 HPNILRLYNYFYDRRRIY--LILEYA--------PRG-----ELY----------KELQKSCTFDEQRTATIMEELADAL 188
Cdd:cd14018   72 HPNIIRVQRAFTDSVPLLpgAIEDYPdvlparlnPSGlghnrTLFlvmknypctlRQYLWVNTPSYRLARVMILQLLEGV 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 189 MYCHGKKVIHRDIKPEN----LLLGLKGELKIADFGWSVHAPSLRRKtmcgtLDY-------------LPPEMIEGR--- 248
Cdd:cd14018  152 DHLVRHGIAHRDLKSDNilleLDFDGCPWLVIADFGCCLADDSIGLQ-----LPFsswyvdrggnaclMAPEVSTAVpgp 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 249 ---MHNEKVDLWCIGVLCYELLVGNPPF----ESASHNETYRRIVKVDLkfPASVPMGAQDLISKLLRHNPSERlPLAQV 321
Cdd:cd14018  227 gvvINYSKADAWAVGAIAYEIFGLSNPFyglgDTMLESRSYQESQLPAL--PSAVPPDVRQVVKDLLQRDPNKR-VSARV 303

                 ..
gi 927602445 322 SA 323
Cdd:cd14018  304 AA 305
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
81-315 2.28e-09

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 57.67  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREK-----KSHFIVALKVLFKSQIEKEGVEHQLRREIEIQAHLHHpnILRLYNYFYDRRRIYLILE 155
Cdd:cd05061   12 RELGQGSFGMVYEGNARdiikgEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHH--VVRLLGVVSKGQPTLVVME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 156 YAPRGELyKELQKSCTFDEQRTA-----TIME------ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-- 222
Cdd:cd05061   90 LMAHGDL-KSYLRSLRPEAENNPgrpppTLQEmiqmaaEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTrd 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYEL-LVGNPPFESASHNETYRRIVKVD-LKFPASVPM 298
Cdd:cd05061  169 IYETDYYRKGGKGLLpvRWMAPESLKDGVFTTSSDMWSFGVVLWEItSLAEQPYQGLSNEQVLKFVMDGGyLDQPDNCPE 248
                        250
                 ....*....|....*..
gi 927602445 299 GAQDLISKLLRHNPSER 315
Cdd:cd05061  249 RVTDLMRMCWQFNPKMR 265
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
81-288 2.32e-09

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 57.50  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHFIVALKVlFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFydRRRIYLILEYAPRG 160
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKC-PPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEYMETG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQRTATIME-ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-----VHAPSLRRKTMC 234
Cdd:cd14025   79 SLEKLLASEPLPWELRFRIIHEtAVGMNFLHCMKPPLLHLDLKPANILLDAHYHVKISDFGLAkwnglSHSHDLSRDGLR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 927602445 235 GTLDYLPPEMI--EGRMHNEKVDLWCIGVLCYELLVGNPPFesASHNETYRRIVKV 288
Cdd:cd14025  159 GTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPF--AGENNILHIMVKV 212
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
125-274 2.66e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 58.08  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 125 EIEIQAHLHHPNILRLYNYFYDRRRIYLILeyaPR--GELYkelqksCTFDEQRTATIMEELA------DALMYCHGKKV 196
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFTCLIL---PRykTDLY------CYLAAKRNIAICDILAiersvlRAIQYLHENRI 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 197 IHRDIKPENLLLGLKGELKIADFG---WSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVG-NPP 272
Cdd:PHA03212 204 IHRDIKAENIFINHPGDVCLGDFGaacFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATChDSL 283

                 ..
gi 927602445 273 FE 274
Cdd:PHA03212 284 FE 285
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
79-324 3.17e-09

