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Conserved domains on  [gi|505383238|ref|WP_015570340|]
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MULTISPECIES: serine/threonine-protein kinase [Enterobacter]

Protein Classification

serine/threonine protein kinase( domain architecture ID 11424655)

serine/threonine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to Bacillus subtilis serine/threonine-protein kinase YbdM

EC:  2.7.11.1
Gene Ontology:  GO:0004674|GO:0005524
PubMed:  3291115

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-477 2.19e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


:

Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 173.27  E-value: 2.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  19 RFNEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSslavRGEDMTLVLRserfgkafsaglnsFIQEARLLARFNH 98
Cdd:COG0515    5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPE----LAADPEARER--------------FRREARALARLNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  99 PNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLfGAIKTIHDEGYLHRDISLDNIQIQDNGL 178
Cdd:COG0515   67 PNIVRVYDVGEEDGRPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLA-EALAAAHAAGIVHRDIKPANILLTPDGR 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 179 PVLLDFGSARRTIGNLSDETETMLR-PGFAPIEQYTDDnesEQGPWTDIYALGAVLRTLIVGSPP-----PVSVVRSIQD 252
Cdd:COG0515  146 VKLIDFGIARALGGATLTQTGTVVGtPGYMAPEQARGE---PVDPRSDVYSLGVTLYELLTGRPPfdgdsPAELLRAHLR 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 253 TCKPLVELMPQGYSIPLLQAIDKALALHMEDRPQSIEEFAALIEMPVAGIDEVLTAKKTGTMLVPVEEETSASALDWRRY 332
Cdd:COG0515  223 EPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 333 KLPGLVAAGVLVGVVAGAMLFGGDSQETPAQTAQTPAVSPPAETSAQAETRPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:COG0515  303 AAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAA 382

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 413 LVYIRMLDGETLKVNGESKALRPGNNGYASLKLPAGETRIELEGNGRTRTQTLDIAKPGTWLVNP 477
Cdd:COG0515  383 AALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAA 447
 
Name Accession Description Interval E-value
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-477 2.19e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 173.27  E-value: 2.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  19 RFNEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSslavRGEDMTLVLRserfgkafsaglnsFIQEARLLARFNH 98
Cdd:COG0515    5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPE----LAADPEARER--------------FRREARALARLNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  99 PNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLfGAIKTIHDEGYLHRDISLDNIQIQDNGL 178
Cdd:COG0515   67 PNIVRVYDVGEEDGRPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLA-EALAAAHAAGIVHRDIKPANILLTPDGR 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 179 PVLLDFGSARRTIGNLSDETETMLR-PGFAPIEQYTDDnesEQGPWTDIYALGAVLRTLIVGSPP-----PVSVVRSIQD 252
Cdd:COG0515  146 VKLIDFGIARALGGATLTQTGTVVGtPGYMAPEQARGE---PVDPRSDVYSLGVTLYELLTGRPPfdgdsPAELLRAHLR 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 253 TCKPLVELMPQGYSIPLLQAIDKALALHMEDRPQSIEEFAALIEMPVAGIDEVLTAKKTGTMLVPVEEETSASALDWRRY 332
Cdd:COG0515  223 EPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 333 KLPGLVAAGVLVGVVAGAMLFGGDSQETPAQTAQTPAVSPPAETSAQAETRPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:COG0515  303 AAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAA 382

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 413 LVYIRMLDGETLKVNGESKALRPGNNGYASLKLPAGETRIELEGNGRTRTQTLDIAKPGTWLVNP 477
Cdd:COG0515  383 AALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAA 447
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 36-296 1.83e-44

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: 156.59  E-value: 1.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEfMPSSLAvrgEDMTLVLRserfgkafsaglnsFIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:cd14014   15 EVYRARDTLLGRPVAIKV-LRPELA---EDEEFRER--------------FLREARALARLSHPNIVRVYDVGEDDGRPY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 116 MGTLFYSGTTLS-RLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTigNL 194
Cdd:cd14014   77 IVMEYVEGGSLAdLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL--GD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 195 SDETET---MLRPGFAPIEQYTDDnesEQGPWTDIYALGAVLRTLIVGSPP-----PVSVVRSIQDTCKPLVELMPQGYS 266
Cdd:cd14014  153 SGLTQTgsvLGTPAYMAPEQARGG---PVDPRSDIYSLGVVLYELLTGRPPfdgdsPAAVLAKHLQEAPPPPSPLNPDVP 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 505383238 267 IPLLQAIDKALALHMEDRPQSIEEFAALIE 296
Cdd:cd14014  230 PALDAIILRALAKDPEERPQSAAELLAALR 259
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
16-293 5.25e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 5.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  16 VGYRFNE-FEIKEVIGGGGFGIVYRAWDHQLERTIAIKeFMPSSLAvrgEDMTLVLRserfgkafsaglnsFIQEARLLA 94
Cdd:NF033483   1 IGKLLGGrYEIGERIGRGGMAEVYLAKDTRLDRDVAVK-VLRPDLA---RDPEFVAR--------------FRREAQSAA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  95 RFNHPNLLHVLrfwvqnDTAYMGTLFY------SGTTLSR-LREEKPELINEAwIRRMLPMLfGAIKTIHDEGYLHRDIS 167
Cdd:NF033483  63 SLSHPNIVSVY------DVGEDGGIPYivmeyvDGRTLKDyIREHGPLSPEEA-VEIMIQIL-SALEHAHRNGIVHRDIK 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLrpG----FAPiEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP- 242
Cdd:NF033483 135 PQNILITKDGRVKVTDFGIARALSSTTMTQTNSVL--GtvhyLSP-EQARGGTVDAR---SDIYSLGIVLYEMLTGRPPf 208

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 243 ----PVSV-VRSIQDTCKPLVELMPqgySIPllQAID----KALALHMEDRPQSIEEFAA 293
Cdd:NF033483 209 dgdsPVSVaYKHVQEDPPPPSELNP---GIP--QSLDavvlKATAKDPDDRYQSAAEMRA 263
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 36-290 1.97e-20

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 90.28  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238    36 IVYRAWDHQLERTIAIKefmpsslavrgedmtlVLRSERFGKAfsagLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:smart00220  14 KVYLARDKKTGKLVAIK----------------VIKKKKIKKD----RERILREIKILKKLKHPNIVRLYDVFEDEDKLY 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238   116 MGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRtignLS 195
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRL-SEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ----LD 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238   196 DETETMLR---PGFAPIEQYTddneseQGPWT---DIYALGAVLRTLIVGSPP---PVSVVRSIQDTCKPLVELMPQGYS 266
Cdd:smart00220 149 PGEKLTTFvgtPEYMAPEVLL------GKGYGkavDIWSLGVILYELLTGKPPfpgDDQLLELFKKIGKPKPPFPPPEWD 222

                          250       260
                   ....*....|....*....|....*.
gi 505383238   267 IP--LLQAIDKALALHMEDRPqSIEE 290
Cdd:smart00220 223 ISpeAKDLIRKLLVKDPEKRL-TAEE 247
pknD PRK13184
serine/threonine-protein kinase PknD;
37-296 8.10e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 61.32  E-value: 8.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEfmpsslaVRgEDMTlvlRSERFGKafsaglnSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM 116
Cdd:PRK13184  18 VYLAYDPVCSRRVALKK-------IR-EDLS---ENPLLKK-------RFLREAKIAADLIHPGIVPVYSICSDGDPVYY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 117 GTLFYSGTTLSRLREE-------KPELINEAWIRRMLPMLF---GAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGS 186
Cdd:PRK13184  80 TMPYIEGYTLKSLLKSvwqkeslSKELAEKTSVGAFLSIFHkicATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 187 ARRTIGNLSDETE-----------TMLRPG--------FAPiEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPPpvsvV 247
Cdd:PRK13184 160 AIFKKLEEEDLLDidvdernicysSMTIPGkivgtpdyMAP-ERLLGVPASES---TDIYALGVILYQMLTLSFP----Y 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 248 R-------SIQDTCKPLVELMPQGYSIPLLQAID-KALALHMEDRPQSIEEFAALIE 296
Cdd:PRK13184 232 RrkkgrkiSYRDVILSPIEVAPYREIPPFLSQIAmKALAVDPAERYSSVQELKQDLE 288
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 85-209 5.44e-06

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: 47.88  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238   85 SFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGT-LFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:pfam07714  47 DFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTeYMPGGDLLDFLRKHKRKL-TLKDLLSMALQIAKGMEYLESKNFVH 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 505383238  164 RDISLDNIQIQDNGLPVLLDFGSArRTIgnLSDETETMLRPGFAPI 209
Cdd:pfam07714 126 RDLAARNCLVSENLVVKISDFGLS-RDI--YDDDYYRKRGGGKLPI 168
 
Name Accession Description Interval E-value
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
19-477 2.19e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 173.27  E-value: 2.19e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  19 RFNEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSslavRGEDMTLVLRserfgkafsaglnsFIQEARLLARFNH 98
Cdd:COG0515    5 LLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPE----LAADPEARER--------------FRREARALARLNH 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  99 PNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLfGAIKTIHDEGYLHRDISLDNIQIQDNGL 178
Cdd:COG0515   67 PNIVRVYDVGEEDGRPYLVMEYVEGESLADLLRRRGPLPPAEALRILAQLA-EALAAAHAAGIVHRDIKPANILLTPDGR 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 179 PVLLDFGSARRTIGNLSDETETMLR-PGFAPIEQYTDDnesEQGPWTDIYALGAVLRTLIVGSPP-----PVSVVRSIQD 252
Cdd:COG0515  146 VKLIDFGIARALGGATLTQTGTVVGtPGYMAPEQARGE---PVDPRSDVYSLGVTLYELLTGRPPfdgdsPAELLRAHLR 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 253 TCKPLVELMPQGYSIPLLQAIDKALALHMEDRPQSIEEFAALIEMPVAGIDEVLTAKKTGTMLVPVEEETSASALDWRRY 332
Cdd:COG0515  223 EPPPPPSELRPDLPPALDAIVLRALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 333 KLPGLVAAGVLVGVVAGAMLFGGDSQETPAQTAQTPAVSPPAETSAQAETRPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:COG0515  303 AAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAAAAAAAAAAAAAAAAAAAAAA 382

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 413 LVYIRMLDGETLKVNGESKALRPGNNGYASLKLPAGETRIELEGNGRTRTQTLDIAKPGTWLVNP 477
Cdd:COG0515  383 AALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAARLLAA 447
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 36-296 1.83e-44

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: 156.59  E-value: 1.83e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEfMPSSLAvrgEDMTLVLRserfgkafsaglnsFIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:cd14014   15 EVYRARDTLLGRPVAIKV-LRPELA---EDEEFRER--------------FLREARALARLSHPNIVRVYDVGEDDGRPY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 116 MGTLFYSGTTLS-RLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTigNL 194
Cdd:cd14014   77 IVMEYVEGGSLAdLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARAL--GD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 195 SDETET---MLRPGFAPIEQYTDDnesEQGPWTDIYALGAVLRTLIVGSPP-----PVSVVRSIQDTCKPLVELMPQGYS 266
Cdd:cd14014  153 SGLTQTgsvLGTPAYMAPEQARGG---PVDPRSDIYSLGVVLYELLTGRPPfdgdsPAAVLAKHLQEAPPPPSPLNPDVP 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 505383238 267 IPLLQAIDKALALHMEDRPQSIEEFAALIE 296
Cdd:cd14014  230 PALDAIILRALAKDPEERPQSAAELLAALR 259
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 37-233 1.54e-27

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: 109.28  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEFMPSSlavrgedmtlvlrserfgkaFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM 116
Cdd:cd00180    9 VYKARDKETGKKVAVKVIPKEK--------------------LKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 117 GTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRtIGNLSD 196
Cdd:cd00180   69 VMEYCEGGSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKD-LDSDDS 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 505383238 197 ETETMLRPGFAPIEQYTDDNESEQGPWTDIYALGAVL 233
Cdd:cd00180  148 LLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVIL 184
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
16-293 5.25e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 5.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  16 VGYRFNE-FEIKEVIGGGGFGIVYRAWDHQLERTIAIKeFMPSSLAvrgEDMTLVLRserfgkafsaglnsFIQEARLLA 94
Cdd:NF033483   1 IGKLLGGrYEIGERIGRGGMAEVYLAKDTRLDRDVAVK-VLRPDLA---RDPEFVAR--------------FRREAQSAA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  95 RFNHPNLLHVLrfwvqnDTAYMGTLFY------SGTTLSR-LREEKPELINEAwIRRMLPMLfGAIKTIHDEGYLHRDIS 167
Cdd:NF033483  63 SLSHPNIVSVY------DVGEDGGIPYivmeyvDGRTLKDyIREHGPLSPEEA-VEIMIQIL-SALEHAHRNGIVHRDIK 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLrpG----FAPiEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP- 242
Cdd:NF033483 135 PQNILITKDGRVKVTDFGIARALSSTTMTQTNSVL--GtvhyLSP-EQARGGTVDAR---SDIYSLGIVLYEMLTGRPPf 208

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 243 ----PVSV-VRSIQDTCKPLVELMPqgySIPllQAID----KALALHMEDRPQSIEEFAA 293
Cdd:NF033483 209 dgdsPVSVaYKHVQEDPPPPSELNP---GIP--QSLDavvlKATAKDPDDRYQSAAEMRA 263
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
 36-290 1.97e-20

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 90.28  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238    36 IVYRAWDHQLERTIAIKefmpsslavrgedmtlVLRSERFGKAfsagLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:smart00220  14 KVYLARDKKTGKLVAIK----------------VIKKKKIKKD----RERILREIKILKKLKHPNIVRLYDVFEDEDKLY 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238   116 MGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRtignLS 195
Cdd:smart00220  74 LVMEYCEGGDLFDLLKKRGRL-SEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ----LD 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238   196 DETETMLR---PGFAPIEQYTddneseQGPWT---DIYALGAVLRTLIVGSPP---PVSVVRSIQDTCKPLVELMPQGYS 266
Cdd:smart00220 149 PGEKLTTFvgtPEYMAPEVLL------GKGYGkavDIWSLGVILYELLTGKPPfpgDDQLLELFKKIGKPKPPFPPPEWD 222

                          250       260
                   ....*....|....*....|....*.
gi 505383238   267 IP--LLQAIDKALALHMEDRPqSIEE 290
Cdd:smart00220 223 ISpeAKDLIRKLLVKDPEKRL-TAEE 247
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
 22-242 1.26e-17

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: 82.25  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  22 EFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSSLAVRgedmtlvlrserfgkafsaglNSFIQEARLLARFNHPNL 101
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKK---------------------ESILNEIAILKKCKHPNI 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 102 LHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWI----RRMLPmlfgAIKTIHDEGYLHRDISLDNIQIQDNG 177
Cdd:cd05122   60 VKYYGSYLKKDELWIVMEFCSGGSLKDLLKNTNKTLTEQQIayvcKEVLK----GLEYLHSHGIIHRDIKAANILLTSDG 135

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 178 LPVLLDFGSArrTIGNLSDETETML-RPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd05122  136 EVKLIDFGLS--AQLSDGKTRNTFVgTPYWMAPEVIQGKPYGFK---ADIWSLGITAIEMAEGKPP 196
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 87-238 4.64e-15

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: 75.02  E-value: 4.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNllhVLRF---WVQNDTAYMGTLFYSGTTL-----SRLREEKpELINEAWirRMLPMLFGAIKTIHD 158
Cdd:cd13996   52 LREVKALAKLNHPN---IVRYytaWVEEPPLYIQMELCEGGTLrdwidRRNSSSK-NDRKLAL--ELFKQILKGVSYIHS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 EGYLHRDISLDNIQIQ-DNGLPVLLDFGSARRtIGNLSDETETMLRPGFAPIEQYTD--------DNESEQGPW----TD 225
Cdd:cd13996  126 KGIVHRDLKPSNIFLDnDDLQVKIGDFGLATS-IGNQKRELNNLNNNNNGNTSNNSVgigtplyaSPEQLDGENynekAD 204

                        170
                 ....*....|...
gi 505383238 226 IYALGAVLRTLIV 238
Cdd:cd13996  205 IYSLGIILFEMLH 217
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
 89-285 2.51e-14

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: 73.10  E-value: 2.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQND-----TAYMGTLFYSGTTLS---RLREEKPELINEAWIRRMLPMLFGAIKTIHDE- 159
Cdd:cd13986   47 EIENYRLFNHPNILRLLDSQIVKEaggkkEVYLLLPYYKRGSLQdeiERRLVKGTFFPEDRILHIFLGICRGLKAMHEPe 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 160 --GYLHRDISLDNIQIQDNGLPVLLDFGS---ARRTIGN------LSDETE---TMlrPGFAPiEQYTDDNESEQGPWTD 225
Cdd:cd13986  127 lvPYAHRDIKPGNVLLSEDDEPILMDLGSmnpARIEIEGrrealaLQDWAAehcTM--PYRAP-ELFDVKSHCTIDEKTD 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 226 IYALGAVLRTLIVGSPP---------PVSVVRsiqdtCKPLVELMPQ-GYSIPLLQAIDKALALHMEDRP 285
Cdd:cd13986  204 IWSLGCTLYALMYGESPferifqkgdSLALAV-----LSGNYSFPDNsRYSEELHQLVKSMLVVNPAERP 268
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
 37-285 9.20e-13

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 67.93  E-value: 9.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEFmpsslavrgedmtlvlrseRFGKAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM 116
Cdd:cd06606   16 VYLALNLDTGELMAVKEV-------------------ELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 117 GTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSD 196
Cdd:cd06606   77 FLEYVPGGSLASLLKKFGKL-PEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 197 ETETMLR--PGF-AP--IEQytddneSEQGPWTDIYALGAVLRTLIVGSPP------PVSVVRSIQDTCKPLVelMPQGY 265
Cdd:cd06606  156 EGTKSLRgtPYWmAPevIRG------EGYGRAADIWSLGCTVIEMATGKPPwselgnPVAALFKIGSSGEPPP--IPEHL 227

                        250       260
                 ....*....|....*....|
gi 505383238 266 SIPLLQAIDKALALHMEDRP 285
Cdd:cd06606  228 SEEAKDFLRKCLQRDPKKRP 247
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 65-287 1.59e-12

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: 67.31  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  65 DMTLVLRSERFGKAFSAGLNSFiQEARLLARFNHPNLLHVLRFWVQNDTAYMgTLFY--SGTTLSRLREEKPELINEAWI 142
Cdd:cd08219   25 DQKYAMKEIRLPKSSSAVEDSR-KEAVLLAKMKHPNIVAFKESFEADGHLYI-VMEYcdGGDLMQKIKLQRGKLFPEDTI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 143 RRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYtddnesEQGP 222
Cdd:cd08219  103 LQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTYVGTPYYVPPEIW------ENMP 176

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 223 W---TDIYALGAVLRTLIVGSPP--PVSVVRSIQDTCKPLVELMPQGYSIPLLQAIDKALALHMEDRPQS 287
Cdd:cd08219  177 YnnkSDIWSLGCILYELCTLKHPfqANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRNPRSRPSA 246
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 89-242 2.82e-12

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: 66.94  E-value: 2.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISL 168
Cdd:cd06626   49 EMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLEELLRHG-RILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKP 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 169 DNIQIQDNGLPVLLDFGSARRtignLSDETeTMLRPG-----------FAPiEQYTDDNESEQGPWTDIYALGAVLRTLI 237
Cdd:cd06626  128 ANIFLDSNGLIKLGDFGSAVK----LKNNT-TTMAPGevnslvgtpayMAP-EVITGNKGEGHGRAADIWSLGCVVLEMA 201


                 ....*
gi 505383238 238 VGSPP 242
Cdd:cd06626  202 TGKRP 206
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 81-294 3.46e-12

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: 66.53  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  81 AGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTaymGTLFY----SGTTLSRLRE--EKPELineAWIRRmLPMLFG--- 151
Cdd:cd14066   32 ASKKEFLTELEMLGRLRHPNLVRLLGYCLESDE---KLLVYeympNGSLEDRLHChkGSPPL---PWPQR-LKIAKGiar 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 152 AIKTIHDEGYL---HRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLR--PGFAPIEQYTDDNESEQgpwTDI 226
Cdd:cd14066  105 GLEYLHEECPPpiiHGDIKSSNILLDEDFEPKLTDFGLARLIPPSESVSKTSAVKgtIGYLAPEYIRTGRVSTK---SDV 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383238 227 YALGAVLRTLIVGSpPPVSVVRSIQDTcKPLVELMPQGYSIPLLQAIDKALALHMEDRPQSIEEFAAL 294
Cdd:cd14066  182 YSFGVVLLELLTGK-PAVDENRENASR-KDLVEWVESKGKEELEDILDKRLVDDDGVEEEEVEALLRL 247
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
 21-241 9.60e-12

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: 65.42  E-value: 9.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  21 NEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSslavrgEDMTLVLRSErfgkafsaglnsfIQEARLLARFNHPN 100
Cdd:cd07833    1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKES------EDDEDVKKTA-------------LREVKVLRQLRHEN 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 101 LLHVLRFWVQNDTAYMgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPV 180
Cdd:cd07833   62 IVNLKEAFRRKGRLYL-VFEYVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLK 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 181 LLDFGSAR----RTIGNLSDETETmlRPGFAPiEQYTDDneSEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd07833  141 LCDFGFARaltaRPASPLTDYVAT--RWYRAP-ELLVGD--TNYGKPVDVWAIGCIMAELLDGEP 200
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
 87-290 9.99e-12

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: 65.10  E-value: 9.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGT-LFYSGTTLSRLREEKPeLINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd14004   56 IHILDTLNKRSHPNIVKLLDFFEDDEFYYLVMeKHGSGMDLFDFIERKP-NMDEKEAKYIFRQVADAVKHLHDQGIVHRD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSA-----------RRTIGNLSDEtetMLRpgfapieqytddNESEQGPWTDIYALGAVLR 234
Cdd:cd14004  135 IKDENVILDGNGTIKLIDFGSAayiksgpfdtfVGTIDYAAPE---VLR------------GNPYGGKEQDIWALGVLLY 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 235 TLIVGSPPPVSVVRSIQDTCKPLVELMPQgysipLLQAIDKALALHMEDRPqSIEE 290
Cdd:cd14004  200 TLVFKENPFYNIEEILEADLRIPYAVSED-----LIDLISRMLNRDVGDRP-TIEE 249
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
 20-242 6.00e-11

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: 62.76  E-value: 6.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  20 FNEFEIKEVIGGGGFGIVYRAwdhqLERTIAiKEFmpsslAVRGEDMTLVLRSERFGKAFsagLNSFIQEARLLARFN-H 98
Cdd:cd14093    2 YAKYEPKEILGRGVSSTVRRC----IEKETG-QEF-----AVKIIDITGEKSSENEAEEL---REATRREIEILRQVSgH 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  99 PNLLHVLRFWvqNDTAYM---------GTLFYSGTTLSRLREEKpelineawIRRMLPMLFGAIKTIHDEGYLHRDISLD 169
Cdd:cd14093   69 PNIIELHDVF--ESPTFIflvfelcrkGELFDYLTEVVTLSEKK--------TRRIMRQLFEAVEFLHSLNIVHRDLKPE 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 170 NIQIQDNGLPVLLDFGSARRTignlsDETETmLR-----PGF-AP--IEQYTDDNESEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd14093  139 NILLDDNLNVKISDFGFATRL-----DEGEK-LRelcgtPGYlAPevLKCSMYDNAPGYGKEVDMWACGVIMYTLLAGCP 212


                 .
gi 505383238 242 P 242
Cdd:cd14093  213 P 213
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
 87-299 6.96e-11

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: 62.48  E-value: 6.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRL---REEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd08215   47 LNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDLAQKikkQKKKGQPFPEEQILDWFVQICLALKYLHSRKILH 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSArRTIGNLSDETETMLrpG----FAPiEQYTD---DNESeqgpwtDIYALGAVLRTL 236
Cdd:cd08215  127 RDLKTQNIFLTKDGVVKLGDFGIS-KVLESTTDLAKTVV--GtpyyLSP-ELCENkpyNYKS------DIWALGCVLYEL 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 237 IVGSPP------PVSVVRSIQDTCKPLvelmPQGYSIPLLQAIDKALALHMEDRPqSIEEfaaLIEMPV 299
Cdd:cd08215  197 CTLKHPfeannlPALVYKIVKGQYPPI----PSQYSSELRDLVNSMLQKDPEKRP-SANE---ILSSPF 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
 87-285 2.12e-10

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: 61.25  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRL---REEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd08530   47 VNEIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDLSKLiskRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILH 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARRTIGNLSD-ETETmlrPGFAPIEQYTDDneseqgPWT---DIYALGAVLRTLIVG 239
Cdd:cd08530  127 RDLKSANILLSAGDLVKIGDLGISKVLKKNLAKtQIGT---PLYAAPEVWKGR------PYDyksDIWSLGCLLYEMATF 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 505383238 240 SPPPVSvvRSIQD----TCKPLVELMPQGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd08530  198 RPPFEA--RTMQElrykVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRP 245
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 88-285 2.18e-10

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: 61.13  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL-SRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd08225   48 KEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGDLmKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDI 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQDNGLPVLL-DFGSARRtignLSDETETMLRPGFAPIeqYTDDNESEQGPW---TDIYALGAVLRTLIVGSPP 242
Cdd:cd08225  128 KSQNIFLSKNGMVAKLgDFGIARQ----LNDSMELAYTCVGTPY--YLSPEICQNRPYnnkTDIWSLGCVLYELCTLKHP 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 505383238 243 --PVSVVRSIQDTCKPLVELMPQGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd08225  202 feGNNLHQLVLKICQGYFAPISPNFSRDLRSLISQLFKVSPRDRP 246
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 77-241 2.91e-10

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: 60.71  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  77 KAFSAGLNSFIQEARLLARFN----HPNLLHVLR--FWVQNDTAYMgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLF 150
Cdd:cd05118   33 KNDFRHPKAALREIKLLKHLNdvegHPNIVKLLDvfEHRGGNHLCL-VFELMGMNLYELIKDYPRGLPLDLIKSYLYQLL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 151 GAIKTIHDEGYLHRDISLDNIQI-QDNGLPVLLDFGSARRTIGNLSDETET--MLRpgfAP--IEQYTDDNESeqgpwTD 225
Cdd:cd05118  112 QALDFLHSNGIIHRDLKPENILInLELGQLKLADFGLARSFTSPPYTPYVAtrWYR---APevLLGAKPYGSS-----ID 183

                        170
                 ....*....|....*.
gi 505383238 226 IYALGAVLRTLIVGSP 241
Cdd:cd05118  184 IWSLGCILAELLTGRP 199
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
 35-291 3.09e-10

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: 60.31  E-value: 3.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  35 GIVYRAWDHQLERTIAIKEFMPSSLAvrgedmtlvlrserfgKAFSAGLNSfiqEARLLARFNHPNLLHVLRFWVQNDTA 114
Cdd:cd14009    7 ATVWKGRHKQTGEVVAIKEISRKKLN----------------KKLQENLES---EIAILKSIKHPNIVRLYDVQKTEDFI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 115 YMGTLFYSGTTLSR-LREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNG-LPVL--LDFGSARrt 190
Cdd:cd14009   68 YLVLEYCAGGDLSQyIRKRG--RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGdDPVLkiADFGFAR-- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 191 igNLSDET--ET-------MlrpgfAP-IEQYTDDNESeqgpwTDIYALGAVLRTLIVGSPP-----PVSVVRSIQDTCK 255
Cdd:cd14009  144 --SLQPASmaETlcgsplyM-----APeILQFQKYDAK-----ADLWSVGAILFEMLVGKPPfrgsnHVQLLRNIERSDA 211

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 505383238 256 PLVELMPQGYSIPLLQAIDKALALHMEDRpQSIEEF 291
Cdd:cd14009  212 VIPFPIAAQLSPDCKDLLRRLLRRDPAER-ISFEEF 246
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
 88-285 3.96e-10

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 60.41  E-value: 3.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpELINEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd14188   50 KEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKAR-KVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGSARRtIGNLSDETETML-RPGFAPIEQYtddNESEQGPWTDIYALGAVLRTLIVGSPPPVSV 246
Cdd:cd14188  129 LGNFFINENMELKVGDFGLAAR-LEPLEHRRRTICgTPNYLSPEVL---NKQGHGCESDIWALGCVMYTMLLGRPPFETT 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 505383238 247 vrSIQDTCKPLVEL---MPQGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd14188  205 --NLKETYRCIREArysLPSSLLAPAKHLIASMLSKNPEDRP 244
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
 36-241 5.31e-10

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: 60.19  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEF--------MPSSlAVRgedmtlvlrserfgkafsaglnsfiqEARLLARFNHPNLLHVLRF 107
Cdd:cd07829   14 VVYKAKDKKTGEIVALKKIrldneeegIPST-ALR--------------------------EISLLKELKHPNIVKLLDV 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 108 WVQNDTAYMgtLF-YSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGS 186
Cdd:cd07829   67 IHTENKLYL--VFeYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGL 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383238 187 ArRTIGNlsdetetmlrpgfaPIEQYTDD-------------NESEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd07829  145 A-RAFGI--------------PLRTYTHEvvtlwyrapeillGSKHYSTAVDIWSVGCIFAELITGKP 197
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
 50-242 7.48e-10

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: 59.49  E-value: 7.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  50 AIKEFMPSSLAVRgedmtlvLRSERFGKAFSAGLNSFIQEARLLARFNHPNL--LH-VLRFwVQNDTAYMgTLFY--SGT 124
Cdd:cd14008   22 AIKIFNKSRLRKR-------REGKNDRGKIKNALDDVRREIAIMKKLDHPNIvrLYeVIDD-PESDKLYL-VLEYceGGP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 125 TLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRtignLSDETETMLR- 203
Cdd:cd14008   93 VMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEM----FEDGNDTLQKt 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 505383238 204 ---PGFAPIEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14008  169 agtPAFLAPELCDGDSKTYSGKAADIWALGVTLYCLVFGRLP 210
pknD PRK13184
serine/threonine-protein kinase PknD;
37-296 8.10e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 61.32  E-value: 8.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEfmpsslaVRgEDMTlvlRSERFGKafsaglnSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM 116
Cdd:PRK13184  18 VYLAYDPVCSRRVALKK-------IR-EDLS---ENPLLKK-------RFLREAKIAADLIHPGIVPVYSICSDGDPVYY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 117 GTLFYSGTTLSRLREE-------KPELINEAWIRRMLPMLF---GAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGS 186
Cdd:PRK13184  80 TMPYIEGYTLKSLLKSvwqkeslSKELAEKTSVGAFLSIFHkicATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 187 ARRTIGNLSDETE-----------TMLRPG--------FAPiEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPPpvsvV 247
Cdd:PRK13184 160 AIFKKLEEEDLLDidvdernicysSMTIPGkivgtpdyMAP-ERLLGVPASES---TDIYALGVILYQMLTLSFP----Y 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 248 R-------SIQDTCKPLVELMPQGYSIPLLQAID-KALALHMEDRPQSIEEFAALIE 296
Cdd:PRK13184 232 RrkkgrkiSYRDVILSPIEVAPYREIPPFLSQIAmKALAVDPAERYSSVQELKQDLE 288
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
 23-242 9.62e-10

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: 59.29  E-value: 9.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKefmpsslavrgedmtLVLRSERFGKAFSAGLNS-FIQEARLLARF-NHPN 100
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIK---------------CLYKSGPNSKDGNDFQKLpQLREIDLHRRVsRHPN 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 101 LLHVLRFWVQNDTAYM-------GTLFYSgTTLSRLREEKPELineawIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQI 173
Cdd:cd13993   67 IITLHDVFETEVAIYIvleycpnGDLFEA-ITENRIYVGKTEL-----IKNVFLQLIDAVKHCHSLGIYHRDIKPENILL 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 174 QDNGLPV-LLDFGSArrtignLSDETETMLRPG----FAPiEQYTDDNESEQGPWT---DIYALGAVLRTLIVGSPP 242
Cdd:cd13993  141 SQDEGTVkLCDFGLA------TTEKISMDFGVGsefyMAP-ECFDEVGRSLKGYPCaagDIWSLGIILLNLTFGRNP 210
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
 87-241 1.20e-09

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: 59.36  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLrEEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd07846   48 MREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVLDDL-EKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSARrtignlsdeteTMLRPGfapiEQYTDD-------------NESEQGPWTDIYALGAVL 233
Cdd:cd07846  127 KPENILVSQSGVVKLCDFGFAR-----------TLAAPG----EVYTDYvatrwyrapellvGDTKYGKAVDVWAVGCLV 191


                 ....*...
gi 505383238 234 RTLIVGSP 241
Cdd:cd07846  192 TEMLTGEP 199
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 98-289 1.32e-09

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: 59.05  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  98 HPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRL---REEKPELINEAWIRRMLPMLFGAIKTIHDE-GYLHRDISLDNIQI 173
Cdd:cd08528   68 HPNIVRYYKTFLENDRLYIVMELIEGAPLGEHfssLKEKNEHFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIML 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 174 QDNGLPVLLDFGSARRTIGNLSDETE---TMLR--PGFAPIEQYTDDneseqgpwTDIYALGAVLRTLIVGSPPPVS--- 245
Cdd:cd08528  148 GEDDKVTITDFGLAKQKGPESSKMTSvvgTILYscPEIVQNEPYGEK--------ADIWALGCILYQMCTLQPPFYStnm 219

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505383238 246 ---VVRSIQDTCKPLVELMpqgYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd08528  220 ltlATKIVEAEYEPLPEGM---YSDDITFVIRSCLTPDPEARPDIVE 263
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
 22-285 1.59e-09

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: 58.58  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  22 EFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFmpsslavrgeDMTLVLRSERfgkafsaglNSFIQEARLLARFNHPnl 101
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQI----------DISRMSRKMR---------EEAIDEARVLSKLNSP-- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 102 lHVLRFW---VQNDTAYMGTLFYSGTTL-SRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIqDNG 177
Cdd:cd08529   60 -YVIKYYdsfVDKGKLNIVMEYAENGDLhSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFL-DKG 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 178 LPVLL-DFGSArRTIGNLSDETETMLRPGFapieqYTDDNESEQGPW---TDIYALGAVLRTLIVGSPP-----PVSVVR 248
Cdd:cd08529  138 DNVKIgDLGVA-KILSDTTNFAQTIVGTPY-----YLSPELCEDKPYnekSDVWALGCVLYELCTGKHPfeaqnQGALIL 211

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 505383238 249 SI-QDTCKPLvelmPQGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd08529  212 KIvRGKYPPI----SASYSQDLSQLIDSCLTKDYRQRP 245
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
 36-268 1.78e-09

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: 58.54  E-value: 1.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEFMPSslavrgEDMTLVLRSErfgkafsaglnsfIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:cd07847   16 VVFKCRNRETGQIVAIKKFVES------EDDPVIKKIA-------------LREIRMLKQLKHPNLVNLIEVFRRKRKLH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 116 MGTLFYSGTTLSRLrEEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIG--- 192
Cdd:cd07847   77 LVFEYCDHTVLNEL-EKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGpgd 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 193 NLSDETETmlRPGFAPiEQYTDDneSEQGPWTDIYALGAVLRTLIVGSP--PPVSVVRSIQDTCKPLVELMPQ------- 263
Cdd:cd07847  156 DYTDYVAT--RWYRAP-ELLVGD--TQYGPPVDVWAIGCVFAELLTGQPlwPGKSDVDQLYLIRKTLGDLIPRhqqifst 230

                        250
                 ....*....|
gi 505383238 264 -----GYSIP 268
Cdd:cd07847  231 nqffkGLSIP 240
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
 37-257 1.85e-09

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


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 58.39  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEfmpsslavrgedmtlvLRSERFGKAFsagLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM 116
Cdd:cd06627   16 VYKGLNLNTGEFVAIKQ----------------ISLEKIPKSD---LKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 117 GTLFY-SGTTLSRLR--EEKPELINEAWIRRMLPMLfgaiKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGN 193
Cdd:cd06627   77 ILEYVeNGSLASIIKkfGKFPESLVAVYIYQVLEGL----AYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 194 LSDETETMLRPGF-AP--IEQytddneseQGPWT--DIYALGAVLRTLIVGSPP-----PVSVV-RSIQDTCKPL 257
Cdd:cd06627  153 EKDENSVVGTPYWmAPevIEM--------SGVTTasDIWSVGCTVIELLTGNPPyydlqPMAALfRIVQDDHPPL 219
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
 23-242 2.00e-09

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 58.08  E-value: 2.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKefmpsslavrgedmtlvLRSERfgKAFSAGLNSFI-QEARLLARFNHPNL 101
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIK-----------------IVSKK--KAPEDYLQKFLpREIEVIKGLKHPNL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 102 LHVL-------RFWVQNDTAYMGTLfysgttLSRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQ 174
Cdd:cd14162   63 ICFYeaiettsRVYIIMELAENGDL------LDYIRKNG--ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLD 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 175 DNGLPVLLDFGSARRTIgnLSDETETMLRPGF------APIE-----QYtddneseQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14162  135 KNNNLKITDFGFARGVM--KTKDGKPKLSETYcgsyayASPEilrgiPY-------DPFLSDIWSMGVVLYTMVYGRLP 204
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
 22-190 2.25e-09

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: 58.53  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  22 EFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEfmpsslaVRGEDmtlvlrsERFGKAFSAglnsfIQEARLLARFNHPNL 101
Cdd:cd07845    8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALKK-------VRMDN-------ERDGIPISS-----LREITLLLNLRHPNI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 102 LHVLRFWVQNdtaYMGTLF----YSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNG 177
Cdd:cd07845   69 VELKEVVVGK---HLDSIFlvmeYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG 145

                        170
                 ....*....|...
gi 505383238 178 LPVLLDFGSARRT 190
Cdd:cd07845  146 CLKIADFGLARTY 158
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
 86-209 2.84e-09

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: 57.56  E-value: 2.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238    86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELINeawIRRMLPMLFGAIKT---IHDEGY 161
Cdd:smart00221  48 FLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMPgGDLLDYLRKNRPKELS---LSDLLSFALQIARGmeyLESKNF 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 505383238   162 LHRDISLDNIQIQDNGLPVLLDFGSARrtigNLSDETETMLRPGFAPI 209
Cdd:smart00221 125 IHRDLAARNCLVGENLVVKISDFGLSR----DLYDDDYYKVKGGKLPI 168
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
 88-242 3.81e-09

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: 57.48  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLR-FWVQNDTAYMGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd14165   50 RELEILARLNHKSIIKTYEiFETSDGKVYIVMELGVQGDLLEFIKLRGAL-PEDVARKMFHQLSSAIKYCHELDIVHRDL 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIqIQDNGLPVLL-DFGSARRTigNLSDETETMLRPGFAPIEQYTDDNESEQGPW----TDIYALGAVLRTLIVGSP 241
Cdd:cd14165  129 KCENL-LLDKDFNIKLtDFGFSKRC--LRDENGRIVLSKTFCGSAAYAAPEVLQGIPYdpriYDIWSLGVILYIMVCGSM 205


                 .
gi 505383238 242 P 242
Cdd:cd14165  206 P 206
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
 91-242 4.24e-09

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 57.35  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  91 RLLAR-------FNHPNLLHVL-------RFWVQNDTAYMGTLFYSGTTLSRLREEkpelinEAwiRRMLPMLFGAIKTI 156
Cdd:cd14075   46 RLLSReissmekLHHPNIIRLYevvetlsKLHLVMEYASGGELYTKISTEGKLSES------EA--KPLFAQIVSAVKHM 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 157 HDEGYLHRDISLDNIQIQDNGLPVLLDFGSArrTIGNLSDETETML-RPGFAPIEQYTDDNESeqGPWTDIYALGAVLRT 235
Cdd:cd14075  118 HENNIIHRDLKAENVFYASNNCVKVGDFGFS--THAKRGETLNTFCgSPPYAAPELFKDEHYI--GIYVDIWALGVLLYF 193


                 ....*..
gi 505383238 236 LIVGSPP 242
Cdd:cd14075  194 MVTGVMP 200
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
 22-289 4.83e-09

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 57.10  E-value: 4.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  22 EFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSSLAVRGEDMTLVLRserfgkafsaglnsfiqEARLLARFNHPNL 101
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQR-----------------EINILKSLEHPGI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 102 LHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPElINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGlPVL 181
Cdd:cd14098   64 VRLIDWYEDDQHIYLVMEYVEGGDLMDFIMAWGA-IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDD-PVI 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 182 L---DFGSARRTIGNlsdeteTMLR-----PGFAPIEQYTDDNESEQGPWT---DIYALGAVLRTLIVGSPPPVSvvrsi 250
Cdd:cd14098  142 VkisDFGLAKVIHTG------TFLVtfcgtMAYLAPEILMSKEQNLQGGYSnlvDMWSVGCLVYVMLTGALPFDG----- 210

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 505383238 251 qDTCKPLVELMPQG-YSIPLL-------QAID---KALALHMEDRPQSIE 289
Cdd:cd14098  211 -SSQLPVEKRIRKGrYTQPPLvdfniseEAIDfilRLLDVDPEKRMTAAQ 259
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
 86-242 6.15e-09

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: 56.76  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYM-------GTLFysgttlSRLREEKPelINEAWIRRMLPMLFGAIKTIHD 158
Cdd:cd14003   46 IKREIEIMKLLNHPNIIKLYEVIETENKIYLvmeyasgGELF------DYIVNNGR--LSEDEARRFFQQLISAVDYCHS 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 EGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNlsdeteTMLR-----PGFAPIEQYtdDNESEQGPWTDIYALGAVL 233
Cdd:cd14003  118 NGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGG------SLLKtfcgtPAYAAPEVL--LGRKYDGPKADVWSLGVIL 189


                 ....*....
gi 505383238 234 RTLIVGSPP 242
Cdd:cd14003  190 YAMLTGYLP 198
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 19-289 6.49e-09

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: 56.81  E-value: 6.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  19 RF-NEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEF-MPSSLAVRGEdmtlVLRserfgkafsaglnsfiqEARLLARF 96
Cdd:cd14048    3 RFlTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIrLPNNELAREK----VLR-----------------EVRALAKL 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  97 NHPNLLHVLRFWVQN---------DTAYMgtlfYSGTTLSRlreeKPELinEAWIRRMLPM--------------LFGAI 153
Cdd:cd14048   62 DHPGIVRYFNAWLERppegwqekmDEVYL----YIQMQLCR----KENL--KDWMNRRCTMesrelfvclnifkqIASAV 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 154 KTIHDEGYLHRDI-------SLDN-IQIQDNGLPVLLDFGSARRTIGNLSDETETML-----RPGFAPiEQYTDDNESEQ 220
Cdd:cd14048  132 EYLHSKGLIHRDLkpsnvffSLDDvVKVGDFGLVTAMDQGEPEQTVLTPMPAYAKHTgqvgtRLYMSP-EQIHGNQYSEK 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 221 gpwTDIYALGAVLRTLIVGSPPPVSVVRSIQDTCK---PLV--ELMPQGYSIpllqaIDKALALHMEDRPQSIE 289
Cdd:cd14048  211 ---VDIFALGLILFELIYSFSTQMERIRTLTDVRKlkfPALftNKYPEERDM-----VQQMLSPSPSERPEAHE 276
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
 86-242 8.46e-09

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: 56.74  E-value: 8.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDT-AYMGTLFYSGTTLSRL--REEKPELineAWIRRmLPMLFGA---IKTIHDE 159
Cdd:cd14158   61 FEQEIQVMAKCQHENLVELLGYSCDGPQlCLVYTYMPNGSLLDRLacLNDTPPL---SWHMR-CKIAQGTangINYLHEN 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 160 GYLHRDISLDNIQIQDNGLPVLLDFGSARRTI-GNLSDETETMLRPG--FAPiEQYtddnESEQGPWTDIYALGAVLRTL 236
Cdd:cd14158  137 NHIHRDIKSANILLDETFVPKISDFGLARASEkFSQTIMTERIVGTTayMAP-EAL----RGEITPKSDIFSFGVVLLEI 211


                 ....*.
gi 505383238 237 IVGSPP 242
Cdd:cd14158  212 ITGLPP 217
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
 37-261 1.01e-08

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: 56.01  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRA-WdhqLERTIAIKEFMPSSLAVRGEDMtlvlrserfgkafsaglnsFIQEARLLARFNHPNllhVLRF--WVQND- 112
Cdd:cd13999    9 VYKGkW---RGTDVAIKKLKVEDDNDELLKE-------------------FRREVSILSKLRHPN---IVQFigACLSPp 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 113 -----TAYM--GTLFysgttlSRLREEKPELineAWIRRMLPMLFGA--IKTIHDEGYLHRDISLDNIQIQDNGLPVLLD 183
Cdd:cd13999   64 plcivTEYMpgGSLY------DLLHKKKIPL---SWSLRLKIALDIArgMNYLHSPPIIHRDLKSLNILLDENFTVKIAD 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 184 FGSAR---RTIGNLSDETET---MlrpgfAPiEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP---------PVSVVR 248
Cdd:cd13999  135 FGLSRiknSTTEKMTGVVGTprwM-----AP-EVLRGEPYTEK---ADVYSFGIVLWELLTGEVPfkelspiqiAAAVVQ 205

                        250
                 ....*....|....*....
gi 505383238 249 S-----IQDTC-KPLVELM 261
Cdd:cd13999  206 KglrppIPPDCpPELSKLI 224
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
 105-242 1.01e-08

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: 57.33  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 105 LRFWVQNDT-AYMGTLFYSG----TTLSRLREEKPELINEAWIRRMLPmlfgAIKTIHDEGYLHRDISLDNIQIQDNGLP 179
Cdd:cd05624  137 LHYAFQDENyLYLVMDYYVGgdllTLLSKFEDKLPEDMARFYIGEMVL----AIHSIHQLHYVHRDIKPDNVLLDMNGHI 212