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 57.25  E-value: 3.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  79 IGRPLGKGKFGNV---YLAREKKSHFIVALKVLFKSQIEKEGVEHQLRrEIEIQAHLHHPNILRLYNYFYD--RRRI--- 150
Cdd:cd14204   11 LGKVLGEGEFGSVmegELQQPDGTNHKVAVKTMKLDNFSQREIEEFLS-EAACMKDFNHPNVIRLLGVCLEvgSQRIpkp 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 151 YLILEYAPRGELYKELQKS------CTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS-- 222
Cdd:cd14204   90 MVILPFMKYGDLHSFLLRSrlgsgpQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSkk 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 223 VHAPSLRRKTMCGTL--DYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVKVD-LKFPASVPM 298
Cdd:cd14204  170 IYSGDYYRQGRIAKMpvKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLLHGHrLKQPEDCLD 249
                        250       260
                 ....*....|....*....|....*.
gi 927602445 299 GAQDLISKLLRHNPSERLPLAQVSAH 324
Cdd:cd14204  250 ELYDIMYSCWRSDPTDRPTFTQLREN 275
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
122-283 3.44e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 57.98  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 122 LRReieiqahLHHPNILRLYNYFYDRRRIYLIL-EYapRGELYKEL-QKSCTFDEQRTATIMEELADALMYCHGKKVIHR 199
Cdd:PHA03211 214 LRR-------LSHPAVLALLDVRVVGGLTCLVLpKY--RSDLYTYLgARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHR 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 200 DIKPENLLLGLKGELKIADFG--------WSVHAPSlrrkTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNP 271
Cdd:PHA03211 285 DIKTENVLVNGPEDICLGDFGaacfargsWSTPFHY----GIAGTVDTNAPEVLAGDPYTPSVDIWSAGLVIFEAAVHTA 360
                        170
                 ....*....|..
gi 927602445 272 PFESASHNETYR 283
Cdd:PHA03211 361 SLFSASRGDERR 372
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
78-275 3.52e-09

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 56.94  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRPLGKGKFGNVYLARekkSHFIVALKvLFKSQIEKEGVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYA 157
Cdd:cd14153    3 EIGELIGKGRFGQVYHGR---WHGEVAIR-LIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELQKSCT-FDEQRTATIMEELADALMYCHGKKVIHRDIKPENlLLGLKGELKIADFGWSVHAPSL-------R 229
Cdd:cd14153   79 KGRTLYSVVRDAKVvLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKN-VFYDNGKVVITDFGLFTISGVLqagrredK 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 927602445 230 RKTMCGTLDYLPPEMI--------EGRM-HNEKVDLWCIGVLCYELLVGNPPFES 275
Cdd:cd14153  158 LRIQSGWLCHLAPEIIrqlspeteEDKLpFSKHSDVFAFGTIWYELHAREWPFKT 212
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
75-205 3.69e-09

BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine/threonine kinase of the Pgl (phage growth limitation) system (now called BREX type 2) and the BREX type 3 system.


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 58.43  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445   75 DDFEIGRPLGKGKFGNVYLAREKKSH-----FIVALKvlfksqiekEGVEHQLRREIEIQAHLHHPNILRLYNyfyDRRR 149
Cdd:NF033442  510 GGFEVRRRLGTGSTSRALLVRDRDADgeervLKVALD---------DEHAARLRAEAEVLGRLRHPRIVALVE---GPLE 577
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  150 I----YLILEYAPRGELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPEN 205
Cdd:NF033442  578 IggrtALLLEYAGEQTLAERLRKEGRLSLDLLERFGDDLLSAVVHLEGQGVWHRDIKPDN 637
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
75-315 4.42e-09

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 56.62  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRPLGKGKFGNVYLArEKKSHFIVALKVLFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFyDRRRIYLIL 154
Cdd:cd05070    9 ESLQLIKRLGNGQFGEVWMG-TWNGNTKVAIKTLKPGTMSPE----SFLEEAQIMKKLKHDKLVQLYAVV-SEEPIYIVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELYKELQ--KSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKT 232
Cdd:cd05070   83 EYMSKGSLLDFLKdgEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 233 MCGT---LDYLPPE-MIEGRMhNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGAQDLISK 306
Cdd:cd05070  163 RQGAkfpIKWTAPEaALYGRF-TIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERgYRMPCPQDCPISLHELMIH 241