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 180 VLLDFGSARRTIGNLSDETETML-RPGF-AP-IEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd05624  213 RLADFGSCLKMNDDGTVQSSVAVgTPDYiSPeILQAMEDGMGKYGPECDWWSLGVCMYEMLYGETP 278
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
 86-209 1.29e-08

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 55.61  E-value: 1.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238    86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELIneawIRRMLPMLFGAIKT---IHDEGY 161
Cdd:smart00219  48 FLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYMEgGDLLSYLRKNRPKLS----LSDLLSFALQIARGmeyLESKNF 123

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 505383238   162 LHRDISLDNIQIQDNGLPVLLDFGSARrtigNLSDETETMLRPGFAPI 209
Cdd:smart00219 124 IHRDLAARNCLVGENLVVKISDFGLSR----DLYDDDYYRKRGGKLPI 167
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
 83-290 1.41e-08

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: 55.68  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  83 LNSFIQEARLLARFNH-PNLLHVLRFWVQNDTAYMGTLF-YSGTTLSR-LREEKPELINEAWIR----RMLPmlfgAIKT 155
Cdd:cd14131   43 LQSYKNEIELLKKLKGsDRIIQLYDYEVTDEDDYLYMVMeCGEIDLATiLKKKRPKPIDPNFIRyywkQMLE----AVHT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 156 IHDEGYLHRDISLDNIQIQDNGLPvLLDFGSARRtIGNlsDET-----ETMLRPGFAPIEQYTDDNESEQ-------GPW 223
Cdd:cd14131  119 IHEEGIVHSDLKPANFLLVKGRLK-LIDFGIAKA-IQN--DTTsivrdSQVGTLNYMSPEAIKDTSASGEgkpkskiGRP 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 224 TDIYALGAVLRTLIVGSPPpvsvVRSIQDTCKPLVELMPQGYSIP--------LLQAIDKALALHMEDRPqSIEE 290
Cdd:cd14131  195 SDVWSLGCILYQMVYGKTP----FQHITNPIAKLQAIIDPNHEIEfpdipnpdLIDVMKRCLQRDPKKRP-SIPE 264
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
 103-285 1.67e-08

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: 55.32  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRF---WVQNDTAYMGTLFYSGTTLSRLREEKPELInEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLP 179
Cdd:cd14189   62 HVVKFshhFEDAENIYIFLELCSRKSLAHIWKARHTLL-EPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMEL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 180 VLLDFGSA---------RRTIGNLSD--ETETMLRPGfapieqytddneseQGPWTDIYALGAVLRTLIVGSPP-PVSVV 247
Cdd:cd14189  141 KVGDFGLAarleppeqrKKTICGTPNylAPEVLLRQG--------------HGPESDVWSLGCVMYTLLCGNPPfETLDL 206

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505383238 248 RSIQDTCKPLVELMPQGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd14189  207 KETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRL 244
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
 120-242 2.23e-08

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: 55.82  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 120 FYSG----TTLSRLREEKPELINEAWIRRMLPmlfgAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARR-----T 190
Cdd:cd05597   82 YYCGgdllTLLSKFEDRLPEEMARFYLAEMVL----AIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSCLKlredgT 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505383238 191 I-GNLSDETETMLRPgfaPIEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd05597  158 VqSSVAVGTPDYISP---EILQAMEDGKGRYGPECDWWSLGVCMYEMLYGETP 207
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 88-287 2.43e-08

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: 54.75  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWvQNDTAY----MGtlFYSGTTL-SRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd08223   48 QEAKLLSKLKHPNIVSYKESF-EGEDGFlyivMG--FCEGGDLyTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNIL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSArRTIGNLSDETETML-RPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIV--- 238
Cdd:cd08223  125 HRDLKTQNIFLTKSNIIKVGDLGIA-RVLESSSDMATTLIgTPYYMSPELFSNKPYNHK---SDVWALGCCVYEMATlkh 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383238 239 --GSPPPVSVVRSIQDTCKPlveLMPQGYSIPLLQAIDKALALHMEDRPQS 287
Cdd:cd08223  201 afNAKDMNSLVYKILEGKLP---PMPKQYSPELGELIKAMLHQDPEKRPSV 248
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
 36-189 2.77e-08

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: 55.27  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEFMPSSLAVRGEdmtlvlrserfGKAFSAglnsfIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:cd07841   15 VVYKARDKETGRIVAIKKIKLGERKEAKD-----------GINFTA-----LREIKLLQELKHPNIIGLLDVFGHKSNIN 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 116 MgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARR 189
Cdd:cd07841   79 L-VFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARS 151
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
 50-187 2.81e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 55.86  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  50 AIKEFMPSSLAVRGEDMTL--VLRSER-FGKAFSAGLNSFIQ---EARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSG 123
Cdd:PHA03210 168 ALRASTEEAEARRGVNSTNqgKPKCERlIAKRVKAGSRAAIQlenEILALGRLNHENILKIEEILRSEANTYMITQKYDF 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 124 TTLSRLREEKPELINEAWI---RRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSA 187
Cdd:PHA03210 248 DLYSFMYDEAFDWKDRPLLkqtRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTA 314
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
 18-244 3.25e-08

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: 54.72  E-value: 3.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  18 YRFNEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEfmpsslaVRGEDMTLVlrserfgkafsaglNSFIQEARLLARFN 97
Cdd:cd06624    5 YEYDESGERVVLGKGTFGVVYAARDLSTQVRIAIKE-------IPERDSREV--------------QPLHEEIALHSRLS 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  98 HPNLlhvlrfwVQndtaYMGTLFYSGT-----------TLSRLREEK--PELINEAWIRRMLPMLFGAIKTIHDEGYLHR 164
Cdd:cd06624   64 HKNI-------VQ----YLGSVSEDGFfkifmeqvpggSLSALLRSKwgPLKDNENTIGYYTKQILEGLKYLHDNKIVHR 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 165 DISLDNIQIQD-NGLPVLLDFGSARRTIGnLSDETETmlrpgFAPIEQYT-----DDNESEQGPWTDIYALGAVLRTLIV 238
Cdd:cd06624  133 DIKGDNVLVNTySGVVKISDFGTSKRLAG-INPCTET-----FTGTLQYMapeviDKGQRGYGPPADIWSLGCTIIEMAT 206


                 ....*.
gi 505383238 239 GSPPPV 244
Cdd:cd06624  207 GKPPFI 212
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
 22-242 3.76e-08

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: 54.48  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  22 EFEIKEVIGGGGFGIVYRAWDHQLERTIAIKefMPSSLAVRGEDMTlvlrserfgkafsaglNSFIQEARLLARFNHPNL 101
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIK--MIDKKAMQKAGMV----------------QRVRNEVEIHCQLKHPSI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 102 LHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVL 181
Cdd:cd14186   64 LELYNYFEDSNYVYLVLEMCHNGEMSRYLKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKI 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383238 182 LDFGSArrTIGNLSDETE-TML-RPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14186  144 ADFGLA--TQLKMPHEKHfTMCgTPNYISPEIAT---RSAHGLESDVWSLGCMFYTLLVGRPP 201
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
 80-315 4.25e-08

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: 54.36  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  80 SAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDE 159
Cdd:cd06611   43 EEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDGGALDSIMLELERGLTEPQIRYVCRQMLEALNFLHSH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 160 GYLHRDISLDNIQIQDNGLPVLLDFG-SARRT---------IGnlsdeTETMLRPGFAPIEQYTDDneseqgPW---TDI 226
Cdd:cd06611  123 KVIHRDLKAGNILLTLDGDVKLADFGvSAKNKstlqkrdtfIG-----TPYWMAPEVVACETFKDN------PYdykADI 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 227 YALGAVLRTLIVGSPP-----PVSVVRSIQDTCKPLVeLMPQGYSIPLLQAIDKALALHMEDRPQSieefAALIEMPVag 301
Cdd:cd06611  192 WSLGITLIELAQMEPPhhelnPMRVLLKILKSEPPTL-DQPSKWSSSFNDFLKSCLVKDPDDRPTA----AELLKHPF-- 264

                        250
                 ....*....|....
gi 505383238 302 IDEVLTAKKTGTML 315
Cdd:cd06611  265 VSDQSDNKAIKDLL 278
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
 88-242 4.58e-08

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: 53.93  E-value: 4.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd14073   50 REIEIMSSLNHPHIIRIYEVFENKDKIVIVMEYASGGELYDYISERRRL-PEREARRIFRQIVSAVHYCHKNGVVHRDLK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGsarrtIGNLSDETETML----RPGFAPIE-----QYtddneseQGPWTDIYALGAVLRTLIV 238
Cdd:cd14073  129 LENILLDQNGNAKIADFG-----LSNLYSKDKLLQtfcgSPLYASPEivngtPY-------QGPEVDCWSLGVLLYTLVY 196


                 ....
gi 505383238 239 GSPP 242
Cdd:cd14073  197 GTMP 200
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
 98-243 4.90e-08

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: 53.93  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  98 HPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKP--ELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQD 175
Cdd:cd13997   59 HPNIVRYYSSWEEGGHLYIQMELCENGSLQDALEELSpiSKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISN 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383238 176 NGLPVLLDFGSARRtIGNLSDETETmlRPGFAPIEQYTDDneSEQGPWTDIYALGAVLRTLIVGSPPP 243
Cdd:cd13997  139 KGTCKIGDFGLATR-LETSGDVEEG--DSRYLAPELLNEN--YTHLPKADIFSLGVTVYEAATGEPLP 201
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 89-242 5.12e-08

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 53.67  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHvLRFWVQNDTA-YMGTLFYSGTTL-SRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd05123   43 ERNILERVNHPFIVK-LHYAFQTEEKlYLVLDYVPGGELfSHLSKEG--RFPEERARFYAAEIVLALEYLHSLGIIYRDL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSARRtigNLSDETETMLRPG----FAP--IEQytddneSEQGPWTDIYALGAVLRTLIVGS 240
Cdd:cd05123  120 KPENILLDSDGHIKLTDFGLAKE---LSSDGDRTYTFCGtpeyLAPevLLG------KGYGKAVDWWSLGVLLYEMLTGK 190


                 ..
gi 505383238 241 PP 242
Cdd:cd05123  191 PP 192
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
 105-242 5.50e-08

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: 55.02  E-value: 5.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 105 LRFWVQNDT-AYMGTLFYSG----TTLSRLREEKPELINEAWIRRMLPmlfgAIKTIHDEGYLHRDISLDNIQIQDNGLP 179
Cdd:cd05623  137 LHYAFQDDNnLYLVMDYYVGgdllTLLSKFEDRLPEDMARFYLAEMVL----AIDSVHQLHYVHRDIKPDNILMDMNGHI 212

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 180 VLLDFGSARRTIGNLSDETETML-RPGFAPIE--QYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd05623  213 RLADFGSCLKLMEDGTVQSSVAVgTPDYISPEilQAMEDGKGKYGPECDWWSLGVCMYEMLYGETP 278
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
 83-298 5.89e-08

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: 54.27  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  83 LNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd06644   53 LEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKII 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDE-----TETMLRPGFAPIEQYTDdneseqGPW---TDIYALGAVLR 234
Cdd:cd06644  133 HRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRdsfigTPYWMAPEVVMCETMKD------TPYdykADIWSLGITLI 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 235 TLIVGSPP-----PVSVVRSIQDTCKPLVeLMPQGYSIPLLQAIDKALALHMEDRPQSieefAALIEMP 298
Cdd:cd06644  207 EMAQIEPPhhelnPMRVLLKIAKSEPPTL-SQPSKWSMEFRDFLKTALDKHPETRPSA----AQLLEHP 270
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
 87-188 6.17e-08

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: 54.24  E-value: 6.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWV--------QNDTAYMgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHD 158
Cdd:cd07866   55 LREIKILKKLKHPNVVPLIDMAVerpdkskrKRGSVYM-VTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHE 133

                         90       100       110
                 ....*....|....*....|....*....|
gi 505383238 159 EGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd07866  134 NHILHRDIKAANILIDNQGILKIADFGLAR 163
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
 23-242 6.75e-08

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: 53.63  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSSLAVRGEDMtlvlrserfgkafsaglnsFIQEARLLARFNHPNLL 102
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEM-------------------LRREIEILKRLDHPNIV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRFWVQNDTAYM-------GTLFysgttlSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNI--QI 173
Cdd:cd05117   63 KLYEVFEDDKNLYLvmelctgGELF------DRIVKKGS--FSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENIllAS 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 174 QDNGLPVLL-DFGSARRTIGNlsDETETML-RPGF-AP--IEQYTDDNESeqgpwtDIYALGAVLRTLIVGSPP 242
Cdd:cd05117  135 KDPDSPIKIiDFGLAKIFEEG--EKLKTVCgTPYYvAPevLKGKGYGKKC------DIWSLGVILYILLCGYPP 200
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
 21-185 7.14e-08

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: 53.52  E-value: 7.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  21 NEFEIKEVIGGGGFGIVYRAWDHQLERTIAIK----EFMPSSLavrgedmtlvlrserfgkafsaglNSFIQEARLLARF 96
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKridlEKCQTSM------------------------DELRKEIQAMSQC 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  97 NHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPE-LINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQ 174
Cdd:cd06610   57 NHPNVVSYYTSFVVGDELWLVMPLLSgGSLLDIMKSSYPRgGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLG 136

                        170
                 ....*....|.
gi 505383238 175 DNGLPVLLDFG 185
Cdd:cd06610  137 EDGSVKIADFG 147
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
 21-242 1.36e-07

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: 52.99  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  21 NEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKefmpsslavrgedmtlVLrSERF----GKAFSAglnsfIQEARLLARF 96
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYAIK----------------VL-DKRHiikeKKVKYV-----TIEKEVLSRL 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  97 NHPNLLHvLRFWVQNDTaymgTLFYS------GTTLSRLReeKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDN 170
Cdd:cd05581   59 AHPGIVK-LYYTFQDES----KLYFVleyapnGDLLEYIR--KYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPEN 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 171 IQIQDNGLPVLLDFGSArRTIGNLSDETETMLRPGFAPIEQYTDD---------------NESEQGPWTDIYALGAVLRT 235
Cdd:cd05581  132 ILLDEDMHIKITDFGTA-KVLGPDSSPESTKGDADSQIAYNQARAasfvgtaeyvspellNEKPAGKSSDLWALGCIIYQ 210


                 ....*..
gi 505383238 236 LIVGSPP 242
Cdd:cd05581  211 MLTGKPP 217
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 88-286 1.39e-07

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: 52.86  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFW---VQNDTAYMGTLFYSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHR 164
Cdd:cd06917   48 KEVALLSQLKLGQPKNIIKYYgsyLKGPSLWIIMDYCEGGSIRTLMRAGP--IAERYIAVIMREVLVALKFIHKDGIIHR 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQGpwTDIYALGAVLRTLIVGSPP-- 242
Cdd:cd06917  126 DIKAANILVTNTGNVKLCDFGVAASLNQNSSKRSTFVGTPYWMAPEVITEGKYYDTK--ADIWSLGITTYEMATGNPPys 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505383238 243 ---PVSVVRSIQDTCKPLVELmpQGYSiPLLQAIdkaLALHMEDRPQ 286
Cdd:cd06917  204 dvdALRAVMLIPKSKPPRLEG--NGYS-PLLKEF---VAACLDEEPK 244
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
 86-189 1.43e-07

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: 52.70  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYM-GTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGaIKTIHDEGYLHR 164
Cdd:cd05085   40 FLSEARILKQYDHPNIVKLIGVCTQRQPIYIvMELVPGGDFLSFLRKKKDELKTKQLVKFSLDAAAG-MAYLESKNCIHR 118

                         90       100
                 ....*....|....*....|....*
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSARR 189
Cdd:cd05085  119 DLAARNCLVGENNALKISDFGMSRQ 143
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
 87-313 1.77e-07

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: 52.80  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd06654   65 INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTET--CMDEGQIAAVCRECLQALEFLHSNQVIHRDI 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSPP---- 242
Cdd:cd06654  143 KSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMIEGEPPylne 219

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 243 -PVSVVRSIQDTCKPLVElMPQGYSIPLLQAIDKALALHMEDRPQSIE----EFAAlIEMPVAGIDEVLTAKKTGT 313
Cdd:cd06654  220 nPLRALYLIATNGTPELQ-NPEKLSAIFRDFLNRCLEMDVEKRGSAKEllqhQFLK-IAKPLSSLTPLIAAAKEAT 293
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
 60-242 2.01e-07

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: 52.13  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  60 AVRGEDMTLVLRSERFGKAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM-GTLFYSGTTLSRLREEKPelIN 138
Cdd:cd14070   24 AVTGEKVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYLvMELCPGGNLMHRIYDKKR--LE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 139 EAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFG-SARRTIGNLSDETETML-RPGFAPIEQYTddn 216
Cdd:cd14070  102 EREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGlSNCAGILGYSDPFSTQCgSPAYAAPELLA--- 178

                        170       180
                 ....*....|....*....|....*.
gi 505383238 217 ESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14070  179 RKKYGPKVDVWSIGVNMYAMLTGTLP 204
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
 36-242 2.19e-07

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: 51.88  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKeFMPsslaVRGEDMTLVLRserfgkafsaglnsfiqEARLLARFNHPNLLHVLRFWvQNDTAY 115
Cdd:cd14006    8 VVKRCIEKATGREFAAK-FIP----KRDKKKEAVLR-----------------EISILNQLQHPRIIQLHEAY-ESPTEL 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 116 MGTLFY--SGTTLSRLREekPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPV--LLDFGSARRti 191
Cdd:cd14006   65 VLILELcsGGELLDRLAE--RGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQikIIDFGLARK-- 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505383238 192 gnLSDETETMLR---PGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd14006  141 --LNPGEELKEIfgtPEFVAPEIVNGEPVSLA---TDMWSIGVLTYVLLSGLSP 189
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
 93-242 3.31e-07

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: 51.42  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  93 LARFNHPNLLHVLRFWVQNDTAYMgTLFYS--GTTLSRLREEKPELINEA--WIRRMLpmlfGAIKTIHDEGYLHRDISL 168
Cdd:cd14080   56 LRKLRHPNIIQVYSIFERGSKVFI-FMEYAehGDLLEYIQKRGALSESQAriWFRQLA----LAVQYLHSLDIAHRDLKC 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 169 DNIQIQDNGLPVLLDFGSARRtigNLSDETETMLR-----PGFAPIE-----QYtddneseQGPWTDIYALGAVLRTLIV 238
Cdd:cd14080  131 ENILLDSNNNVKLSDFGFARL---CPDDDGDVLSKtfcgsAAYAAPEilqgiPY-------DPKKYDIWSLGVILYIMLC 200


                 ....
gi 505383238 239 GSPP 242
Cdd:cd14080  201 GSMP 204
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
 81-242 3.83e-07

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: 51.49  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  81 AGLNSFIQEARLLARFNHPNLLHVLRfwVQNDTA----YMGTLFYSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTI 156
Cdd:cd14200   65 APLERVYQEIAILKKLDHVNIVKLIE--VLDDPAednlYMVFDLLRKGPVMEVPSDKP--FSEDQARLYFRDIVLGIEYL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 157 HDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQGPWTDIYALGAVLRTL 236
Cdd:cd14200  141 HYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGKALDVWAMGVTLYCF 220


                 ....*.
gi 505383238 237 IVGSPP 242
Cdd:cd14200  221 VYGKCP 226
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
 87-289 4.29e-07

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: 51.65  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd06655   64 INEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLTDVVTET--CMDEAQIAAVCRECLQALEFLHANQVIHRDI 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSPP---- 242
Cdd:cd06655  142 KSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMVEGEPPylne 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 505383238 243 -PVSVVRSIQDTCKPLVElMPQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06655  219 nPLRALYLIATNGTPELQ-NPEKLSPIFRDFLNRCLEMDVEKRGSAKE 265
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
 84-242 4.54e-07

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: 51.45  E-value: 4.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFN-HPNLLHVlrfwvqNDTAYMGTLFYSGTTLSRLRE------EKPELiNEAWIRRMLPMLFGAIKTI 156
Cdd:cd14182   54 EATLKEIDILRKVSgHPNIIQL------KDTYETNTFFFLVFDLMKKGElfdyltEKVTL-SEKETRKIMRALLEVICAL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 157 HDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRtIGNLSDETETMLRPGF-AP--IEQYTDDNESEQGPWTDIYALGAVL 233
Cdd:cd14182  127 HKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQ-LDPGEKLREVCGTPGYlAPeiIECSMDDNHPGYGKEVDMWSTGVIM 205


                 ....*....
gi 505383238 234 RTLIVGSPP 242
Cdd:cd14182  206 YTLLAGSPP 214
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 86-188 5.87e-07

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 50.91  E-value: 5.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd05059   46 FIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRD 125

                         90       100
                 ....*....|....*....|...
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05059  126 LAARNCLVGEQNVVKVSDFGLAR 148
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 98-261 6.10e-07

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: 51.19  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  98 HPNL--LHVLrFWVQNDTAYMGTLFYSGTTLSRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQD 175
Cdd:cd14179   61 HPNIvkLHEV-YHDQLHTFLVMELLKGGELLERIKKKQ--HFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTD 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 176 ---NGLPVLLDFGSARRTignlSDETETMLRPGF----APIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPPPVSVVR 248
Cdd:cd14179  138 esdNSEIKIIDFGFARLK----PPDNQPLKTPCFtlhyAAPELLNYNGYDES---CDLWSLGVILYTMLSGQVPFQCHDK 210

                        170
                 ....*....|...
gi 505383238 249 SIqdTCKPLVELM 261
Cdd:cd14179  211 SL--TCTSAEEIM 221
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
 88-289 6.16e-07

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: 50.90  E-value: 6.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGaIKTIHDEGYLHRDIS 167
Cdd:cd06631   52 EEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPGGSIASILARFGALEEPVFCRYTKQILEG-VAYLHNNNVIHRDIK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGSARRTIGNLSDETET-MLR-----PGFAPIEQYtddNESEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd06631  131 GNNIMLMPNGVIKLIDFGCAKRLCINLSSGSQSqLLKsmrgtPYWMAPEVI---NETGHGRKSDIWSIGCTVFEMATGKP 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505383238 242 P-----PVSVVRSIQDTCKPLVELmPQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06631  208 PwadmnPMAAIFAIGSGRKPVPRL-PDKFSPEARDFVHACLTRDQDERPSAEQ 259
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 88-246 6.78e-07

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: 50.58  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL-SRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd08218   48 KEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLyKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDI 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSAR---------RT-IGnlsdeTETMLRPGFAPIEQYtdDNESeqgpwtDIYALGAVLRTL 236
Cdd:cd08218  128 KSQNIFLTKDGIIKLGDFGIARvlnstvelaRTcIG-----TPYYLSPEICENKPY--NNKS------DIWALGCVLYEM 194

                        170       180
                 ....*....|....*....|....*....
gi 505383238 237 -------------------IVGSPPPVSV 246
Cdd:cd08218  195 ctlkhafeagnmknlvlkiIRGSYPPVPS 223
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
 87-289 7.39e-07