                 ....*....
gi 927602445 307 LLRHNPSER 315
Cdd:cd05070  242 CWKKDPEER 250
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
77-316 9.80e-09

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 56.03  E-value: 9.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLAREKKSHFIVALKvlfKSQIEK-EGVEHQLRREIEIQA-HLHHPNILRL-------------Y 141
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNApENVELALREFWALSSiQRQHPNVIQLeecvlqrdglaqrM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 142 NYFYDRRRIYLIL-EYAPRGELYKELQKSCTF---------------------DEQRTATIMEELADALMYCHGKKVIHR 199
Cdd:cd13977   79 SHGSSKSDLYLLLvETSLKGERCFDPRSACYLwfvmefcdggdmneyllsrrpDRQTNTSFMLQLSSALAFLHRNQIVHR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 200 DIKPENLLLGLKGELKI---ADFGWS-------------VHAPSLRRKTMCGTLDYLPPEMIEGRmHNEKVDLWCIGVLC 263
Cdd:cd13977  159 DLKPDNILISHKRGEPIlkvADFGLSkvcsgsglnpeepANVNKHFLSSACGSDFYMAPEVWEGH-YTAKADIFALGIII 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 264 YELLVGNPPFESASHNE---TY----RRIV----------KVDLKFPA----SVPMGAQDLISKLLRHNPSERL 316
Cdd:cd13977  238 WAMVERITFRDGETKKEllgTYiqqgKEIVplgeallenpKLELQIPLkkkkSMNDDMKQLLRDMLAANPQERP 311
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
85-267 1.09e-08

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 55.42  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  85 KGKFGNVYLAREKKSHfiVALKVlFKSQiekEGVEHQLRREIEIQAHLHHPNILRlynYFYDRRR-------IYLILEYA 157
Cdd:cd14140    5 RGRFGCVWKAQLMNEY--VAVKI-FPIQ---DKQSWQSEREIFSTPGMKHENLLQ---FIAAEKRgsnlemeLWLITAFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 158 PRGELYKELqKSCTFDEQRTATIMEELADALMYCH---------GKK--VIHRDIKPENLLLGLKGELKIADFGWSVH-- 224
Cdd:cd14140   76 DKGSLTDYL-KGNIVSWNELCHIAETMARGLSYLHedvprckgeGHKpaIAHRDFKSKNVLLKNDLTAVLADFGLAVRfe 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 225 --APSLRRKTMCGTLDYLPPEMIEGRMHNE-----KVDLWCIGVLCYELL 267
Cdd:cd14140  155 pgKPPGDTHGQVGTRRYMAPEVLEGAINFQrdsflRIDMYAMGLVLWELV 204
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
85-271 1.12e-08

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 55.61  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  85 KGKFGNVYLAREKKSHFIValKVLFKSQIEKEG-VEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYLILEYAPRGELY 163
Cdd:cd14157    3 EGTFADIYKGYRHGKQYVI--KRLKETECESPKsTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 164 KELQKSCTFD----EQRTaTIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRK-TMCGT-- 236
Cdd:cd14157   81 DRLQQQGGSHplpwEQRL-SISLGLLKAVQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGLRLCPVDKKSVyTMMKTkv 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 927602445 237 ----LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNP 271
Cdd:cd14157  160 lqisLAYLPEDFVRHGQLTEKVDIFSCGVVLAEILTGIK 198
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
72-322 1.15e-08

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 55.57  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVY------LAREKKShFIVALKVLFKS--QIEKEGvehqLRREIEIQAHL-HHPNILRLYN 142
Cdd:cd05055   32 FPRNNLSFGKTLGAGAFGKVVeataygLSKSDAV-MKVAVKMLKPTahSSEREA----LMSELKIMSHLgNHENIVNLLG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 143 YFYDRRRIYLILEYAPRGELYKELQKS----CTFDE-----QRTATIMEELADalmychgKKVIHRDIKPENLLLGLKGE 213
Cdd:cd05055  107 ACTIGGPILVITEYCCYGDLLNFLRRKresfLTLEDllsfsYQVAKGMAFLAS-------KNCIHRDLAARNVLLTHGKI 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 214 LKIADFGwsvhapsLRRKTMCGT-----------LDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNET 281
Cdd:cd05055  180 VKICDFG-------LARDIMNDSnyvvkgnarlpVKWMAPESIFNCVYTFESDVWSYGILLWEIFsLGSNPYPGMPVDSK 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 927602445 282 YRRIVKVDLKF--PASVPMGAQDLISKLLRHNPSERLPLAQVS 322
Cdd:cd05055  253 FYKLIKEGYRMaqPEHAPAEIYDIMKTCWDADPLKRPTFKQIV 295
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
78-267 1.40e-08

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 55.42  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRPLGKGKFGNVYLAR----------------EKKSHFIVALKVLfKSQIEKEGVEhQLRREIEIQAHLHHPNILRLY 141
Cdd:cd05051    8 EFVEKLGEGQFGEVHLCEanglsdltsddfigndNKDEPVLVAVKML-RPDASKNARE-DFLKEVKIMSQLKDPNIVRLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 142 NYFYDRRRIYLILEYAPRGELYKELQKSCTFDEQRTAT------------IMEELADALMYCHGKKVIHRDIKPENLLLG 209
Cdd:cd05051   86 GVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASATnsktlsygtllyMATQIASGMKYLESLNFVHRDLATRNCLVG 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 210 LKGELKIADFGWSvhapslrRKTMCGtlDYLppeMIEGR-------MHNE---------KVDLWCIGVLCYELL 267
Cdd:cd05051  166 PNYTIKIADFGMS-------RNLYSG--DYY---RIEGRavlpirwMAWEsillgkfttKSDVWAFGVTLWEIL 227
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
78-269 1.76e-08

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 54.80  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  78 EIGRPLGKGKFGNVYLAREKKSHFIVALKVLFKSQiEKE----GVEHQLRREIEiqahlHHPNILRLYNYFYDRR----- 148
Cdd:cd13975    3 KLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPD-DKHwndlALEFHYTRSLP-----KHERIVSLHGSVIDYSygggs 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 --RIYLILEYAPRgELYKELQKSCTFDEQrtATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVhAP 226
Cdd:cd13975   77 siAVLLIMERLHR-DLYTGIKAGLSLEER--LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCK-PE 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 927602445 227 SLRRKTMCGTLDYLPPEMIEGRMHNEkVDLWCIGVLCYELLVG 269
Cdd:cd13975  153 AMMSGSIVGTPIHMAPELFSGKYDNS-VDVYAFGILFWYLCAG 194
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
72-287 2.76e-08

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 54.60  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  72 FTIDDFEIGRPLGKGKFGNVYLAR-----EKKSHFIVALKVLfksqieKEGVEHQ----LRREIEIQAHL-HHPNILRLY 141
Cdd:cd05103    4 FPRDRLKLGKPLGRGAFGQVIEADafgidKTATCRTVAVKML------KEGATHSehraLMSELKILIHIgHHLNVVNLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 142 -----------------------NYFYDRRRIYLILEY-APR--------GELYKELQK------------SCTFDEQRT 177
Cdd:cd05103   78 gactkpggplmvivefckfgnlsAYLRSKRSEFVPYKTkGARfrqgkdyvGDISVDLKRrldsitssqssaSSGFVEEKS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 178 ATIMEE------------------------LADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWS---VHAPSLRR 230
Cdd:cd05103  158 LSDVEEeeagqedlykdfltledlicysfqVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLArdiYKDPDYVR 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 927602445 231 KTMCG-TLDYLPPEMIEGRMHNEKVDLWCIGVLCYELL-VGNPPFESASHNETYRRIVK 287
Cdd:cd05103  238 KGDARlPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFsLGASPYPGVKIDEEFCRRLK 296
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
83-249 3.12e-08