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: 50.31  E-value: 7.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd06647   52 INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTET--CMDEGQIAAVCRECLQALEFLHSNQVIHRDI 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSPP---- 242
Cdd:cd06647  130 KSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMVEGEPPylne 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 505383238 243 -PVSVVRSIQDTCKPLVElMPQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06647  207 nPLRALYLIATNGTPELQ-NPEKLSAIFRDFLNRCLEMDVEKRGSAKE 253
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
 97-240 8.19e-07

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: 50.61  E-value: 8.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  97 NHPNLLHVLRFWVQNDTAYM------GTLFysgtTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDN 170
Cdd:cd07830   56 EHPNIVKLKEVFRENDELYFvfeymeGNLY----QLMKDRKGKP--FSESVIRSIIYQILQGLAHIHKHGFFHRDLKPEN 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 171 IQIQDNGLPVLLDFGSARRtIGNLSDET-----------ETMLRPGF--APIeqytddneseqgpwtDIYALGAV----- 232
Cdd:cd07830  130 LLVSGPEVVKIADFGLARE-IRSRPPYTdyvstrwyrapEILLRSTSysSPV---------------DIWALGCImaely 193


                 ....*....
gi 505383238 233 -LRTLIVGS 240
Cdd:cd07830  194 tLRPLFPGS 202
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
 37-188 8.57e-07

Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 50.64  E-value: 8.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEfmpsslaVRGEDmtlvlrsERFGKAFSAglnsfIQEARLLARFNHPNLLHVLRFWVQNDTA-Y 115
Cdd:cd07840   15 VYKARNKKTGELVALKK-------IRMEN-------EKEGFPITA-----IREIKLLQKLDHPNVVRLKEIVTSKGSAkY 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 116 MGTLF----YSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd07840   76 KGSIYmvfeYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR 152
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
 76-289 8.72e-07

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: 50.81  E-value: 8.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  76 GKAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKT 155
Cdd:cd06633   58 GKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWL-VMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAY 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 156 IHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTignlSDETETMLRPGFAPIEQYTDDNESEQGPWTDIYALGAVLRT 235
Cdd:cd06633  137 LHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA----SPANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITCIE 212

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 236 LIVGSPP-----PVSVVRSIQDTCKPlvELMPQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06633  213 LAERKPPlfnmnAMSALYHIAQNDSP--TLQSNEWTDSFRGFVDYCLQKIPQERPSSAE 269
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
 71-242 9.58e-07

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: 50.44  E-value: 9.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  71 RSERFGKAFSAGLNSFIQEARLLARFNHPN---LLHVLrfwvqNDTA----YMGTLFYSGTTLSRLREEKPELINEAWiR 143
Cdd:cd14118   46 RKPGALGKPLDPLDRVYREIAILKKLDHPNvvkLVEVL-----DDPNednlYMVFELVDKGAVMEVPTDNPLSEETAR-S 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 144 RMLPMLFGaIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQGPW 223
Cdd:cd14118  120 YFRDIVLG-IEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSGKA 198

                        170
                 ....*....|....*....
gi 505383238 224 TDIYALGAVLRTLIVGSPP 242
Cdd:cd14118  199 LDIWAMGVTLYCFVFGRCP 217
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
 36-241 1.02e-06

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: 50.41  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEfmpssLAVRgedmtlvlrserfgKAFSAGLNSFIQEARLLARFN-HPNLLHVLRfwVQNDTA 114
Cdd:cd07832   15 IVFKAKDRETGETVALKK-----VALR--------------KLEGGIPNQALREIKALQACQgHPYVVKLRD--VFPHGT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 115 YMGTLF-YSGTTLS-RLR-EEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTi 191
Cdd:cd07832   74 GFVLVFeYMLSSLSeVLRdEERP--LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLF- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 192 gnlSDETETMLRPGF------APIEQYtddNESEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd07832  151 ---SEEDPRLYSHQVatrwyrAPELLY---GSRKYDEGVDLWAVGCIFAELLNGSP 200
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
 20-242 1.08e-06

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: 49.97  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  20 FNEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKefmpsSLAVRGEDMTLvlrsERFGKAFSAGLNSfIQEARLLArfNHP 99
Cdd:cd14181    9 YQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVK-----IIEVTAERLSP----EQLEEVRSSTLKE-IHILRQVS--GHP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 100 NLLHVLRFWvqNDTAYMGTLF---YSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDN 176
Cdd:cd14181   77 SIITLIDSY--ESSTFIFLVFdlmRRGELFDYLTEKVT--LSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQ 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 177 GLPVLLDFGSARRTignlsdETETMLR-----PGF-AP--IEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14181  153 LHIKLSDFGFSCHL------EPGEKLRelcgtPGYlAPeiLKCSMDETHPGYGKEVDLWACGVILFTLLAGSPP 220
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
 50-242 1.13e-06

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: 50.00  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  50 AIKEFMPSSLAVRGEDMTLVLRSErfgkafsaglnsFIqearLLARFNHPNLLHVLRFWVQNDTAYMGTL-FYSGTTLSR 128
Cdd:cd13994   24 AVKEYRRRDDESKRKDYVKRLTSE------------YI----ISSKLHHPNIVKVLDLCQDLHGKWCLVMeYCPGGDLFT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 129 LREEKPEL-INEA--WIRRMLPmlfgAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSArrTIGNLSDETETMLRPG 205
Cdd:cd13994   88 LIEKADSLsLEEKdcFFKQILR----GVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTA--EVFGMPAEKESPMSAG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 505383238 206 FAPIEQYTDDNESEQGPW----TDIYALGAVLRTLIVGSPP 242
Cdd:cd13994  162 LCGSEPYMAPEVFTSGSYdgraVDVWSCGIVLFALFTGRFP 202
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
 93-285 1.18e-06

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 49.84  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  93 LARFNHPNLLHVLRFWVQND---------TAYMGtlfySGTT---LSRLREEKPELINEAWiRRMLPMLFGAIKTIH--D 158
Cdd:cd13984   49 LIQLDHPNIVKFHRYWTDVQeekarvifiTEYMS----SGSLkqfLKKTKKNHKTMNEKSW-KRWCTQILSALSYLHscD 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 EGYLHRDISLDNIQIQDNGlpvLLDFGS-ARRTIGNLSDETETMLRPG--FAPIEQYTDDneseQGPWTDIYALG----- 230
Cdd:cd13984  124 PPIIHGNLTCDTIFIQHNG---LIKIGSvAPDAIHNHVKTCREEHRNLhfFAPEYGYLED----VTTAVDIYSFGmcale 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 231 -AVLRTLIVGSPPPVS---VVRSIQDTCKPLVELMpqgysipllqaIDKALALHMEDRP 285
Cdd:cd13984  197 mAALEIQSNGEKVSANeeaIIRAIFSLEDPLQKDF-----------IRKCLSVAPQDRP 244
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 47-299 1.21e-06

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: 49.74  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  47 RTIAIKEFMPSSLAVRGEDMTLVLRSE-RFGKAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTT 125
Cdd:cd08221    6 RVLGRGAFGEAVLYRKTEDNSLVVWKEvNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 126 L-SRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARR--TIGNLSDE---TE 199
Cdd:cd08221   86 LhDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVldSESSMAESivgTP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 200 TMLRPGFAPIEQYtdDNESeqgpwtDIYALGAVL-------RTLIVGSPppvsvVRSIQDTCKPLVELMPQGYSIPLLQA 272
Cdd:cd08221  166 YYMSPELVQGVKY--NFKS------DIWAVGCVLyelltlkRTFDATNP-----LRLAVKIVQGEYEDIDEQYSEEIIQL 232

                        250       260
                 ....*....|....*....|....*..
gi 505383238 273 IDKALALHMEDRPqSIEEfaaLIEMPV 299
Cdd:cd08221  233 VHDCLHQDPEDRP-TAEE---LLERPL 255
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
 36-242 1.44e-06

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: 49.53  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEFMPSSLAvrgedmtlvlRSERfgkafsaglNSFIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:cd13983   16 TVYRAFDTEEGIEVAWNEIKLRKLP----------KAER---------QRFKQEIEILKSLKHPNIIKFYDSWESKSKKE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 116 M---GTLFYSGTT---LSRLREEKPELInEAWIRRMLpmlfgaiktihdEG--YL--------HRDISLDNI-------- 171
Cdd:cd13983   77 VifiTELMTSGTLkqyLKRFKRLKLKVI-KSWCRQIL------------EGlnYLhtrdppiiHRDLKCDNIfingntge 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 172 -QIQDNGLPVLLDFGSARRTIGNlsdetetmlrPGF-APiEQYTDD-NESeqgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd13983  144 vKIGDLGLATLLRQSFAKSVIGT----------PEFmAP-EMYEEHyDEK-----VDIYAFGMCLLEMATGEYP 201
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
 83-242 1.48e-06

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: 49.56  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  83 LNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTtLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd14002   44 LRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQGE-LFQILEDDGTL-PEEEVRSIAKQLVSALHYLHSNRII 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSARrtigNLSDETETMLRPGFAPI--------EQYTDDNeseqgpwTDIYALGAVLR 234
Cdd:cd14002  122 HRDMKPQNILIGKGGVVKLCDFGFAR----AMSCNTLVLTSIKGTPLymapelvqEQPYDHT-------ADLWSLGCILY 190


                 ....*...
gi 505383238 235 TLIVGSPP 242
Cdd:cd14002  191 ELFVGQPP 198
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
 61-242 1.68e-06

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: 49.24  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  61 VRGEDMTLvlrseRFGKAFSAGLNSFIQEARL-LARFNHPNLLHVLRFWVQNDTAYMGTLFY--SGTTLSRLreeKPEL- 136
Cdd:cd13987   16 GSGTKMAL-----KFVPKPSTKLKDFLREYNIsLELSVHPHIIKTYDVAFETEDYYVFAQEYapYGDLFSII---PPQVg 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 137 INEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPV--LLDFGSARRTiGNLSDETETMLrPGFAPIEQYTD 214
Cdd:cd13987   88 LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRvkLCDFGLTRRV-GSTVKRVSGTI-PYTAPEVCEAK 165

                        170       180
                 ....*....|....*....|....*....
gi 505383238 215 DNESEQ-GPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd13987  166 KNEGFVvDPSIDVWAFGVLLFCCLTGNFP 194
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
 85-289 1.90e-06

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: 49.35  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEK---PELINEAWIRRMLpmlfGAIKTIHDEGY 161
Cdd:cd06630   49 AIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSKYgafSENVIINYTLQIL----RGLAYLHDNQI 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 162 LHRDISLDNIQIQDNGLPV-LLDFGSARR--TIGNLSDE-------TETMLRPGFAPIEQYtddneseqGPWTDIYALGA 231
Cdd:cd06630  125 IHRDLKGANLLVDSTGQRLrIADFGAAARlaSKGTGAGEfqgqllgTIAFMAPEVLRGEQY--------GRSCDVWSVGC 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 232 VLRTLIVGSPP--------PVSVVRSIQDTCKPlvELMPQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06630  197 VIIEMATAKPPwnaekisnHLALIFKIASATTP--PPIPEHLSPGLRDVTLRCLELQPEDRPPARE 260
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
 21-289 1.93e-06

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: 49.61  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  21 NEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMPSSLAVRGEDMTLvlrserfgkafsaglnsfiQEARLLARFNHPN 100
Cdd:cd07848    1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTL-------------------RELKMLRTLKQEN 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 101 LLHVLRFWVQNDTAYMgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPV 180
Cdd:cd07848   62 IVELKEAFRRRGKLYL-VFEYVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLK 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 181 LLDFGSARR-TIGNLSDETETMLRPGFAPIEQYTDdneSEQGPWTDIYALGAVLRTLIVGSP-----PPVSVVRSIQDTC 254
Cdd:cd07848  141 LCDFGFARNlSEGSNANYTEYVATRWYRSPELLLG---APYGKAVDMWSVGCILGELSDGQPlfpgeSEIDQLFTIQKVL 217

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 505383238 255 KPL-VELMPQGYSIPLLQAIDKALALHmedrPQSIE 289
Cdd:cd07848  218 GPLpAEQMKLFYSNPRFHGLRFPAVNH----PQSLE 249
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
 36-242 1.98e-06

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: 49.13  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEfMPsslaVRGEDMTLVlrserfgkafsaglnsfIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:cd06614   15 EVYKATDRATGKEVAIKK-MR----LRKQNKELI-----------------INEILIMKECKHPNIVDYYDSYLVGDELW 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 116 MGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSArrtiGNLS 195
Cdd:cd06614   73 VVMEYMDGGSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFA----AQLT 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383238 196 DETE---TML-RPGFAPIEQYTDdneSEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd06614  149 KEKSkrnSVVgTPYWMAPEVIKR---KDYGPKVDIWSLGIMCIEMAEGEPP 196
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
 139-242 2.00e-06

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: 49.02  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 139 EAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARrtIGNLSDETETML-RPGFAPIEQYTDDNE 217
Cdd:cd05611   96 EDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSR--NGLEKRHNKKFVgTPDYLAPETILGVGD 173

                         90       100
                 ....*....|....*....|....*
gi 505383238 218 SEQGpwtDIYALGAVLRTLIVGSPP 242
Cdd:cd05611  174 DKMS---DWWSLGCVIFEFLFGYPP 195
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
 89-233 2.07e-06

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 49.29  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPnllHVLRF---WVQNDTAYMGTLFYSGTTLSRL-REEKPELINEAWirRMLPMLFGAIKTIHDEGYLHR 164
Cdd:cd14046   54 EVMLLSRLNHQ---HVVRYyqaWIERANLYIQMEYCEKSTLRDLiDSGLFQDTDRLW--RLFRQILEGLAYIHSQGIIHR 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSArrTIGNLSDETETMLRPGFAPIEQYTDDN-------------ESEQGPWT------D 225
Cdd:cd14046  129 DLKPVNIFLDSNGNVKIGDFGLA--TSNKLNVELATQDINKSTSAALGSSGDltgnvgtalyvapEVQSGTKStynekvD 206


                 ....*...
gi 505383238 226 IYALGAVL 233
Cdd:cd14046  207 MYSLGIIF 214
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
 74-242 2.16e-06

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


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 49.23  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  74 RFGKAFSAGLNSFI-QEARLLARFNHPNLLHVL-RFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFG 151
Cdd:cd14191   33 KFFKAYSAKEKENIrQEISIMNCLHHPKLVQCVdAFEEKANIVMVLEMVSGGELFERIIDEDFELTERECIKYMRQISEG 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 152 aIKTIHDEGYLHRDISLDNIQ-IQDNGLPV-LLDFGSARRTignlsdETETMLRPGFAPIEQYTDD--NESEQGPWTDIY 227
Cdd:cd14191  113 -VEYIHKQGIVHLDLKPENIMcVNKTGTKIkLIDFGLARRL------ENAGSLKVLFGTPEFVAPEviNYEPIGYATDMW 185

                        170
                 ....*....|....*
gi 505383238 228 ALGAVLRTLIVGSPP 242
Cdd:cd14191  186 SIGVICYILVSGLSP 200
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
 85-277 2.20e-06

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 49.30  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLARFNHPNLLHVLRFwVQNDTAYMGTLFYS-GTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd05069   53 AFLQEAQIMKKLRHDKLVPLYAV-VSEEPIYIVTEFMGkGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIH 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARrtignLSDETETMLRPGFAPIEQYTDDNESEQGPWT---DIYALGAVLRTLIVGS 240
Cdd:cd05069  132 RDLRAANILVGDNLVCKIADFGLAR-----LIEDNEYTARQGAKFPIKWTAPEAALYGRFTiksDVWSFGILLTELVTKG 206

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 505383238 241 --PPPVSVVRSIqdtckplVELMPQGYSIPLLQAIDKAL 277
Cdd:cd05069  207 rvPYPGMVNREV-------LEQVERGYRMPCPQGCPESL 238
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
 88-292 2.36e-06

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: 49.56  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFY-----SGTTLSRLReeKPELINEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd07880   63 RELRLLKHMKHENVIGLLDVFTPDLSLDRFHDFYlvmpfMGTDLGKLM--KHEKLSEDRIQFLVYQMLKGLKYIHAAGII 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETmlRPGFAP-----IEQYTDDneseqgpwTDIYALGAVLRTLI 237
Cdd:cd07880  141 HRDLKPGNLAVNEDCELKILDFGLARQTDSEMTGYVVT--RWYRAPevilnWMHYTQT--------VDIWSVGCIMAEML 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 238 VGSP--------------------PPVSVVRSIQDT-----CKPLVELMPQGYSIPLLQA-------IDKALALHMEDRP 285
Cdd:cd07880  211 TGKPlfkghdhldqlmeimkvtgtPSKEFVQKLQSEdaknyVKKLPRFRKKDFRSLLPNAnplavnvLEKMLVLDAESRI 290


                 ....*..
gi 505383238 286 QSIEEFA 292
Cdd:cd07880  291 TAAEALA 297
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 126-298 2.44e-06

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: 49.08  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 126 LSRLREEKpELINEAWIRRMLPMLFGAIKTIHDEGY-----LHRDISLDNIQIQDNGLPVLLDFGSArRTIGNLSDETET 200
Cdd:cd08217   92 IKKCKKEN-QYIPEEFIWKIFTQLLLALYECHNRSVgggkiLHRDLKPANIFLDSDNNVKLGDFGLA-RVLSHDSSFAKT 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 201 ML-RPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP-----PVSVVRSIQD-TCKPLvelmPQGYSIPLLQAI 273
Cdd:cd08217  170 YVgTPYYMSPELLNEQSYDEK---SDIWSLGCLIYELCALHPPfqaanQLELAKKIKEgKFPRI----PSRYSSELNEVI 242

                        170       180
                 ....*....|....*....|....*
gi 505383238 274 DKALALHMEDRPqSIEEfaaLIEMP 298
Cdd:cd08217  243 KSMLNVDPDKRP-SVEE---LLQLP 263
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
 88-242 2.55e-06

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: 48.80  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd14161   51 REIEIMSSLNHPHIISVYEVFENSSKIVIVMEYASRGDLYDYISERQRL-SELEARHFFRQIVSAVHYCHANGIVHRDLK 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGsarrtIGNLSdETETMLR-----PGFAPIEqyTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14161  130 LENILLDANGNIKIADFG-----LSNLY-NQDKFLQtycgsPLYASPE--IVNGRPYIGPEVDSWSLGVLLYILVHGTMP 201
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
 21-241 2.66e-06

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: 49.03  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  21 NEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEfmpsslaVRgedmtlvLRSERFGKAFSAglnsfIQEARLLARFNHPN 100
Cdd:cd07864    7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKK-------VR-------LDNEKEGFPITA-----IREIKILRQLNHRS 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 101 LLHV----------LRFWVQNDTAYMgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDN 170
Cdd:cd07864   68 VVNLkeivtdkqdaLDFKKDKGAFYL-VFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSN 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 171 IQIQDNGLPVLLDFGSARrtIGNLSDE---TETMLRPGFAPIEQYTddNESEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd07864  147 ILLNNKGQIKLADFGLAR--LYNSEESrpyTNKVITLWYRPPELLL--GEERYGPAIDVWSCGCILGELFTKKP 216
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
 89-252 2.87e-06

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: 48.48  E-value: 2.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTAY-------MGTLFYSGTTLSRLREEkpelinEAwiRRMLPMLFGAIKTIHDEGY 161
Cdd:cd14095   48 EVAILRRVKHPNIVQLIEEYDTDTELYlvmelvkGGDLFDAITSSTKFTER------DA--SRMVTDLAQALKYLHSLSI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 162 LHRDISLDNIQIQDNGLPV----LLDFGSARRTIGNLSD--ETETMLRPGFApieqytddNESEQGPWTDIYALGAVLRT 235
Cdd:cd14095  120 VHRDIKPENLLVVEHEDGSkslkLADFGLATEVKEPLFTvcGTPTYVAPEIL--------AETGYGLKVDIWAAGVITYI 191

                        170
                 ....*....|....*..
gi 505383238 236 LIVGSPPPVSVVRSIQD 252
Cdd:cd14095  192 LLCGFPPFRSPDRDQEE 208
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
 88-242 3.05e-06

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: 48.81  E-value: 3.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFW--VQNDTAYMGTLFYSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd14199   74 QEIAILKKLDHPNVVKLVEVLddPSEDHLYMVFELVKQGPVMEVPTLKP--LSEDQARFYFQDLIKGIEYLHYQKIIHRD 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14199  152 VKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIFSGKALDVWAMGVTLYCFVFGQCP 228
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
 84-188 3.07e-06

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: 48.39  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM-GTLFYSGTTLSRLREEKPELINEAWIrRMLPMLFGAIKTIHDEGYL 162
Cdd:cd05084   39 AKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIvMELVQGGDFLTFLRTEGPRLKVKELI-RMVENAAAGMEYLESKHCI 117

                         90       100
                 ....*....|....*....|....*.
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05084  118 HRDLAARNCLVTEKNVLKISDFGMSR 143
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
 98-185 3.11e-06

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: 48.46  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  98 HPNLLHVLRFWVQNDTAYMGTLfYSGTTLSRLREEKPEL-INEAWirRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDN 176
Cdd:cd14050   60 HPNCVRFIKAWEEKGILYIQTE-LCDTSLQQYCEETHSLpESEVW--NILLDLLKGLKHLHDHGLIHLDIKPANIFLSKD 136


                 ....*....
gi 505383238 177 GLPVLLDFG 185
Cdd:cd14050  137 GVCKLGDFG 145
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
 77-245 3.17e-06

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: 48.70  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  77 KAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpELINEAWIRRMLPMLFGAIKTI 156
Cdd:cd14097   38 KAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELKELLLRK-GFFSENETRHIIQSLASAVAYL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 157 HDEGYLHRDISLDNIQIQ----DNGLPV---LLDFGSARRTIGNLSDE-TETMLRPGFAPIEQYTDDNESEqgpWTDIYA 228
Cdd:cd14097  117 HKNDIVHRDLKLENILVKssiiDNNDKLnikVTDFGLSVQKYGLGEDMlQETCGTPIYMAPEVISAHGYSQ---QCDIWS 193

                        170
                 ....*....|....*..
gi 505383238 229 LGAVLRTLIVGSPPPVS 245
Cdd:cd14097  194 IGVIMYMLLCGEPPFVA 210
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
 87-242 4.07e-06

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: 48.21  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL-------SRLREEKPelineawiRRMLPMLFGAIKTIHDE 159
Cdd:cd14077   61 IREAALSSLLNHPHICRLRDFLRTPNHYYMLFEYVDGGQLldyiishGKLKEKQA--------RKFARQIASALDYLHRN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 160 GYLHRDISLDNIQIQDNGLPVLLDFGsarrtIGNLSDEtETMLR----------PGFAPIEQYTddneseqGPWTDIYAL 229
Cdd:cd14077  133 SIVHRDLKIENILISKSGNIKIIDFG-----LSNLYDP-RRLLRtfcgslyfaaPELLQAQPYT-------GPEVDVWSF 199

                        170
                 ....*....|...
gi 505383238 230 GAVLRTLIVGSPP 242
Cdd:cd14077  200 GVVLYVLVCGKVP 212
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
 61-287 4.51e-06