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 54.31  E-value: 3.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHF----IVALKVLFKSQIEKEGVEhqlrREIEIQAHLHHPNILRLY----NYFYDRRRIYLIL 154
Cdd:cd14055    3 VGKGRFAEVWKAKLKQNASgqyeTVAVKIFPYEEYASWKNE----KDIFTDASLKHENILQFLtaeeRGVGLDRQYWLIT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 155 EYAPRGELyKELQKSCTFDEQRTATIMEELADALMYCHGKK---------VIHRDIKPENLLLGLKGELKIADFGWSVHA 225
Cdd:cd14055   79 AYHENGSL-QDYLTRHILSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRDLKSSNILVKNDGTCVLADFGLALRL 157
                        170       180       190
                 ....*....|....*....|....*....|
gi 927602445 226 -PSLRRKTMC-----GTLDYLPPEMIEGRM 249
Cdd:cd14055  158 dPSLSVDELAnsgqvGTARYMAPEALESRV 187
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
75-315 3.43e-08

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 53.95  E-value: 3.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  75 DDFEIGRP-------LGKGKFGNVYLAREKKShFIVALKVLFKSQIEKEgvehQLRREIEIQAHLHHPNILRLYNYFYDR 147
Cdd:cd05068    1 DQWEIDRKslkllrkLGSGQFGEVWEGLWNNT-TPVAVKTLKPGTMDPE----DFLREAQIMKKLRHPKLIQLYAVCTLE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 148 RRIYLILEYAPRGELYKELQKSCTFDEQRTATIME-ELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGwsvhap 226
Cdd:cd05068   76 EPIYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAaQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFG------ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 227 sLRRKTMC--------GT---LDYLPPEMIEGRMHNEKVDLWCIGVLCYELLV-GNPPFESASHNETyrrIVKVDLKF-- 292
Cdd:cd05068  150 -LARVIKVedeyeareGAkfpIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEV---LQQVERGYrm 225
                        250       260
                 ....*....|....*....|....*
gi 927602445 293 --PASVPMGAQDLISKLLRHNPSER 315
Cdd:cd05068  226 pcPPNCPPQLYDIMLECWKADPMER 250
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
83-266 3.47e-08

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 54.29  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYLAREKKSHfiVALKVLFKSQiekegvEHQLRREIEI--QAHLHHPNILRLYNYFY----DRRRIYLILEY 156
Cdd:cd14219   13 IGKGRYGEVWMGKWRGEK--VAVKVFFTTE------EASWFRETEIyqTVLMRHENILGFIAADIkgtgSWTQLYLITDY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 157 APRGELYKELqKSCTFDEQRTATIMEELADALMYCH-------GKKVI-HRDIKPENLLLGLKGELKIADFGWSVHAPS- 227
Cdd:cd14219   85 HENGSLYDYL-KSTTLDTKAMLKLAYSSVSGLCHLHteifstqGKPAIaHRDLKSKNILVKKNGTCCIADLGLAVKFISd 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 927602445 228 -----LRRKTMCGTLDYLPPEMIE---GRMHNEK---VDLWCIGVLCYEL 266
Cdd:cd14219  164 tnevdIPPNTRVGTKRYMPPEVLDeslNRNHFQSyimADMYSFGLILWEV 213
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
77-293 4.92e-08

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 53.77  E-value: 4.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  77 FEIGRPLGKGKFGNVYLARE-KKSHFIVALKVLFKSQI-EKEGvehqlRREIEIQAHL--HHPN----ILRLYNYFYDRR 148
Cdd:cd14135    2 YRVYGYLGKGVFSNVVRARDlARGNQEVAIKIIRNNELmHKAG-----LKELEILKKLndADPDdkkhCIRLLRHFEHKN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 149 RIYLILEYAPRG--ELYKELQKSCTFDEQRTATIMEELADALMYCHGKKVIHRDIKPENL-LLGLKGELKIADFGWSVHA 225
Cdd:cd14135   77 HLCLVFESLSMNlrEVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNIlVNEKKNTLKLCDFGSASDI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 927602445 226 ------PSLRRKTmcgtldYLPPEMIEGRMHNEKVDLWCIGVLCYELLVGNPPFESASHNETYRRIVKVDLKFP 293
Cdd:cd14135  157 geneitPYLVSRF------YRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFP 224
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
121-272 6.75e-08

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 53.04  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 121 QLRREIEIQAHLHHPNILRLYNYfyDRRRIYLILEYAPRGEL---YKELQKSCTF---DEQRTATIMEELADALMYCHGK 194
Cdd:cd14067   56 EFRQEASMLHSLQHPCIVYLIGI--SIHPLCFALELAPLGSLntvLEENHKGSSFmplGHMLTFKIAYQIAAGLAYLHKK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 195 KVIHRDIKPEN-----LLLGLKGELKIADFGWSVHAPSLRRKTMCGTLDYLPPEMIEGRMHNEKVDLWCIGVLCYELLVG 269
Cdd:cd14067  134 NIIFCDLKSDNilvwsLDVQEHINIKLSDYGISRQSFHEGALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSG 213

                 ...
gi 927602445 270 NPP 272
Cdd:cd14067  214 QRP 216
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
81-315 7.31e-08

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 52.61  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  81 RPLGKGKFGNVYLAREKKSHfIVALKVLFKSQIEKEGvehqLRREIEIQAHLHHPNILRLYNYFYDRRrIYLILEYAPRG 160
Cdd:cd14203    1 VKLGQGCFGEVWMGTWNGTT-KVAIKTLKPGTMSPEA----FLEEAQIMKKLRHDKLVQLYAVVSEEP-IYIVTEFMSKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 161 ELYKELQKSCTFDEQ--RTATIMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKIADFGWSVHAPSLRRKTMCGT-- 236
Cdd:cd14203   75 SLLDFLKDGEGKYLKlpQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAkf 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 237 -LDYLPPE-MIEGRMhNEKVDLWCIGVLCYELLV-GNPPFESASHNETYRRIVK-VDLKFPASVPMGAQDLISKLLRHNP 312
Cdd:cd14203  155 pIKWTAPEaALYGRF-TIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERgYRMPCPPGCPESLHELMCQCWRKDP 233

                 ...
gi 927602445 313 SER 315
Cdd:cd14203  234 EER 236
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
83-267 8.74e-08

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 52.71  E-value: 8.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445  83 LGKGKFGNVYlarekKSHF----------IVALKVLfKSQIEKEgVEHQLRREIEIQAHLHHPNILRLYNYFYDRRRIYL 152
Cdd:cd05091   14 LGEDRFGKVY-----KGHLfgtapgeqtqAVAIKTL-KDKAEGP-LREEFRHEAMLRSRLQHPNIVCLLGVVTKEQPMSM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 927602445 153 ILEYAPRGELYKEL------QKSCTFDEQRTAT----------IMEELADALMYCHGKKVIHRDIKPENLLLGLKGELKI 216
Cdd:cd05091   87 IFSYCSHGDLHEFLvmrsphSDVGSTDDDKTVKstlepadflhIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVKI 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 927602445 217 ADFGW--SVHAPSLrRKTMCGTL---DYLPPEMIEGRMHNEKVDLWCIGVLCYELL 267
Cdd:cd05091  167 SDLGLfrEVYAADY-YKLMGNSLlpiRWMSPEAIMYGKFSIDSDIWSYGVVLWEVF 221
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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