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: 48.48  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  61 VRGEDMTLVLRSERFGKAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMgTLFYSGTTLSRLREEKPELINEA 140
Cdd:cd06634   37 VRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWL-VMEYCLGSASDLLEVHKKPLQEV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 141 WIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSArrtiGNLSDETETMLRPGFAPIEQYTDDNESEQ 220
Cdd:cd06634  116 EIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSA----SIMAPANSFVGTPYWMAPEVILAMDEGQY 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383238 221 GPWTDIYALGAVLRTLIVGSPP-----PVSVVRSIQDTCKPLveLMPQGYSIPLLQAIDKALALHMEDRPQS 287
Cdd:cd06634  192 DGKVDVWSLGITCIELAERKPPlfnmnAMSALYHIAQNESPA--LQSGHWSEYFRNFVDSCLQKIPQDRPTS 261
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
 87-242 4.71e-06

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: 48.18  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd06656   64 INEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTET--CMDEGQIAAVCRECLQALDFLHSNQVIHRDI 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd06656  142 KSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVT---RKAYGPKVDIWSLGIMAIEMVEGEPP 214
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
 85-209 5.44e-06

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: 47.88  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238   85 SFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGT-LFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:pfam07714  47 DFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTeYMPGGDLLDFLRKHKRKL-TLKDLLSMALQIAKGMEYLESKNFVH 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 505383238  164 RDISLDNIQIQDNGLPVLLDFGSArRTIgnLSDETETMLRPGFAPI 209
Cdd:pfam07714 126 RDLAARNCLVSENLVVKISDFGLS-RDI--YDDDYYRKRGGGKLPI 168
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
 61-289 5.48e-06

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: 48.12  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  61 VRGEDMTLVLRSERFGKAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTlSRLREEKPELINEA 140
Cdd:cd06635   47 VRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSA-SDLLEVHKKPLQEI 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 141 WIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTignlSDETETMLRPGFAPIEQYTDDNESEQ 220
Cdd:cd06635  126 EIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIA----SPANSFVGTPYWMAPEVILAMDEGQY 201

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 221 GPWTDIYALGAVLRTLIVGSPP-----PVSVVRSIQDTCKPlvELMPQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06635  202 DGKVDVWSLGITCIELAERKPPlfnmnAMSALYHIAQNESP--TLQSNEWSDYFRNFVDSCLQKIPQDRPTSEE 273
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
 80-242 5.79e-06

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: 47.77  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  80 SAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSG-------TTLSRLREekpeliNEAwiRRMLPMLFGA 152
Cdd:cd14071   40 EENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNgeifdylAQHGRMSE------KEA--RKKFWQILSA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 153 IKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGsarrtIGNLSDETETML----RPGFAPIEQYtdDNESEQGPWTDIYA 228
Cdd:cd14071  112 VEYCHKRHIVHRDLKAENLLLDANMNIKIADFG-----FSNFFKPGELLKtwcgSPPYAAPEVF--EGKEYEGPQLDIWS 184

                        170
                 ....*....|....
gi 505383238 229 LGAVLRTLIVGSPP 242
Cdd:cd14071  185 LGVVLYVLVCGALP 198
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
 86-259 5.88e-06

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: 48.11  E-value: 5.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd06658   66 LFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTR--MNEEQIATVCLSVLRALSYLHNQGVIHRD 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSP---- 241
Cdd:cd06658  144 IKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPEVIS---RLPYGTEVDIWSLGIMVIEMIDGEPpyfn 220

                        170
                 ....*....|....*....
gi 505383238 242 -PPVSVVRSIQDTCKPLVE 259
Cdd:cd06658  221 ePPLQAMRRIRDNLPPRVK 239
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
 87-188 8.87e-06

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: 47.36  E-value: 8.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPN---LLHVLRFWVQNDTAYMGTLF----YSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDE 159
Cdd:cd07865   59 LREIKILQLLKHENvvnLIEICRTKATPYNRYKGSIYlvfeFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRN 138

                         90       100
                 ....*....|....*....|....*....
gi 505383238 160 GYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd07865  139 KILHRDMKAANILITKDGVLKLADFGLAR 167
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
 37-190 9.24e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 47.45  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEfmpsslaVRGEDMTLVLRSERfGKAFSAGLN-SFIQEARLLARFNHPNLLHVLRFWVQNDtaY 115
Cdd:PTZ00024  25 VEKAYDTLTGKIVAIKK-------VKIIEISNDVTKDR-QLVGMCGIHfTTLRELKIMNEIKHENIMGLVDVYVEGD--F 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 116 MGTLF-YSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRT 190
Cdd:PTZ00024  95 INLVMdIMASDLKKVVDRKIRL-TESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARRY 169
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
 83-284 9.88e-06

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: 47.33  E-value: 9.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  83 LNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd06643   46 LEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKII 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNeSEQGPW---TDIYALGAVLRTLIVG 239
Cdd:cd06643  126 HRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIGTPYWMAPEVVMCET-SKDRPYdykADVWSLGVTLIEMAQI 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 505383238 240 SPP-----PVSVVRSIQDTCKPLVElMPQGYSIPLLQAIDKALALHMEDR 284
Cdd:cd06643  205 EPPhhelnPMRVLLKIAKSEPPTLA-QPSRWSPEFKDFLRKCLEKNVDAR 253
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
 85-187 1.01e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 47.97  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLARFNHPNLLHVLRFWVQNDTA------YMGTLFysgTTLSRlreeKPELINEAWIRRMLPMLFGAIKTIHD 158
Cdd:PHA03211 206 SSVHEARLLRRLSHPAVLALLDVRVVGGLTclvlpkYRSDLY---TYLGA----RLRPLGLAQVTAVARQLLSAIDYIHG 278

                         90       100
                 ....*....|....*....|....*....
gi 505383238 159 EGYLHRDISLDNIQIQDNGLPVLLDFGSA 187
Cdd:PHA03211 279 EGIIHRDIKTENVLVNGPEDICLGDFGAA 307
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 36-245 1.05e-05

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: 46.83  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKeFMPsslaVRGEDMTLVLRserfgkafsaglnsfiqEARLLARFNHPNLlhvlrfwVQNDTAY 115
Cdd:cd14110   18 VVRQCEEKRSGQMLAAK-IIP----YKPEDKQLVLR-----------------EYQVLRRLSHPRI-------AQLHSAY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 116 MgtlfySGTTLSRLRE--EKPELI---------NEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDF 184
Cdd:cd14110   69 L-----SPRHLVLIEElcSGPELLynlaernsySEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDL 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383238 185 GSARrtigNLSDETETMLRPGFAPIEQYTDDNESEQG--PWTDIYALGaVLRTLIVGSPPPVS 245
Cdd:cd14110  144 GNAQ----PFNQGKVLMTDKKGDYVETMAPELLEGQGagPQTDIWAIG-VTAFIMLSADYPVS 201
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
 36-189 1.08e-05

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: 47.22  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEfmpsslavrgedmtLVLRSERFGKAFSAglnsfIQEARLLARFNHPNLLHVLRFWVQN--DT 113
Cdd:cd07843   20 VVYRARDKKTGEIVALKK--------------LKMEKEKEGFPITS-----LREINILLKLQHPNIVTVKEVVVGSnlDK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 114 AYMgTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARR 189
Cdd:cd07843   81 IYM-VMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLARE 155
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 85-268 1.19e-05

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: 46.83  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLARFNHPNLLHvLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd14203   36 AFLEEAQIMKKLRHDKLVQ-LYAVVSEEPIYIVTEFMSkGSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIH 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARrtignLSDETETMLRPGFA-PIeQYTDDNESEQGPWT---DIYALGAVLRTLIVG 239
Cdd:cd14203  115 RDLRAANILVGDNLVCKIADFGLAR-----LIEDNEYTARQGAKfPI-KWTAPEAALYGRFTiksDVWSFGILLTELVTK 188

                        170       180       190
                 ....*....|....*....|....*....|.
gi 505383238 240 S--PPPVSVVRSIqdtckplVELMPQGYSIP 268
Cdd:cd14203  189 GrvPYPGMNNREV-------LEQVERGYRMP 212
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
 91-187 1.22e-05

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: 47.03  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  91 RLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPEL--INEAWIRRMLPMLFGAIKTIHDEGYLHRDISL 168
Cdd:cd14052   55 RELTLDGHDNIVQLIDSWEYHGHLYIQTELCENGSLDVFLSELGLLgrLDEFRVWKILVELSLGLRFIHDHHFVHLDLKP 134

                         90
                 ....*....|....*....
gi 505383238 169 DNIQIQDNGLPVLLDFGSA 187
Cdd:cd14052  135 ANVLITFEGTLKIGDFGMA 153
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
 115-241 1.26e-05

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: 47.28  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 115 YMGTLFYSGTTLSRLREEKpELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTigNL 194
Cdd:cd05573   77 YLVMEYMPGGDLMNLLIKY-DVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKM--NK 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 505383238 195 SDETETMLrpgfapIEQYTDDNESEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd05573  154 SGDRESYL------NDSVNTLFQDNVLARRRPHKQRRVRAYSAVGTP 194
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
 33-242 1.34e-05

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: 46.62  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  33 GFGIVYRAWDHQLERTIAIKEFMPSSLAVRGedmtlvlrSERFGKAFSAglnsfIQEARLLARFNHPNLLHVLRFWVQND 112
Cdd:cd14084   18 ACGEVKLAYDKSTCKKVAIKIINKRKFTIGS--------RREINKPRNI-----ETEIEILKKLSHPCIIKIEDFFDAED 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 113 TAYMGTLFYSGTTL-SRLREEK--PELINEAWIRRMLPmlfgAIKTIHDEGYLHRDISLDNIQIQDNGLPVLL---DFGS 186
Cdd:cd14084   85 DYYIVLELMEGGELfDRVVSNKrlKEAICKLYFYQMLL----AVKYLHSNGIIHRDLKPENVLLSSQEEECLIkitDFGL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 187 ARrtignLSDETETML----RPGFAPIEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14084  161 SK-----ILGETSLMKtlcgTPTYLAPEVLRSFGTEGYTRAVDCWSLGVILFICLSGYPP 215
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
 117-242 1.49e-05

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: 46.61  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 117 GTLFYSGTTLSRLREEkpelinEAwiRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSD 196
Cdd:cd14078   86 GELFDYIVAKDRLSED------EA--RVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGMDH 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 505383238 197 ETETML-RPGFAPIE-----QYTddneseqGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14078  158 HLETCCgSPAYAAPEliqgkPYI-------GSEADVWSMGVLLYALLCGFLP 202
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 64-286 1.50e-05

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: 46.26  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  64 EDMTlvlRSERfgkafSAGLNsfiqEARLLARFNHPNLLHVLRFWVQnDTAYMGTLFYS--GTTLSRLREEKPELINEAW 141
Cdd:cd08220   36 EQMT---KEER-----QAALN----EVKVLSMLHHPNIIEYYESFLE-DKALMIVMEYApgGTLFEYIQQRKGSLLSEEE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 142 IRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLL-DFGSARRtignLSDETETMLRPGfAPIeqYTDDNESEQ 220
Cdd:cd08220  103 ILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVVKIgDFGISKI----LSSKSKAYTVVG-TPC--YISPELCEG 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 221 GPW---TDIYALGAVLRTLIV------GSPPPVSVVRSIQDTCKPLVELmpqgYSIPLLQAIDKALALHMEDRPQ 286
Cdd:cd08220  176 KPYnqkSDIWALGCVLYELASlkrafeAANLPALVLKIMRGTFAPISDR----YSEELRHLILSMLHLDPNKRPT 246
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
 85-189 1.51e-05

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: 46.92  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEAR-LLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd05601   46 SFFEEERdIMAKANSPWITKLQYAFQDSENLYLVMEYHPGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVH 125

                         90       100
                 ....*....|....*....|....*.
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARR 189
Cdd:cd05601  126 RDIKPENILIDRTGHIKLADFGSAAK 151
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
 86-242 1.53e-05

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: 46.61  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTA-----YMGTLFYSGTT---LSRLREEKPELInEAWIRRMLP-MLFGAIKTi 156
Cdd:cd14032   47 FKEEAEMLKGLQHPNIVRFYDFWESCAKGkrcivLVTELMTSGTLktyLKRFKVMKPKVL-RSWCRQILKgLLFLHTRT- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 157 hdEGYLHRDISLDNI---------QIQDNGLPVLLDFGSARRTIGNlsdetetmlrPGFAPIEQYTDDNESEqgpwTDIY 227
Cdd:cd14032  125 --PPIIHRDLKCDNIfitgptgsvKIGDLGLATLKRASFAKSVIGT----------PEFMAPEMYEEHYDES----VDVY 188

                        170
                 ....*....|....*
gi 505383238 228 ALGAVLRTLIVGSPP 242
Cdd:cd14032  189 AFGMCMLEMATSEYP 203
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 77-242 1.57e-05

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: 46.56  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  77 KAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL-SRLREEKpeLINEAWIRRMLPMLFGAIKT 155
Cdd:cd14167   39 KALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELfDRIVEKG--FYTERDASKLIFQILDAVKY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 156 IHDEGYLHRDISLDN-----------IQIQDNGLPVLLDFGSArrtignLSDETETmlrPGFAPIEQYTddneseQGPWT 224
Cdd:cd14167  117 LHDMGIVHRDLKPENllyysldedskIMISDFGLSKIEGSGSV------MSTACGT---PGYVAPEVLA------QKPYS 181

                        170       180
                 ....*....|....*....|.
gi 505383238 225 ---DIYALGAVLRTLIVGSPP 242
Cdd:cd14167  182 kavDCWSIGVIAYILLCGYPP 202
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
 86-233 1.58e-05

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: 46.38  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYM-------GTLfysgttLSRLREEKPELINEAW----IRRMLPMLFGA-- 152
Cdd:cd00192   43 FLKEARVMKKLGHPNVVRLLGVCTEEEPLYLvmeymegGDL------LDFLRKSRPVFPSPEPstlsLKDLLSFAIQIak 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 153 -IKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIgnlSDETETMLRPGFAPI-----EQYTDDNESEQgpwTDI 226
Cdd:cd00192  117 gMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIY---DDDYYRKKTGGKLPIrwmapESLKDGIFTSK---SDV 190


                 ....*..
gi 505383238 227 YALGAVL 233
Cdd:cd00192  191 WSFGVLL 197
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
 88-242 1.65e-05

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: 46.49  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLH-------VLRFWVQNDTAYMGTLFYSGTTLSRLREEKPEL-INEawirrmlpmLFGAIKTIHDE 159
Cdd:cd14116   54 REVEIQSHLRHPNILRlygyfhdATRVYLILEYAPLGTVYRELQKLSKFDEQRTATyITE---------LANALSYCHSK 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 160 GYLHRDISLDNIQIQDNGLPVLLDFG------SARRTI--GNLSDETETMlrpgfapIEQYTDDNEseqgpwTDIYALGA 231
Cdd:cd14116  125 RVIHRDIKPENLLLGSAGELKIADFGwsvhapSSRRTTlcGTLDYLPPEM-------IEGRMHDEK------VDLWSLGV 191

                        170
                 ....*....|.
gi 505383238 232 VLRTLIVGSPP 242
Cdd:cd14116  192 LCYEFLVGKPP 202
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
 83-188 1.66e-05

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: 46.26  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  83 LNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGY 161
Cdd:cd05052   46 VEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPyGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNF 125

                         90       100
                 ....*....|....*....|....*..
gi 505383238 162 LHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05052  126 IHRDLAARNCLVGENHLVKVADFGLSR 152
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
 86-256 1.84e-05

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: 46.55  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd06657   64 LFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTR--MNEEQIAAVCLAVLKALSVLHAQGVIHRD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSP---- 241
Cdd:cd06657  142 IKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELIS---RLPYGPEVDIWSLGIMVIEMVDGEPpyfn 218

                        170
                 ....*....|....*.
gi 505383238 242 -PPVSVVRSIQDTCKP 256
Cdd:cd06657  219 ePPLKAMKMIRDNLPP 234
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
 86-201 1.86e-05

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: 46.21  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSR-LREEKPELINEAWIrRMLPMLFGAIKTIHDEGYLHR 164
Cdd:cd05033   52 FLTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENGSLDKfLRENDGKFTVTQLV-GMLRGIASGMKYLSEMNYVHR 130

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSARRtIGNLSDETETM 201
Cdd:cd05033  131 DLAARNILVNSDLVCKVSDFGLSRR-LEDSEATYTTK 166
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
 89-233 1.99e-05

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: 46.26  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL----SRLREEK----PELINEAWIRRMLpmlfgAIKTIHDEG 160
Cdd:cd08222   52 EAKLLSKLDHPAIVKFHDSFVEKESFCIVTEYCEGGDLddkiSEYKKSGttidENQILDWFIQLLL-----AVQYMHERR 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 161 YLHRDISLDNIQIQDNGLPVlLDFGSARRTIGNlSDETETM------LRPGFAPIEQYTDDneseqgpwTDIYALGAVL 233
Cdd:cd08222  127 ILHRDLKAKNIFLKNNVIKV-GDFGISRILMGT-SDLATTFtgtpyyMSPEVLKHEGYNSK--------SDIWSLGCIL 195
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
 36-276 2.00e-05

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: 46.41  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEFM-PSSLAVrgedmtLVLRSERfgkafsaglnsfiqEARLLARFNHPNLLHVLRFWVQ--ND 112
Cdd:cd07856   25 LVCSARDQLTGQNVAVKKIMkPFSTPV------LAKRTYR--------------ELKLLKHLRHENIISLSDIFISplED 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 113 TAYMGTLFysGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIG 192
Cdd:cd07856   85 IYFVTELL--GTDLHRLLTSRP--LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 193 NLSDETETmlRPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSP--------------------PPVSVVRSI-- 250
Cdd:cd07856  161 QMTGYVST--RYYRAPEIMLTWQKYDVE---VDIWSAGCIFAEMLEGKPlfpgkdhvnqfsiitellgtPPDDVINTIcs 235

                        250       260
                 ....*....|....*....|....*.
gi 505383238 251 QDTCKpLVELMPQGYSIPLLQAIDKA 276
Cdd:cd07856  236 ENTLR-FVQSLPKRERVPFSEKFKNA 260
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
 88-188 2.04e-05

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: 46.24  E-value: 2.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd06632   51 QEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGGSIHKLLQRYGAF-EEPVIRLYTRQILSGLAYLHSRNTVHRDIK 129

                         90       100
                 ....*....|....*....|.
gi 505383238 168 LDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd06632  130 GANILVDTNGVVKLADFGMAK 150
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
 88-289 2.10e-05

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: 46.22  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd06641   51 QEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGP--LDETQIATILREILKGLDYLHSEKKIHRDIK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGSArrtiGNLSDetETMLRPGF-------AP--IEQYTDDNESeqgpwtDIYALGAVLRTLIV 238
Cdd:cd06641  129 AANVLLSEHGEVKLADFGVA----GQLTD--TQIKRN*FvgtpfwmAPevIKQSAYDSKA------DIWSLGITAIELAR 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238 239 GSPP-----PVSVVRSIQDTCKPLVElmpQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06641  197 GEPPhselhPMKVLFLIPKNNPPTLE---GNYSKPLKEFVEACLNKEPSFRPTAKE 249
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
 85-181 2.32e-05

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. 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. The STRAD-beta 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: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 46.40  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLAR-FNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELINEAWIRRMLpmlFGAIKT---IHDE 159
Cdd:cd08226   44 KALQNEVVLSHfFRHPNIMTHWTVFTEGSWLWVISPFMAyGSARGLLKTYFPEGMNEALIGNIL---YGAIKAlnyLHQN 120

                         90       100
                 ....*....|....*....|..
gi 505383238 160 GYLHRDISLDNIQIQDNGLPVL 181
Cdd:cd08226  121 GCIHRSVKASHILISGDGLVSL 142
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 87-242 2.41e-05

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: 45.79  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRL---REEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd08228   50 VKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADAGDLSQMikyFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMH 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd08228  130 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFK---SDIWSLGCLLYEMAALQSP 205
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
 83-242 2.43e-05

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: 45.62  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  83 LNSFI-QEARLLARFNHPNLLHVLRFW-VQNDTAYMGTLFYSGTTLSRLREEKpeLINEAWIRRMLPMLFGAIKTIHDEG 160
Cdd:cd14164   43 VQKFLpRELSILRRVNHPNIVQMFECIeVANGRLYIVMEAAATDLLQKIQEVH--HIPKDLARDMFAQMVGAVNYLHDMN 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 161 YLHRDISLDNIQIQDNGLPV-LLDFGSARRtignLSDETEtmLRPGFAPIEQYTDDNESEQGPWT----DIYALGAVLRT 235
Cdd:cd14164  121 IVHRDLKCENILLSADDRKIkIADFGFARF----VEDYPE--LSTTFCGSRAYTPPEVILGTPYDpkkyDVWSLGVVLYV 194


                 ....*..
gi 505383238 236 LIVGSPP 242
Cdd:cd14164  195 MVTGTMP 201
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
 92-289 2.44e-05

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: 46.16  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  92 LLARFNHPNllhVLRFW--------VQNDTAYMGTLFYSGTTLSRLRE---EKPELINEAWIRRMLPMLFGAIKTIHDEG 160
Cdd:cd06638   68 LKALSDHPN---VVKFYgmyykkdvKNGDQLWLVLELCNGGSVTDLVKgflKRGERMEEPIIAYILHEALMGLQHLHVNK 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 161 YLHRDISLDNIQIQDNGLPVLLDFG-----SARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQgpwTDIYALGAVLRT 235
Cdd:cd06638  145 TIHRDVKGNNILLTTEGGVKLVDFGvsaqlTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTYDAR---CDVWSLGITAIE 221

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 236 LIVGSPP-----PVSVVRSIQDTCKPLVElMPQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06638  222 LGDGDPPladlhPMRALFKIPRNPPPTLH-QPELWSNEFNDFIRKCLTKDYEKRPTVSD 279
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
 152-242 2.50e-05

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: 46.06  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 152 AIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARrtIGnLSDETETMLRPGFAPIEQYTDDNE-------------- 217
Cdd:cd05579  105 ALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSK--VG-LVRRQIKLSIQKKSNGAPEKEDRRivgtpdylapeill 181

                         90       100
                 ....*....|....*....|....*.
gi 505383238 218 -SEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd05579  182 gQGHGKTVDWWSLGVILYEFLVGIPP 207
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
 93-242 3.04e-05

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: 46.05  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  93 LARfNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLsRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQ 172
Cdd:cd05590   51 LAR-NHPFLTQLYCCFQTPDRLFFVMEFVNGGDL-MFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVL 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383238 173 IQDNGLPVLLDFGSARRTIGNLSDETETMLRPGF-AP-IEQytddnESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd05590  129 LDHEGHCKLADFGMCKEGIFNGKTTSTFCGTPDYiAPeILQ-----EMLYGPSVDWWAMGVLLYEMLCGHAP 195
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
 88-242 3.12e-05

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: 45.40  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREekPEL-INEAWIRRMLPMLFGAIKTIHDEGYLHRDI 166
Cdd:cd14069   49 KEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGELFDKIE--PDVgMPEDVAQFYFQQLMAGLKYLHSCGITHRDI 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 167 SLDNIQIQDNGLPVLLDFGSARRTIGNlSDETETMLRPGFAP-IEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14069  127 KPENLLLDENDNLKISDFGLATVFRYK-GKERLLNKMCGTLPyVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELP 202
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
 84-242 3.51e-05

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: 45.59  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFY-SGTTLSRLREEK--PELineAWIRRmLPMLFG---AIKTIH 157
Cdd:cd14159   37 NSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLpNGSLEDRLHCQVscPCL---SWSQR-LHVLLGtarAIQYLH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 158 DE--GYLHRDISLDNIQIQDNGLPVLLDFGSAR-----RTIGNLSDETETMLRPG---FAPiEQYTDDneSEQGPWTDIY 227
Cdd:cd14159  113 SDspSLIHGDVKSSNILLDAALNPKLGDFGLARfsrrpKQPGMSSTLARTQTVRGtlaYLP-EEYVKT--GTLSVEIDVY 189

                        170
                 ....*....|....*
gi 505383238 228 ALGAVLRTLIVGSPP 242
Cdd:cd14159  190 SFGVVLLELLTGRRA 204
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
 86-239 3.58e-05

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: 45.26  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDT-----AYM--GTLFYSgttLSRLREEKPelinEAWIRRmLPMLFGAIKTIHd 158
Cdd:cd14160   39 FLSELEVLLLFQHPNILELAAYFTETEKfclvyPYMqnGTLFDR---LQCHGVTKP----LSWHER-INILIGIAKAIH- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 egYLHR---------DISLDNIQIQDNGLPVLLDFGSARRTiGNLSDETETMLRP-------GFAPIEQYTDDNESEQgp 222
Cdd:cd14160  110 --YLHNsqpctvicgNISSANILLDDQMQPKLTDFALAHFR-PHLEDQSCTINMTtalhkhlWYMPEEYIRQGKLSVK-- 184

                        170
                 ....*....|....*..
gi 505383238 223 wTDIYALGAVLRTLIVG 239
Cdd:cd14160  185 -TDVYSFGIVIMEVLTG 200
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
 86-188 3.58e-05

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: 45.13  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYM-GTLFYSGTTLSRLREEKPELIneawIRRMLPMLFGA---IKTIHDEGY 161
Cdd:cd05041   40 FLQEARILKQYDHPNIVKLIGVCVQKQPIMIvMELVPGGSLLTFLRKKGARLT----VKQLLQMCLDAaagMEYLESKNC 115

                         90       100
                 ....*....|....*....|....*..
gi 505383238 162 LHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05041  116 IHRDLAARNCLVGENNVLKISDFGMSR 142
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
 87-237 4.97e-05

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 44.77  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGaIKTIHDEGYLHRDI 166
Cdd:cd14155   36 LREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQLLDSNEPLSWTVRVKLALDIARG-LSYLHSKGIFHRDL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 167 SLDNIQIQ--DNGL-PVLLDFGSARRtIGNLSDETETMLRPG----FAPieqytddnESEQGPW----TDIYALGAVLRT 235
Cdd:cd14155  115 TSKNCLIKrdENGYtAVVGDFGLAEK-IPDYSDGKEKLAVVGspywMAP--------EVLRGEPynekADVFSYGIILCE 185


                 ..
gi 505383238 236 LI 237
Cdd:cd14155  186 II 187
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
 23-188 4.98e-05

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: 45.19  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKEfmpsslaVRgedmtlvLRSERFGKAFSAglnsfIQEARLLARFNHPNLL 102
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKK-------IR-------LDTETEGVPSTA-----IREISLLKELNHPNIV 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLL 182
Cdd:cd07860   63 KLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLA 142


                 ....*.
gi 505383238 183 DFGSAR 188
Cdd:cd07860  143 DFGLAR 148
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
 84-233 5.01e-05

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: 44.79  E-value: 5.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDtaymGTLFYSGTTLSRLRE----------EKPELinEAWIRRM-----LPM 148
Cdd:cd14047   44 EKAEREVKALAKLDHPNIVRYNGCWDGFD----YDPETSSSNSSRSKTkclfiqmefcEKGTL--ESWIEKRngeklDKV 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 149 ----LFGAIKT----IHDEGYLHRDISLDNIQIQDNGLPVLLDFG--SARRTIGNLSDE--TETMLRPgfapiEQYTDDN 216
Cdd:cd14047  118 laleIFEQITKgveyIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGlvTSLKNDGKRTKSkgTLSYMSP-----EQISSQD 192

                        170
                 ....*....|....*..
gi 505383238 217 ESEQgpwTDIYALGAVL 233
Cdd:cd14047  193 YGKE---VDIYALGLIL 206
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
 86-191 5.47e-05

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: 44.85  E-value: 5.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFY-SGTTLSRLREEKPELINEAWIRrMLPMLFGAIKTIHDEGYLHR 164
Cdd:cd05114   46 FIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMeNGCLLNYLRQRRGKLSRDMLLS-MCQDVCEGMEYLERNNFIHR 124

                         90       100
                 ....*....|....*....|....*..
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSARRTI 191
Cdd:cd05114  125 DLAARNCLVNDTGVVKVSDFGMTRYVL 151
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
 85-268 6.02e-05

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 44.68  E-value: 6.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLARFNHPNLLHVLRFwVQNDTAYMGTLFYS-GTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd05071   50 AFLQEAQVMKKLRHEKLVQLYAV-VSEEPIYIVTEYMSkGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVH 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARrtignLSDETETMLRPGFAPIEQYTDDNESEQGPWT---DIYALGAVLRTLIVGS 240
Cdd:cd05071  129 RDLRAANILVGENLVCKVADFGLAR-----LIEDNEYTARQGAKFPIKWTAPEAALYGRFTiksDVWSFGILLTELTTKG 203

                        170       180       190
                 ....*....|....*....|....*....|
gi 505383238 241 --PPPVSVVRSIQDTCKplvelmpQGYSIP 268
Cdd:cd05071  204 rvPYPGMVNREVLDQVE-------RGYRMP 226
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
 21-285 6.21e-05

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: 44.54  E-value: 6.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  21 NEFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFmpsSLAVRGEDMTLVLrserfgkafsaglnsfiQEARLLARFNHPN 100
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVI---DLEEAEDEIEDIQ-----------------QEIQFLSQCDSPY 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 101 LlhvlrfwvqndTAYMGTlFYSGTTL----------SRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDN 170
Cdd:cd06609   61 I-----------TKYYGS-FLKGSKLwiimeycgggSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAAN 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 171 IQIQDNGLPVLLDFGSArrtiGNLSDeteTMLR-------PgF--AP--IEQYTDDNESeqgpwtDIYALGAVLRTLIVG 239
Cdd:cd06609  129 ILLSEEGDVKLADFGVS----GQLTS---TMSKrntfvgtP-FwmAPevIKQSGYDEKA------DIWSLGITAIELAKG 194

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383238 240 SPP-----PVSVVRSIQDTCKPLVElmPQGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd06609  195 EPPlsdlhPMRVLFLIPKNNPPSLE--GNKFSKPFKDFVELCLNKDPKERP 243
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
 152-258 7.02e-05

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: 44.91  E-value: 7.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 152 AIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFG---------SARRTIGNlSDET--ETMLRPGfapieqYTDDneseq 220
Cdd:cd05599  113 AIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGlctglkkshLAYSTVGT-PDYIapEVFLQKG------YGKE----- 180

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505383238 221 gpwTDIYALGAVLRTLIVGSPPPVSvvRSIQDTCKPLV 258
Cdd:cd05599  181 ---CDWWSLGVIMYEMLIGYPPFCS--DDPQETCRKIM 213
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
 86-188 7.16e-05

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: 44.47  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL-SRLREEKPELIneawIRRMLPMLFG---AIKTIHDEGY 161
Cdd:cd05066   52 FLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGSLdAFLRKHDGQFT----VIQLVGMLRGiasGMKYLSDMGY 127

                         90       100
                 ....*....|....*....|....*..
gi 505383238 162 LHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05066  128 VHRDLAARNILVNSNLVCKVSDFGLSR 154
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
 93-243 8.75e-05

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: 43.89  E-value: 8.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  93 LARFNHPNLLHVLRFWVQNDTAYMGTLFY------SGTTLSRLREEKPEL-INEA--WIRRMLPmlfgAIKTIHDEGYLH 163
Cdd:cd14012   52 LKKLRHPNLVSYLAFSIERRGRSDGWKVYllteyaPGGSLSELLDSVGSVpLDTArrWTLQLLE----ALEYLHRNGVVH 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQI---QDNGLPVLLDFGSARRTIGNLSDETE-TMLRPGFAPIEQYTDDNESeqGPWTDIYALGAVLRTLIVG 239
Cdd:cd14012  128 KSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSLdEFKQTYWLPPELAQGSKSP--TRKTDVWDLGLLFLQMLFG 205


                 ....
gi 505383238 240 SPPP 243
Cdd:cd14012  206 LDVL 209
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 87-190 8.87e-05

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 42.64  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLAR-----FNHPNLLHVLRfwvqnDTAYMGTLFYSGTTLSRLREEKPeLINEAWIRrmlpmLFGAIKTIHDEGY 161
Cdd:COG3642    4 RREARLLRElreagVPVPKVLDVDP-----DDADLVMEYIEGETLADLLEEGE-LPPELLRE-----LGRLLARLHRAGI 72

                         90       100
                 ....*....|....*....|....*....
gi 505383238 162 LHRDISLDNIQIQDNGLpVLLDFGSARRT 190
Cdd:COG3642   73 VHGDLTTSNILVDDGGV-YLIDFGLARYS 100
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
 19-230 9.21e-05

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: 44.22  E-value: 9.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  19 RFNEFEIKevIGGGGFGIVYRAWDHQLERTIAIKEFMPSSLAvrgedmtlvlRSERfgkafsaglNSFIQEARLLARFNH 98
Cdd:cd14033    1 RFLKFNIE--IGRGSFKTVYRGLDTETTVEVAWCELQTRKLS----------KGER---------QRFSEEVEMLKGLQH 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  99 PNLLHVLRFWV-----QNDTAYMGTLFYSGT---TLSRLREEKPELInEAWIRRMLPMLfgaiKTIHDEG--YLHRDISL 168
Cdd:cd14033   60 PNIVRFYDSWKstvrgHKCIILVTELMTSGTlktYLKRFREMKLKLL-QRWSRQILKGL----HFLHSRCppILHRDLKC 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383238 169 DNI---------QIQDNGLPVLLDFGSARRTIGNlsdetetmlrPGFAPIEQYtddnESEQGPWTDIYALG 230
Cdd:cd14033  135 DNIfitgptgsvKIGDLGLATLKRASFAKSVIGT----------PEFMAPEMY----EEKYDEAVDVYAFG 191
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
 97-298 1.07e-04

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: 44.21  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  97 NHPNLLHVLRFWVQNDTAYMGTLFY--------SGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISL 168
Cdd:cd06639   77 NHPNVVKFYGMFYKADQYVGGQLWLvlelcnggSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKG 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 169 DNIQIQDNGLPVLLDFG-----SARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP- 242
Cdd:cd06639  157 NNILLTTEGGVKLVDFGvsaqlTSARLRRNTSVGTPFWMAPEVIACEQQYDYSYDAR---CDVWSLGITAIELADGDPPl 233

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 243 ----PVSVVRSIQDTCKPLVeLMPQGYSIPLLQAIDKALALHMEDRPQSIEefaaLIEMP 298
Cdd:cd06639  234 fdmhPVKALFKIPRNPPPTL-LNPEKWCRGFSHFISQCLIKDFEKRPSVTH----LLEHP 288
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 123-242 1.15e-04

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: 44.21  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 123 GTTLSRLReeKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPV---LLDFGSARrtignLSDETE 199
Cdd:cd14092   84 GELLERIR--KKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAeikIVDFGFAR-----LKPENQ 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383238 200 TMLRPGF-----AP--IEQYTDDNE-SEQgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd14092  157 PLKTPCFtlpyaAPevLKQALSTQGyDES---CDLWSLGVILYTMLSGQVP 204
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 77-188 1.22e-04

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: 43.55  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  77 KAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGT-LFYSGTTLSRLREEK-----PELINeawirrMLPMLF 150
Cdd:cd05068   41 KPGTMDPEDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITeLMKHGSLLEYLQGKGrslqlPQLID------MAAQVA 114

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 505383238 151 GAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05068  115 SGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLAR 152
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
 123-242 1.24e-04

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 43.79  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 123 GTTLSRLREEKPE-LINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQI----QDNGLPVLLDFGSARRTIgNLSDE 197
Cdd:cd14017   79 GPNLAELRRSQPRgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGLARQYT-NKDGE 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 505383238 198 TETMLR--PGFAPIEQYTDDN---ESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14017  158 VERPPRnaAGFRGTVRYASVNahrNKEQGRRDDLWSWFYMLIEFVTGQLP 207
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
 163-285 1.24e-04

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: 43.86  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSA---------RRTIGNLSDETETMLRPGF-AP--IEQYTDDNESEQgpwTDIYALG 230
Cdd:cd13985  128 HRDIKIENILFSNTGRFKLCDFGSAttehyplerAEEVNIIEEEIQKNTTPMYrAPemIDLYSKKPIGEK---ADIWALG 204

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 231 AVLRTLIVGSPP--PVSVVRSIqdTCKPLVELMPqGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd13985  205 CLLYKLCFFKLPfdESSKLAIV--AGKYSIPEQP-RYSPELHDLIRHMLTPDPAERP 258
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
 89-256 1.27e-04

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: 43.59  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL------SRLREEKPELINEAWIRrmlpmlfgAIKTIHDEGYL 162
Cdd:cd06648   54 EVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALtdivthTRMNEEQIATVCRAVLK--------ALSFLHSQGVI 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSArrtiGNLSDE---------TETMLRPGFAPIEQYtddneseqGPWTDIYALGAVL 233
Cdd:cd06648  126 HRDIKSDSILLTSDGRVKLSDFGFC----AQVSKEvprrkslvgTPYWMAPEVISRLPY--------GTEVDIWSLGIMV 193

                        170       180
                 ....*....|....*....|....*...
gi 505383238 234 RTLIVGSPP-----PVSVVRSIQDTCKP 256
Cdd:cd06648  194 IEMVDGEPPyfnepPLQAMKRIRDNEPP 221
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
 36-203 1.28e-04

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: 43.43  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTI-AIKEFMPSSLAvrgedmtlvlrserfgkafSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTA 114
Cdd:cd14121   10 TVYKAYRKSGAREVvAVKCVSKSSLN-------------------KASTENLLTEIELLKKLKHPHIVELKDFQWDEEHI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 115 YMGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVL--LDFGSARRtig 192
Cdd:cd14121   71 YLIMEYCSGGDLSRFIRSRRTL-PESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLklADFGFAQH--- 146

                        170
                 ....*....|..
gi 505383238 193 nLSDETE-TMLR 203
Cdd:cd14121  147 -LKPNDEaHSLR 157
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 88-242 1.34e-04

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: 43.50  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd06645   57 QEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGPL-SESQIAYVSRETLQGLYYLHSKGKMHRDIK 135

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 168 LDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd06645  136 GANILLTDNGHVKLADFGVSAQITATIAKRKSFIGTPYWMAPEVAAVERKGGYNQLCDIWAVGITAIELAELQPP 210
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
 88-289 1.60e-04

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: 43.51  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTtlSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd06642   51 QEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGG--SALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 168 LDNIQIQDNGLPVLLDFGSArrtiGNLSDetETMLRPGFAPIEQYTDDNESEQGPW---TDIYALGAVLRTLIVGSPP-- 242
Cdd:cd06642  129 AANVLLSEQGDVKLADFGVA----GQLTD--TQIKRNTFVGTPFWMAPEVIKQSAYdfkADIWSLGITAIELAKGEPPns 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 505383238 243 ---PVSVVRSIQDTCKPLVElmpQGYSIPLLQAIDKALALHMEDRPQSIE 289
Cdd:cd06642  203 dlhPMRVLFLIPKNSPPTLE---GQHSKPFKEFVEACLNKDPRFRPTAKE 249
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 66-242 1.70e-04

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: 43.84  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  66 MTLVLRSERFGKAFSAglnsFIQEARLLARFNHPNLLHVLRFWVQNDT-AYMGTLFYSGTTLSRLREEKPelINEAWIRR 144
Cdd:cd05622  103 MKLLSKFEMIKRSDSA----FFWEERDIMAFANSPWVVQLFYAFQDDRyLYMVMEYMPGGDLVNLMSNYD--VPEKWARF 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 145 MLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTignlsdETETMLR-------PGF-APIEQYTDDN 216
Cdd:cd05622  177 YTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKM------NKEGMVRcdtavgtPDYiSPEVLKSQGG 250

                        170       180
                 ....*....|....*....|....*.
gi 505383238 217 ESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd05622  251 DGYYGRECDWWSVGVFLYEMLVGDTP 276
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
 85-280 1.73e-04

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: 43.52  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLARFNHPNLLHVLRFwVQNDTAYMGTLFYS-GTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd05070   50 SFLEEAQIMKKLKHDKLVQLYAV-VSEEPIYIVTEYMSkGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIH 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARrtignLSDETETMLRPGFAPIEQYTDDNESEQGPWT---DIYALGAVLRTLIVGS 240
Cdd:cd05070  129 RDLRSANILVGNGLICKIADFGLAR-----LIEDNEYTARQGAKFPIKWTAPEAALYGRFTiksDVWSFGILLTELVTKG 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 505383238 241 PPPVSVVRSiqdtcKPLVELMPQGYSIPLLQaiDKALALH 280
Cdd:cd05070  204 RVPYPGMNN-----REVLEQVERGYRMPCPQ--DCPISLH 236
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
 23-188 1.82e-04

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: 43.67  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMP----SSLAVRgedmtlVLRserfgkafsaglnsfiqEARLLARFNH 98
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfddLIDAKR------ILR-----------------EIKILRHLKH 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  99 PNLLHVLRFWVQNDTAYMGTLF----YSGTTLSR-LREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQI 173
Cdd:cd07834   59 ENIIGLLDILRPPSPEEFNDVYivteLMETDLHKvIKSPQP--LTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILV 136

                        170
                 ....*....|....*
gi 505383238 174 QDNGLPVLLDFGSAR 188
Cdd:cd07834  137 NSNCDLKICDFGLAR 151
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
 37-187 1.83e-04

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: 43.21  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEfMPSSlavrgedmtlvlrserfGKAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYM 116
Cdd:cd06607   17 VYYARNKRTSEVVAIKK-MSYS-----------------GKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383238 117 gTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSA 187
Cdd:cd06607   79 -VMEYCLGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSA 148
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
 81-298 1.84e-04

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: 43.30  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  81 AGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPEL--INEAWIRRMLPMLFGAIKTIHD 158
Cdd:cd06622   41 SKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGSLDKLYAGGVATegIPEDVLRRITYAVVKGLKFLKE 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 E-GYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSdETETMLRPGFAPiEQYTDDNESEQGPWT---DIYALGAVLR 234
Cdd:cd06622  121 EhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLA-KTNIGCQSYMAP-ERIKSGGPNQNPTYTvqsDVWSLGLSIL 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 235 TLIVGS---PPPV--SVVRSIQDTCKPLVELMPQGYSIPLLQAIDKALALHMEDRPqsieEFAALIEMP 298
Cdd:cd06622  199 EMALGRypyPPETyaNIFAQLSAIVDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRP----TYAQLLEHP 263
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
 87-241 1.88e-04

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: 43.41  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPN--LLHVLrfwVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHR 164
Cdd:cd07870   46 IREASLLKGLKHANivLLHDI---IHTKETLTFVFEYMHTDLAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHR 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSAR-RTI--GNLSDETETM-LRPGFAPI--EQYTDDneseqgpwTDIYALGAVLRTLIV 238
Cdd:cd07870  123 DLKPQNLLISYLGELKLADFGLARaKSIpsQTYSSEVVTLwYRPPDVLLgaTDYSSA--------LDIWGAGCIFIEMLQ 194


                 ...
gi 505383238 239 GSP 241
Cdd:cd07870  195 GQP 197
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 88-242 1.88e-04

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: 43.16  E-value: 1.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTAYM-------GTLFYSGTTLSRLREEKPelineawiRRMLPMLFGAIKTIHDEG 160
Cdd:cd14663   49 REIAIMKLLRHPNIVELHEVMATKTKIFFvmelvtgGELFSKIAKNGRLKEDKA--------RKYFQQLIDAVDYCHSRG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 161 YLHRDISLDNIQIQDNGLPVLLDFG-----SARRTIGNLSDETETmlrPGFAPIEQYTDDneSEQGPWTDIYALGAVLRT 235
Cdd:cd14663  121 VFHRDLKPENLLLDEDGNLKISDFGlsalsEQFRQDGLLHTTCGT---PNYVAPEVLARR--GYDGAKADIWSCGVILFV 195


                 ....*..
gi 505383238 236 LIVGSPP 242
Cdd:cd14663  196 LLAGYLP 202
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
 77-242 1.90e-04

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: 43.14  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  77 KAFSAGLNSFIQEARLlARFNHPNLLHVLRFWVQNDTAYMGTL---FYSGTTL-SRLREEKPELINEAWIRRMLPMLfGA 152
Cdd:cd13979   38 RKNRASRQSFWAELNA-ARLRHENIVRVLAAETGTDFASLGLIimeYCGNGTLqQLIYEGSEPLPLAHRILISLDIA-RA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 153 IKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGnlSDETETMLR-----PGFAPIEQYTDDnesEQGPWTDIY 227
Cdd:cd13979  116 LRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGE--GNEVGTPRShiggtYTYRAPELLKGE---RVTPKADIY 190

                        170
                 ....*....|....*
gi 505383238 228 ALGAVLRTLIVGSPP 242
Cdd:cd13979  191 SFGITLWQMLTRELP 205
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
 86-256 2.01e-04

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: 43.17  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNllhVLRFWVQNDTAYMGT--------LFYSGTT---LSRLREEKPELInEAWIRRMLPmlfgAIK 154
Cdd:cd14031   56 FKEEAEMLKGLQHPN---IVRFYDSWESVLKGKkcivlvteLMTSGTLktyLKRFKVMKPKVL-RSWCRQILK----GLQ 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 155 TIHDEG--YLHRDISLDNI---------QIQDNGLPVLLDFGSARRTIGNlsdetetmlrPGFAPIEQYTDDNESEqgpw 223
Cdd:cd14031  128 FLHTRTppIIHRDLKCDNIfitgptgsvKIGDLGLATLMRTSFAKSVIGT----------PEFMAPEMYEEHYDES---- 193

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 505383238 224 TDIYALGAVLRTLIVGSPP------PVSVVRSIQDTCKP 256
Cdd:cd14031  194 VDVYAFGMCMLEMATSEYPysecqnAAQIYRKVTSGIKP 232
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
 88-242 2.01e-04

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: 43.37  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHV------LRFWVqNDTAYMGTLFYSGTTLSRLREeKPEL---INEAWIRRMLPMLFGAIKTIHD 158
Cdd:cd14039   40 HEIQIMKKLNHPNVVKAcdvpeeMNFLV-NDVPLLAMEYCSGGDLRKLLN-KPENccgLKESQVLSLLSDIGSGIQYLHE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 EGYLHRDISLDNIQIQD-NGLPV--LLDFGSARrtignlsDETETMLRPGFAPIEQYTDDNESEQGPWT---DIYALGAV 232
Cdd:cd14039  118 NKIIHRDLKPENIVLQEiNGKIVhkIIDLGYAK-------DLDQGSLCTSFVGTLQYLAPELFENKSYTvtvDYWSFGTM 190

                        170
                 ....*....|
gi 505383238 233 LRTLIVGSPP 242
Cdd:cd14039  191 VFECIAGFRP 200
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
 89-242 2.12e-04

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: 43.01  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTAYM-------GTLFYSGTTLSRLREEKPELineawirrMLPMLFGAIKTIHDEGY 161
Cdd:cd14185   48 EILIIKSLSHPNIVKLFEVYETEKEIYLileyvrgGDLFDAIIESVKFTEHDAAL--------MIIDLCEALVYIHSKHI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 162 LHRDISLDNIQIQDNGLPV----LLDFGSARRTIGNLSDETETmlrPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLI 237
Cdd:cd14185  120 VHRDLKPENLLVQHNPDKSttlkLADFGLAKYVTGPIFTVCGT---PTYVAPEILS---EKGYGLEVDMWAAGVILYILL 193


                 ....*
gi 505383238 238 VGSPP 242
Cdd:cd14185  194 CGFPP 198
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 97-185 2.13e-04

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 41.27  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  97 NHPNLLHVLRfwvQNDTAYMGTLFYSGTTLSR--LREEKPELINEAWIRRMLpmlfGAIKTIHDEGYLHRDISLDNIQIQ 174
Cdd:cd13968   53 NIPKVLVTED---VDGPNILLMELVKGGTLIAytQEEELDEKDVESIMYQLA----ECMRLLHSFHLIHRDLNNDNILLS 125

                         90
                 ....*....|.
gi 505383238 175 DNGLPVLLDFG 185
Cdd:cd13968  126 EDGNVKLIDFG 136
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
 152-242 2.13e-04

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: 43.25  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 152 AIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGF-AP-IEQytddnESEQGPWTDIYAL 229
Cdd:cd05591  108 ALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFCGTPDYiAPeILQ-----ELEYGPSVDWWAL 182

                         90
                 ....*....|...
gi 505383238 230 GAVLRTLIVGSPP 242
Cdd:cd05591  183 GVLMYEMMAGQPP 195
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 83-242 2.26e-04

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: 42.91  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  83 LNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd06628   50 LDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEYVPGGSVATLLNNYGAF-EESLVRNFVRQILKGLNYLHNRGII 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGF-------AP--IEQ--YTddneseqgPWTDIYALGA 231
Cdd:cd06628  129 HRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNNGARPSLqgsvfwmAPevVKQtsYT--------RKADIWSLGC 200

                        170
                 ....*....|.
gi 505383238 232 VLRTLIVGSPP 242
Cdd:cd06628  201 LVVEMLTGTHP 211
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
 87-242 2.34e-04

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: 43.07  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPnLLHVLRFWVQN--------DTAYMGTLFYSgttLSRLReekpeLINEAWIRRMLPMLFGAIKTIHD 158
Cdd:cd05595   43 VTESRVLQNTRHP-FLTALKYAFQThdrlcfvmEYANGGELFFH---LSRER-----VFTEDRARFYGAEIVSALEYLHS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 EGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGF-APieQYTDDNesEQGPWTDIYALGAVLRTLI 237
Cdd:cd05595  114 RDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCGTPEYlAP--EVLEDN--DYGRAVDWWGLGVVMYEMM 189


                 ....*
gi 505383238 238 VGSPP 242
Cdd:cd05595  190 CGRLP 194
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
 86-242 2.37e-04

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: 42.85  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNllhVLRF--WVQNDT--------AYMGTLFysgttlSRLREEKPelINEAWIRRMLPMLFGAIKT 155
Cdd:cd14007   47 LRREIEIQSHLRHPN---ILRLygYFEDKKriylileyAPNGELY------KELKKQKR--FDEKEAAKYIYQLALALDY 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 156 IHDEGYLHRDISLDNIQIQDNGLPVLLDFG------SARR-----TIGNLSDEtetMLrpgfapieqytddNESEQGPWT 224
Cdd:cd14007  116 LHSKNIIHRDIKPENILLGSNGELKLADFGwsvhapSNRRktfcgTLDYLPPE---MV-------------EGKEYDYKV 179

                        170
                 ....*....|....*...
gi 505383238 225 DIYALGAVLRTLIVGSPP 242
Cdd:cd14007  180 DIWSLGVLCYELLVGKPP 197
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
 87-285 2.46e-04

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: 43.10  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRL---REEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd08229   72 IKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMikhFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMH 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPPP 243
Cdd:cd08229  152 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSLVGTPYYMSPERIHENGYNFK---SDIWSLGCLLYEMAALQSPF 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 505383238 244 VSVVRSIQDTCKPLVE-----LMPQGYSIPLLQAIDKALALHMEDRP 285
Cdd:cd08229  229 YGDKMNLYSLCKKIEQcdyppLPSDHYSEELRQLVNMCINPDPEKRP 275
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
 36-188 2.59e-04

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: 42.66  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKEfmpsslaVRgedmtlvLRSERFGKAFSAglnsfIQEARLLARFNHPNLLHVLRFWVQNDTAY 115
Cdd:cd07835   14 VVYKARDKLTGEIVALKK-------IR-------LETEDEGVPSTA-----IREISLLKELNHPNIVRLLDVVHSENKLY 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505383238 116 MgtLF-YSGTTLSRLREEKPEL-INEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd07835   75 L--VFeFLDLDLKKYMDSSPLTgLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLAR 147
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
 89-242 2.74e-04

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: 42.78  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL-SRLReeKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDIS 167
Cdd:cd14209   51 EKRILQAINFPFLVKLEYSFKDNSNLYMVMEYVPGGEMfSHLR--RIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLK 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 168 LDNIQIQDNGLPVLLDFGSARRTIGNLSD--ETETMLRPGFAPIEQYtddNESeqgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd14209  129 PENLLIDQQGYIKVTDFGFAKRVKGRTWTlcGTPEYLAPEIILSKGY---NKA-----VDWWALGVLIYEMAAGYPP 197
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
 85-188 2.90e-04

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: 42.49  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELIneAWIRRMlpMLFGAIKT----IHDEG 160
Cdd:cd14154   36 NFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKDVLKDMARPL--PWAQRV--RFAKDIASgmayLHSMN 111

                         90       100
                 ....*....|....*....|....*...
gi 505383238 161 YLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd14154  112 IIHRDLNSHNCLVREDKTVVVADFGLAR 139
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
 66-188 3.50e-04

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: 42.37  E-value: 3.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  66 MTLVLRSERFGKAFSAglnsfIQEARLLARFNHPNLLhVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRM 145
Cdd:cd07869   35 LKVIRLQEEEGTPFTA-----IREASLLKGLKHANIV-LLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPENVKLF 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 505383238 146 LPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd07869  109 LFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR 151
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
 20-242 3.71e-04

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: 42.34  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  20 FNEFEIKEVIGGGGFGIVYRA-WDHQlerTIAIKefmpsslAVR---GEDMTLVLRSERfgkafsaglnsfiQEARLLAR 95
Cdd:cd14145    5 FSELVLEEIIGIGGFGKVYRAiWIGD---EVAVK-------AARhdpDEDISQTIENVR-------------QEAKLFAM 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  96 FNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEK---PELINEAWIRRMLPMLFgaiktIHDEG---YLHRDISLD 169
Cdd:cd14145   62 LKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRVLSGKripPDILVNWAVQIARGMNY-----LHCEAivpVIHRDLKSS 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 170 NIQIQD--------NGLPVLLDFGSAR---RTIGNLSDETETMLRPGFAPIEQYTDDneseqgpwTDIYALGAVLRTLIV 238
Cdd:cd14145  137 NILILEkvengdlsNKILKITDFGLARewhRTTKMSAAGTYAWMAPEVIRSSMFSKG--------SDVWSYGVLLWELLT 208


                 ....
gi 505383238 239 GSPP 242
Cdd:cd14145  209 GEVP 212
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
 138-188 3.90e-04

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: 42.26  E-value: 3.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383238 138 NEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPvLLDFGSAR 188
Cdd:cd07831   98 PEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDILK-LADFGSCR 147
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
 87-187 4.87e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 42.29  E-value: 4.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVlrfwvqndtayMGTLFYSGTTLSRLREEKPELINEAWIRRMLPM---------LFGAIKTIH 157
Cdd:PHA03212 131 ATEAHILRAINHPSIIQL-----------KGTFTYNKFTCLILPRYKTDLYCYLAAKRNIAIcdilaiersVLRAIQYLH 199

                         90       100       110
                 ....*....|....*....|....*....|
gi 505383238 158 DEGYLHRDISLDNIQIQDNGLPVLLDFGSA 187
Cdd:PHA03212 200 ENRIIHRDIKAENIFINHPGDVCLGDFGAA 229
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
 84-188 5.04e-04

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: 41.79  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd05113   44 DEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMAnGCLLNYLREMRKRF-QTQQLLEMCKDVCEAMEYLESKQFL 122

                         90       100
                 ....*....|....*....|....*.
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05113  123 HRDLAARNCLVNDQGVVKVSDFGLSR 148
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 152-242 5.22e-04

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: 41.91  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 152 AIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTignLSDETETMLrpGFAPIEQY-----TDDNESEQGPWTDI 226
Cdd:cd05613  117 ALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEF---LLDENERAY--SFCGTIEYmapeiVRGGDSGHDKAVDW 191

                         90
                 ....*....|....*.
gi 505383238 227 YALGAVLRTLIVGSPP 242
Cdd:cd05613  192 WSLGVLMYELLTGASP 207
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
 80-188 6.15e-04

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: 41.57  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  80 SAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELINeawirRMLPMLFgAIKTIHD 158
Cdd:cd05039   41 STAAQAFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAkGSLVDYLRSRGRAVIT-----RKDQLGF-ALDVCEG 114

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505383238 159 EGYL------HRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05039  115 MEYLeskkfvHRDLAARNVLVSEDNVAKVSDFGLAK 150
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
 84-188 6.23e-04

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 41.89  E-value: 6.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRL---REEKPEL--------INEAWIRRMLPMLFGA 152
Cdd:cd05097   62 NDFLKEIKIMSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFlsqREIESTFthannipsVSIANLLYMAVQIASG 141

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505383238 153 IKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05097  142 MKYLASLNFVHRDLATRNCLVGNHYTIKIADFGMSR 177
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
 149-245 6.62e-04

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: 41.51  E-value: 6.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 149 LFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARR-------TIGNLSDETETMLRP------GF----APiEQ 211
Cdd:cd14010  103 LVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARRegeilkeLFGQFSDEGNVNKVSkkqakrGTpyymAP-EL 181

                         90       100       110
                 ....*....|....*....|....*....|....
gi 505383238 212 YTDDNESEQgpwTDIYALGAVLRTLIVGSPPPVS 245
Cdd:cd14010  182 FQGGVHSFA---SDLWALGCVLYEMFTGKPPFVA 212
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
 84-188 6.78e-04

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 41.52  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSR-LREEKPE----------LINEAWIRRMLPMLFGA 152
Cdd:cd05095   64 NDFLKEIKIMSRLKDPNIIRLLAVCITDDPLCMITEYMENGDLNQfLSRQQPEgqlalpsnalTVSYSDLRFMAAQIASG 143

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 505383238 153 IKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05095  144 MKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR 179
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
 37-188 6.86e-04

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: 41.60  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  37 VYRAWDHQLERTIAIKEfmpsslaVRgedmtlvLRSERfGKAFSAglnsfIQEARLLARFNHPN--LLHVLrfwVQNDTA 114
Cdd:cd07844   16 VYKGRSKLTGQLVALKE-------IR-------LEHEE-GAPFTA-----IREASLLKDLKHANivTLHDI---IHTKKT 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505383238 115 YMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd07844   73 LTLVFEYLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR 146
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
 88-242 6.91e-04

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: 41.32  E-value: 6.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFwVQNDTaYMGTL--FYSGTTLSRLREEKpELINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd14076   55 REINILKGLTHPNIVRLLDV-LKTKK-YIGIVleFVSGGELFDYILAR-RRLKDSVACRLFAQLISGVAYLHKKGVVHRD 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETML-RPGFAPIEQYTDDNESEqGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14076  132 LKLENLLLDKNRNLVITDFGFANTFDHFNGDLMSTSCgSPCYAAPELVVSDSMYA-GRKADIWSCGVILYAMLAGYLP 208
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
 23-242 7.83e-04

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: 41.38  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTiaikeFMPSSLAVRGEDMTLVLRserfgkafsaglnsfiqEARLLARFNHPNLL 102
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKT-----YMAKFVKVKGADQVLVKK-----------------EISILNIARHRNIL 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRFWVQNDTAYMGTLFYSGTTL-SRLREEKPELiNEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNI--QIQDNGLP 179
Cdd:cd14104   60 RLHESFESHEELVMIFEFISGVDIfERITTARFEL-NEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIiyCTRRGSYI 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505383238 180 VLLDFGSARRtignlsdetetmLRPG------FAPIEQYTDD--NESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14104  139 KIIEFGQSRQ------------LKPGdkfrlqYTSAEFYAPEvhQHESVSTATDMWSLGCLVYVLLSGINP 197
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
 123-242 7.90e-04

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: 41.19  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 123 GTTLSRLREEKpelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSArrtiGNLSD---ETE 199
Cdd:cd06640   87 GSALDLLRAGP---FDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVA----GQLTDtqiKRN 159

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 505383238 200 TMLRPGF--AP--IEQYTDDNESeqgpwtDIYALGAVLRTLIVGSPP 242
Cdd:cd06640  160 TFVGTPFwmAPevIQQSAYDSKA------DIWSLGITAIELAKGEPP 200
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
 89-242 7.92e-04

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: 41.27  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVlrFWVQNDTAYMGTLFY---SGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd05612   51 EKRVLKEVSHPFIIRL--FWTEHDQRFLYMLMEyvpGGELFSYLRNSGR--FSNSTGLFYASEIVCALEYLHSKEIVYRD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSARRtignLSDETETML-RPGF-AP-IEQYTDDNESeqgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd05612  127 LKPENILLDKEGHIKLTDFGFAKK----LRDRTWTLCgTPEYlAPeVIQSKGHNKA-----VDWWALGILIYEMLVGYPP 197
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
 44-296 7.93e-04

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 41.17  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  44 QLERTIAIKEFMPSSLAVRGEDMTLVLRSERFGkafSAGLNSFIQEARLLARFNHPNLLHvLRFWVQNDTAYMGTLFYS- 122
Cdd:cd05073   14 KLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPG---SMSVEAFLAEANVMKTLQHDKLVK-LHAVVTKEPIYIITEFMAk 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 123 GTTLSRLREEKPElineawiRRMLPML--FGA-----IKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARrtignLS 195
Cdd:cd05073   90 GSLLDFLKSDEGS-------KQPLPKLidFSAqiaegMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLAR-----VI 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 196 DETETMLRPGFAPIEQYTDDNESEQGPWT---DIYALGAVLRTLIVGSPPP------VSVVRSIQDTCKplvelMPQGYS 266
Cdd:cd05073  158 EDNEYTAREGAKFPIKWTAPEAINFGSFTiksDVWSFGILLMEIVTYGRIPypgmsnPEVIRALERGYR-----MPRPEN 232

                        250       260       270
                 ....*....|....*....|....*....|..
gi 505383238 267 IP--LLQAIDKALALHMEDRPqSIEEFAALIE 296
Cdd:cd05073  233 CPeeLYNIMMRCWKNRPEERP-TFEYIQSVLD 263
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
 152-185 8.44e-04

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: 41.37  E-value: 8.44e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 505383238 152 AIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFG 185
Cdd:cd05629  113 AIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFG 146
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
 89-256 8.97e-04

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: 41.12  E-value: 8.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPelINEAWIRRMLPMLFGAIKTIHDEGYLHRDISL 168
Cdd:cd06659   68 EVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTR--LNEEQIATVCEAVLQALAYLHSQGVIHRDIKS 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 169 DNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTddnESEQGPWTDIYALGAVLRTLIVGSPP-----P 243
Cdd:cd06659  146 DSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVIS---RCPYGTEVDIWSLGIMVIEMVDGEPPyfsdsP 222

                        170
                 ....*....|...
gi 505383238 244 VSVVRSIQDTCKP 256
Cdd:cd06659  223 VQAMKRLRDSPPP 235
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
 24-209 9.24e-04

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: 41.01  E-value: 9.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  24 EIKEVIGGGGFGIVYRAWDHQL---ERTIAIKEFMPSSLAVRGEDmtlvlrserfgkafsaglnsFIQEARLLARFNHPN 100
Cdd:cd05065    7 KIEEVIGAGEFGEVCRGRLKLPgkrEIFVAIKTLKSGYTEKQRRD--------------------FLSEASIMGQFDHPN 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 101 LLHVLRFWVQNDTAYMGTLFYSGTTL-SRLREEKPELIneawIRRMLPMLFG---AIKTIHDEGYLHRDISLDNIQIQDN 176
Cdd:cd05065   67 IIHLEGVVTKSRPVMIITEFMENGALdSFLRQNDGQFT----VIQLVGMLRGiaaGMKYLSEMNYVHRDLAARNILVNSN 142

                        170       180       190
                 ....*....|....*....|....*....|...
gi 505383238 177 GLPVLLDFGSARRTIGNLSDETETMLRPGFAPI 209
Cdd:cd05065  143 LVCKVSDFGLSRFLEDDTSDPTYTSSLGGKIPI 175
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
 160-242 1.03e-03

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: 41.10  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 160 GYLH------RDISLDNIQIQDNGLPVLLDFGSARRTIGNlSDETETmlrpgFAPIEQYTDDNESEQGPW---TDIYALG 230
Cdd:cd05604  111 GYLHsinivyRDLKPENILLDSQGHIVLTDFGLCKEGISN-SDTTTT-----FCGTPEYLAPEVIRKQPYdntVDWWCLG 184

                         90
                 ....*....|..
gi 505383238 231 AVLRTLIVGSPP 242
Cdd:cd05604  185 SVLYEMLYGLPP 196
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
 77-285 1.04e-03

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: 40.79  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  77 KAFSAGLNSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPElineawiRRMLPML--FGA- 152
Cdd:cd05072   40 KPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAkGSLLDFLKSDEGG-------KVLLPKLidFSAq 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 153 ----IKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARrtignLSDETETMLRPGFA-PIeQYTDDNESEQGPWT--- 224
Cdd:cd05072  113 iaegMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLAR-----VIEDNEYTAREGAKfPI-KWTAPEAINFGSFTiks 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 225 DIYALGAVLRTLIV-GSPPPVSVVRSiqdtckPLVELMPQGYSIPLLQAIDKALALHM--------EDRP 285
Cdd:cd05072  187 DVWSFGILLYEIVTyGKIPYPGMSNS------DVMSALQRGYRMPRMENCPDELYDIMktcwkekaEERP 250
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
 96-242 1.04e-03

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: 40.69  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  96 FNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKpELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQD 175
Cdd:cd14187   64 LAHQHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRR-KALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLND 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 176 NGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP 242
Cdd:cd14187  143 DMEVKIGDFGLATKVEYDGERKKTLCGTPNYIAPEVLSKKGHSFE---VDIWSIGCIMYTLLVGKPP 206
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
 23-189 1.11e-03

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: 40.95  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKEfmpsslavrgedmtlVLRSERFgkafsagLNsfiQEARLLARFNHPNLL 102
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKK---------------VLQDKRY-------KN---RELQIMRRLKHPNIV 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRFWV----QNDTAYMGTLF-YSGTTLSRLreekpeLINEAWIRRMLPM---------LFGAIKTIHDEGYLHRDISL 168
Cdd:cd14137   61 KLKYFFYssgeKKDEVYLNLVMeYMPETLYRV------IRHYSKNKQTIPIiyvklysyqLFRGLAYLHSLGICHRDIKP 134

                        170       180
                 ....*....|....*....|..
gi 505383238 169 DNIQI-QDNGLPVLLDFGSARR 189
Cdd:cd14137  135 QNLLVdPETGVLKLCDFGSAKR 156
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
 122-287 1.29e-03

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: 40.76  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 122 SGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFG-SAR--RTIG--NLSD 196
Cdd:cd06636  103 AGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGvSAQldRTVGrrNTFI 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 197 ETETMLRPGFAPIEQYTDDNESEQgpwTDIYALGAVLRTLIVGSPP-----PVSVVRSIQDTCKPlvELMPQGYSIPLLQ 271
Cdd:cd06636  183 GTPYWMAPEVIACDENPDATYDYR---SDIWSLGITAIEMAEGAPPlcdmhPMRALFLIPRNPPP--KLKSKKWSKKFID 257

                        170
                 ....*....|....*.
gi 505383238 272 AIDKALALHMEDRPQS 287
Cdd:cd06636  258 FIEGCLVKNYLSRPST 273
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
 103-242 1.32e-03

Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TTBK is a neuron-specific kinase that phosphorylates the microtubule-associated protein tau and promotes its aggregation. Higher vertebrates contain two TTBK proteins, TTBK1 and TTBK2, both of which have been implicated in neurodegeneration. Mutations in TTBK2 is associated with the development of spinocerebellar ataxia type 11, belonging to a group of neurodegenerative disorders characterized by progressive incoordination, dysarthria and impairment of eye movements. Brain tissues of SCA11 patients show the presence of neurofibrillary tangles and tau deposition in the brain, similar to Alzheimer's disease (AD) patients. The TTBK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271031 [Multi-domain]  Cd Length: 262  Bit Score: 40.42  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRF--WVQNDTAYMGTLFYSGTTLSRLREEKPE-LINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIqdNGLP 179
Cdd:cd14129   57 HVCRFigCGRNDRFNYVVMQLQGRNLADLRRSQSRgTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAM--GRFP 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383238 180 ------VLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDN---ESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14129  135 stcrkcYMLDFGLARQFTNSCGDVRPPRAVAGFRGTVRYASINahrNREMGRHDDLWSLFYMLVEFVVGQLP 206
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 359-412 1.32e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.24  E-value: 1.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 359 ETPAQ-TAQTPAVSPPAETS-AQAETRPATADVSEPVAPPA---SAQQSAPPVDASPVA 412
Cdd:PRK14951 379 KTPARpEAAAPAAAPVAQAAaAPAPAAAPAAAASAPAAPPAaapPAPVAAPAAAAPAAA 437
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
 88-242 1.34e-03

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: 40.44  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFwVQNDTAYMGTLFY--SGTTLSRLReeKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd06629   57 SEIDTLKDLDHPNIVQYLGF-EETEDYFSIFLEYvpGGSIGSCLR--KYGKFEEDLVRFFTRQILDGLAYLHSKGILHRD 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 166 ISLDNIQIQDNGLPVLLDFGSARRTiGNLSDETETMLRPG----FAPieQYTDDNESEQGPWTDIYALGAVLRTLIVGSP 241
Cdd:cd06629  134 LKADNILVDLEGICKISDFGISKKS-DDIYGNNGATSMQGsvfwMAP--EVIHSQGQGYSAKVDIWSLGCVVLEMLAGRR 210


                 .
gi 505383238 242 P 242
Cdd:cd06629  211 P 211
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 89-184 1.51e-03

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: 40.68  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVL-RFwvQNDT-AYMGTLFYSGTTLSRLREEKPE-LINEAWIRRMLPMLFGAIKTIHDEGYLHRD 165
Cdd:cd05574   51 EREILATLDHPFLPTLYaSF--QTSThLCFVMDYCPGGELFRLLQKQPGkRLPEEVARFYAAEVLLALEYLHLLGFVYRD 128

                         90
                 ....*....|....*....
gi 505383238 166 ISLDNIQIQDNGLPVLLDF 184
Cdd:cd05574  129 LKPENILLHESGHIMLTDF 147
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
 88-239 1.56e-03

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: 40.80  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQ-------NDTAYMGTLFysGTTLSRLreEKPELINEAWIRRMLPMLFGAIKTIHDEG 160
Cdd:cd07878   63 RELRLLKHMKHENVIGLLDVFTPatsienfNEVYLVTNLM--GADLNNI--VKCQKLSDEHVQFLIYQLLRGLKYIHSAG 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 161 YLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDNESeqgpwTDIYALGAVLRTLIVG 239
Cdd:cd07878  139 IIHRDLKPSNVAVNEDCELRILDFGLARQADDEMTGYVATRWYRAPEIMLNWMHYNQT-----VDIWSVGCIMAELLKG 212
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
 161-268 1.74e-03

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: 40.38  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 161 YLHRDISLDNIQIQDNGLPVLLDFGSARrtIGNLSDETETMLRPGFAPIEQYTDDN--ESEQGPWTDIYALGAVLRTLIV 238
Cdd:cd14205  129 YIHRDLATRNILVENENRVKIGDFGLTK--VLPQDKEYYKVKEPGESPIFWYAPESltESKFSVASDVWSFGVVLYELFT 206

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505383238 239 GS----PPPVSVVRSI------QDTCKPLVELMPQGYSIP 268
Cdd:cd14205  207 YIekskSPPAEFMRMIgndkqgQMIVFHLIELLKNNGRLP 246
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 357-413 1.76e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 1.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 505383238 357 SQETPAQTAQTPAVSPPAETSAQAEtrPATADVSEPVAPPAS-AQQSAPPVDASPVAL 413
Cdd:PRK14951 392 APVAQAAAAPAPAAAPAAAASAPAA--PPAAAPPAPVAAPAAaAPAAAPAAAPAAVAL 447
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
 89-190 1.77e-03

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: 40.35  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  89 EARLLARFNHPNLLHVLRFWVQNDTA------YMGTLFYsGTTLSR-LREEKpelINEAWIRRMLPMLFGAIKTIHDEGY 161
Cdd:cd07851   64 ELRLLKHMKHENVIGLLDVFTPASSLedfqdvYLVTHLM-GADLNNiVKCQK---LSDDHIQFLVYQILRGLKYIHSAGI 139

                         90       100
                 ....*....|....*....|....*....
gi 505383238 162 LHRDISLDNIQIQDNGLPVLLDFGSARRT 190
Cdd:cd07851  140 IHRDLKPSNLAVNEDCELKILDFGLARHT 168
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
 142-249 1.78e-03

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 40.50  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 142 IRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQD-NGLPVLLDFGSAR--RTIGNLSDEtETMLRPGFAPIEQYTDDNES 218
Cdd:cd14013  122 IKSIMRQILVALRKLHSTGIVHRDVKPQNIIVSEgDGQFKIIDLGAAAdlRIGINYIPK-EFLLDPRYAPPEQYIMSTQT 200

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 505383238 219 EQGP------------WT-------DIYALGAVLRTLIVGSPPPVSVVRS 249
Cdd:cd14013  201 PSAPpapvaaalspvlWQmnlpdrfDMYSAGVILLQMAFPNLRSDSNLIA 250
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
 87-188 1.79e-03

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: 40.10  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  87 IQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSgTTLSRLREEKP--ELINEAWIRRMLPMLFGAIKTIHDEGYLHR 164
Cdd:cd07861   47 IREISLLKELQHPNIVCLEDVLMQENRLYLVFEFLS-MDLKKYLDSLPkgKYMDAELVKSYLYQILQGILFCHSRRVLHR 125

                         90       100
                 ....*....|....*....|....
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd07861  126 DLKPQNLLIDNKGVIKLADFGLAR 149
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
 142-243 1.82e-03

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: 39.90  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 142 IRRMLPMLFGAIKTIHDEGYLHRDISLDNIQI-QDNGLPVLLDFGSARRTIGNLSDETETMLRPGFAPIE---QYTDdne 217
Cdd:cd14019  103 IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYnRETGKGVLVDFGLAQREEDRPEQRAPRAGTRGFRAPEvlfKCPH--- 179

                         90       100
                 ....*....|....*....|....*.
gi 505383238 218 seQGPWTDIYALGAVLRTLIVGSPPP 243
Cdd:cd14019  180 --QTTAIDIWSAGVILLSILSGRFPF 203
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
 152-185 1.86e-03

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: 40.38  E-value: 1.86e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 505383238 152 AIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFG 185
Cdd:cd05598  113 AIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFG 146
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
 82-242 1.94e-03

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: 39.98  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  82 GLNSFIQ-EARLLARFNHPNLLHVLRFWVQNDTAYM-------GTLFYSGTTLSRLREEKPElineawirRMLPMLFGAI 153
Cdd:cd14183   46 GKEHMIQnEVSILRRVKHPNIVLLIEEMDMPTELYLvmelvkgGDLFDAITSTNKYTERDAS--------GMLYNLASAI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 154 KTIHDEGYLHRDISLDNIQI---QDNGLPVLL-DFGSARRTIGNLSDETETmlrPGFAPIEQYTddnESEQGPWTDIYAL 229
Cdd:cd14183  118 KYLHSLNIVHRDIKPENLLVyehQDGSKSLKLgDFGLATVVDGPLYTVCGT---PTYVAPEIIA---ETGYGLKVDIWAA 191

                        170
                 ....*....|...
gi 505383238 230 GAVLRTLIVGSPP 242
Cdd:cd14183  192 GVITYILLCGFPP 204
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 66-242 2.02e-03

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: 40.37  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  66 MTLVLRSERFGKAFSAglnSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPelINEAWIRRM 145
Cdd:cd05621   82 MKLLSKFEMIKRSDSA---FFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYD--VPEKWAKFY 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 146 LPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETML-RPGF-APIEQYTDDNESEQGPW 223
Cdd:cd05621  157 TAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCMKMDETGMVHCDTAVgTPDYiSPEVLKSQGGDGYYGRE 236

                        170
                 ....*....|....*....
gi 505383238 224 TDIYALGAVLRTLIVGSPP 242
Cdd:cd05621  237 CDWWSVGVFLFEMLVGDTP 255
PRK10856 PRK10856
cytoskeleton protein RodZ;
357-414 2.09e-03

cytoskeleton protein RodZ;


Pssm-ID: 236776 [Multi-domain]  Cd Length: 331  Bit Score: 40.01  E-value: 2.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383238 357 SQETPAQTAQTPAVSPPAETSAQAETRPATADVSEP----VAPPASAQQSAPPVDASpvALV 414
Cdd:PRK10856 196 TAPAPAVDPQQNAVVAPSQANVDTAATPAPAAPATPdgaaPLPTDQAGVSTPAADPN--ALV 255
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
 86-188 2.21e-03

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: 39.82  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAY-MGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHD--EGYL 162
Cdd:cd14064   38 FCREVSILCRLNHPCVIQFVGACLDDPSQFaIVTQYVSGGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHNltQPII 117

                         90       100
                 ....*....|....*....|....*.
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd14064  118 HRDLNSHNILLYEDGHAVVADFGESR 143
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
 103-242 2.29e-03

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


Pssm-ID: 271032 [Multi-domain]  Cd Length: 262  Bit Score: 39.62  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRF--WVQNDTAYMGTLFYSGTTLSRLREEKPE-LINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIqdNGLP 179
Cdd:cd14130   57 HVCRFigCGRNEKFNYVVMQLQGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM--GRLP 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505383238 180 ------VLLDFGSARRTIGNLSDETETMLRPGFAPIEQYTDDN---ESEQGPWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14130  135 styrkcYMLDFGLARQYTNTTGEVRPPRNVAGFRGTVRYASVNahkNREMGRHDDLWSLFYMLVEFAVGQLP 206
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
 23-242 2.38e-03

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: 39.87  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKeFMPSSlAVRGEDMTLVlrserfgkafsaglnsfiQEARLLARFNHPNLL 102
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALK-CIPKK-ALRGKEAMVE------------------NEIAVLRRINHENIV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRFWVQNDTAYMG-TLFYSGTTLSRLREEKPELINEAwiRRMLPMLFGAIKTIHDEGYLHRDISLDNI----QIQDNG 177
Cdd:cd14169   65 SLEDIYESPTHLYLAmELVTGGELFDRIIERGSYTEKDA--SQLIGQVLQAVKYLHQLGIVHRDLKPENLlyatPFEDSK 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 178 LpVLLDFG-SARRTIGNLSDETETmlrPGFAPIEQYtddnesEQGPW---TDIYALGAVLRTLIVGSPP 242
Cdd:cd14169  143 I-MISDFGlSKIEAQGMLSTACGT---PGYVAPELL------EQKPYgkaVDVWAIGVISYILLCGYPP 201
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
 23-187 2.64e-03

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: 39.56  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAWDHQLERTIAIKefmpsslavrgedmtlVLRSErfgKAFsagLNSFIQEARLLARFN----- 97
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALK----------------IIKNN---KDY---LDQSLDEIRLLELLNkkdka 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  98 -HPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDN 176
Cdd:cd14133   59 dKYHIVRLKDVFYFKNHLCIVFELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASY 138

                        170
                 ....*....|...
gi 505383238 177 GLPV--LLDFGSA 187
Cdd:cd14133  139 SRCQikIIDFGSS 151
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
 152-242 3.11e-03

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: 39.52  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 152 AIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTignLSDETETMLrpGFAPIEQYTDD----NESEQGPWTDIY 227
Cdd:cd05614  117 ALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEF---LTEEKERTY--SFCGTIEYMAPeiirGKSGHGKAVDWW 191

                         90
                 ....*....|....*
gi 505383238 228 ALGAVLRTLIVGSPP 242
Cdd:cd05614  192 SLGILMFELLTGASP 206
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
 88-242 3.12e-03

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: 39.16  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  88 QEARLLARFNHPNLLHVLRFWVQNDTA--YMgTLFYSGTTLSrlreekpELINEAWIRRmLPM---------LFGAIKTI 156
Cdd:cd14119   43 REIQILRRLNHRNVIKLVDVLYNEEKQklYM-VMEYCVGGLQ-------EMLDSAPDKR-LPIwqahgyfvqLIDGLEYL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 157 HDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLR--PGFAPIEqYTDDNESEQGPWTDIYALGAVLR 234
Cdd:cd14119  114 HSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALDLFAEDDTCTTSQgsPAFQPPE-IANGQDSFSGFKVDIWSAGVTLY 192


                 ....*...
gi 505383238 235 TLIVGSPP 242
Cdd:cd14119  193 NMTTGKYP 200
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
 268-412 3.29e-03

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 39.83  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 268 PLLQAIDKALALHMEDRPQSIEEFAALIEMPVAGIDEVLTAKKTGTMLVPVEEETSASALDWRRYKLPGLVAAGVLVGVV 347
Cdd:COG3266  165 LALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGEAVAAAAELAALALLAAGAAEVLTARL 244

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505383238 348 AGAMLFGGDSQETPAQTA-------------QTPAVSPPAETSAQAETRPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:COG3266  245 VLLLLIIGSALKAPSQASsasapattslgeqQEVSLPPAVAAQPAAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQP 322
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
 137-189 3.34e-03

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: 39.67  E-value: 3.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505383238 137 INEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARR 189
Cdd:cd05596  122 VPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMK 174
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
 85-230 3.38e-03

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: 39.59  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  85 SFIQEARLLAR-FNHPNLL-HVLRFWVQND----TAYMGtlFYSGTTLsrLREEKPELINEAWIRRMLPMLFGAIKTIHD 158
Cdd:cd08216   44 KFLQQEILTSRqLQHPNILpYVTSFVVDNDlyvvTPLMA--YGSCRDL--LKTHFPEGLPELAIAFILRDVLNALEYIHS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 159 EGYLHRDISLDNIQIQDNGLPVLLDFGSARrtignlsdeteTMLRPGF--APIEQYTDDNESEQgPW------------- 223
Cdd:cd08216  120 KGYIHRSVKASHILISGDGKVVLSGLRYAY-----------SMVKHGKrqRVVHDFPKSSEKNL-PWlspevlqqnllgy 187

                        170
                 ....*....|
gi 505383238 224 ---TDIYALG 230
Cdd:cd08216  188 nekSDIYSVG 197
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
 86-188 3.43e-03

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: 39.32  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYM-GTLFYSGTTLSRLREEKPELINEAWI--RRMLPMLFGAIKTIH---DE 159
Cdd:cd05044   46 FLKEAHLMSNFKHPNILKLLGVCLDNDPQYIiLELMEGGDLLSYLRAARPTAFTPPLLtlKDLLSICVDVAKGCVyleDM 125

                         90       100       110
                 ....*....|....*....|....*....|...
gi 505383238 160 GYLHRDISLDNIQIQDNGLPVLL----DFGSAR 188
Cdd:cd05044  126 HFVHRDLAARNCLVSSKDYRERVvkigDFGLAR 158
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
 84-188 3.45e-03

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: 39.19  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYS-GTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYL 162
Cdd:cd05034   35 EAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSkGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYI 114

                         90       100
                 ....*....|....*....|....*.
gi 505383238 163 HRDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05034  115 HRDLAARNILVGENNVCKVADFGLAR 140
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
 86-188 3.56e-03

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: 39.16  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  86 FIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSR-LREEKPELINEAWIRRMLPMLFGaIKTIHDEGYLHR 164
Cdd:cd05112   46 FIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDyLRTQRGLFSAETLLGMCLDVCEG-MAYLEEASVIHR 124

                         90       100
                 ....*....|....*....|....
gi 505383238 165 DISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05112  125 DLAARNCLVGENQVVKVSDFGMTR 148
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
 23-232 3.63e-03

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: 39.10  E-value: 3.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  23 FEIKEVIGGGGFGIVYRAwDHQLERTIAIKEFMPsslavrgedmtlvLRSERFGKAFsaglnsfiQEARLLARFNHPNLL 102
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRV-THKGNGECCAAKFIP-------------LRSSTRARAF--------QERDILARLSHRRLT 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 103 HVLRFWVQNDTAYMGT-LFYSGTTLSRLReeKPELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIqiqdngLPV- 180
Cdd:cd14107   62 CLLDQFETRKTLILILeLCSSEELLDRLF--LKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNI------LMVs 133

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 181 -------LLDFGSARRtIGNLSDETETMLRPGFAPIEQYTDDNESEQgpwTDIYALGAV 232
Cdd:cd14107  134 ptredikICDFGFAQE-ITPSEHQFSKYGSPEFVAPEIVHQEPVSAA---TDIWALGVI 188
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
 157-289 3.69e-03

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: 39.17  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 157 HDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDETETMLRPGF-AP--IEQYTDDNEseqgpwTDIYALGAVL 233
Cdd:cd06612  116 HSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTVIGTPFWmAPevIQEIGYNNK------ADIWSLGITA 189

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 234 RTLIVGSPP-----PVSVVRSIQDtcKPlvelmPQGYSIP------LLQAIDKALALHMEDRPQSIE 289
Cdd:cd06612  190 IEMAEGKPPysdihPMRAIFMIPN--KP-----PPTLSDPekwspeFNDFVKKCLVKDPEERPSAIQ 249
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
 134-290 3.84e-03

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: 39.18  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 134 PELINEAWIRRMLPmlfgAIKTIHDEGYLHRDISLDNIQIQDN-GLPVLLDFGSA---RRTIGNLSDETETMLRPGFAPI 209
Cdd:cd14100  104 PEELARSFFRQVLE----AVRHCHNCGVLHRDIKDENILIDLNtGELKLIDFGSGallKDTVYTDFDGTRVYSPPEWIRF 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 210 EQYtddneseQGPWTDIYALGAVLRTLIVGSPPpvsvVRSIQDTCKPLVeLMPQGYSIPLLQAIDKALALHMEDRPqSIE 289
Cdd:cd14100  180 HRY-------HGRSAAVWSLGILLYDMVCGDIP----FEHDEEIIRGQV-FFRQRVSSECQHLIKWCLALRPSDRP-SFE 246


                 .
gi 505383238 290 E 290
Cdd:cd14100  247 D 247
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
 153-189 3.92e-03

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: 38.98  E-value: 3.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 505383238 153 IKTIHDEGYLHRDISLDNIQIqdnGLPV------LLDFGSARR 189
Cdd:cd14016  109 LEYLHSKGYIHRDIKPENFLM---GLGKnsnkvyLIDFGLAKK 148
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
 22-293 3.94e-03

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: 39.03  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  22 EFEIKEVIGGGGFGIVYRAWDHQLERTIAIKEFMpsslavrGEDMtlvlrserfgkafsAGLNSFIQEARLLARFN-HPN 100
Cdd:cd14036    1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLL-------SNEE--------------EKNKAIIQEINFMKKLSgHPN 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 101 LLHVLrfwvqnDTAYMG--------------TLFYSGTTLSRLRE-EKPELINEAWIRRMLPMLFGAIKTIHDEG--YLH 163
Cdd:cd14036   60 IVQFC------SAASIGkeesdqgqaeylllTELCKGQLVDFVKKvEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIH 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSARRTI------------GNLSDETETMLRPGF-AP--IEQYTDDNESEQgpwTDIYA 228
Cdd:cd14036  134 RDLKIENLLIGNQGQIKLCDFGSATTEAhypdyswsaqkrSLVEDEITRNTTPMYrTPemIDLYSNYPIGEK---QDIWA 210

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 229 LGAVLRTLIVGSPPpvsvvrsIQDTCKplVELMPQGYSIP--------LLQAIDKALALHMEDRP------QSIEEFAA 293
Cdd:cd14036  211 LGCILYLLCFRKHP-------FEDGAK--LRIINAKYTIPpndtqytvFHDLIRSTLKVNPEERLsiteivEQLQELAA 280
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
 135-185 3.97e-03

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: 39.61  E-value: 3.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505383238 135 ELINEAWIRRMLPMLFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFG 185
Cdd:cd05626   96 EVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFG 146
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
 149-187 3.98e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 39.44  E-value: 3.98e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 505383238 149 LFGAIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSA 187
Cdd:PHA03207 194 LLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAA 232
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
 162-187 4.22e-03

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: 39.19  E-value: 4.22e-03
                         10        20
                 ....*....|....*....|....*.
gi 505383238 162 LHRDISLDNIQIQDNGLPVLLDFGSA 187
Cdd:cd14037  132 IHRDLKVENVLISDSGNYKLCDFGSA 157
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
 20-242 4.37e-03

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: 38.86  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  20 FNEFEIKEVIGGGGFGIVYR-AWDHQLertIAIKefmpsslAVR---GEDMTLVLRSERfgkafsaglnsfiQEARLLAR 95
Cdd:cd14147    2 FQELRLEEVIGIGGFGKVYRgSWRGEL---VAVK-------AARqdpDEDISVTAESVR-------------QEARLFAM 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  96 FNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRL---REEKPELINEAWIRRMLPMLFgaiktIHDEGY---LHRDISLD 169
Cdd:cd14147   59 LAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRAlagRRVPPHVLVNWAVQIARGMHY-----LHCEALvpvIHRDLKSN 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 170 NIQIQDNGLP--------VLLDFGSAR---RTIGNLSDETETMLRPGFApieqytddNESEQGPWTDIYALGAVLRTLIV 238
Cdd:cd14147  134 NILLLQPIENddmehktlKITDFGLARewhKTTQMSAAGTYAWMAPEVI--------KASTFSKGSDVWSFGVLLWELLT 205


                 ....
gi 505383238 239 GSPP 242
Cdd:cd14147  206 GEVP 209
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
 84-188 4.49e-03

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: 38.91  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTL------SRLREEKPELINeawirrMLPMLFGAI---- 153
Cdd:cd05036   54 MDFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILLELMAGGDLksflreNRPRPEQPSSLT------MLDLLQLAQdvak 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505383238 154 --KTIHDEGYLHRDISLDNIQIQDNG---LPVLLDFGSAR 188
Cdd:cd05036  128 gcRYLEENHFIHRDIAARNCLLTCKGpgrVAKIGDFGMAR 167
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
 156-242 6.10e-03

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: 38.47  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 156 IHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIGNLSDE-----TETMLRPGFAPIEQYTDDNEseqgpWTDIYALG 230
Cdd:cd06646  122 LHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIAKRksfigTPYWMAPEVAAVEKNGGYNQ-----LCDIWAVG 196

                         90
                 ....*....|..
gi 505383238 231 AVLRTLIVGSPP 242
Cdd:cd06646  197 ITAIELAELQPP 208
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
 84-188 6.11e-03

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: 38.42  E-value: 6.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  84 NSFIQEARLLARFNHPNLLHVLRFWVQNDTAYMGTLFYSGTTLSRLREEKPELINEAWIRRMLPMLFGAIKTIHDEGYLH 163
Cdd:cd05063   51 QDFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVH 130

                         90       100
                 ....*....|....*....|....*
gi 505383238 164 RDISLDNIQIQDNGLPVLLDFGSAR 188
Cdd:cd05063  131 RDLAARNILVNSNLECKVSDFGLSR 155
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
 148-204 7.10e-03

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: 38.55  E-value: 7.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505383238 148 MLFGaIKTIHDEGYLHRDISLDNIQIQDNGLPVLLDFGSARRTIgnlsdeTETMLRP 204
Cdd:cd07850  111 MLCG-IKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAG------TSFMMTP 160
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
 354-412 8.11e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 38.54  E-value: 8.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 354 GGDSQETPAQTAQTPAVSPPAETSAQAETRPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:PRK14951 367 AAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAP 425
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
 36-299 8.16e-03

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: 38.36  E-value: 8.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  36 IVYRAWDHQLERTIAIKefmpsslAVRGEdmTLVLRSERfgkafsaglNSFIQEARLL--ARFNHpnLLHVlrFWVQNDT 113
Cdd:cd14026   12 TVSRARHADWRVTVAIK-------CLKLD--SPVGDSER---------NCLLKEAEILhkARFSY--ILPI--LGICNEP 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 114 AYMG--TLFYSGTTLSRLREEKPELINEAW-IR-RMLPMLFGAIKTIHDEG--YLHRDISLDNIQIQDNGLPVLLDFG-S 186
Cdd:cd14026   70 EFLGivTEYMTNGSLNELLHEKDIYPDVAWpLRlRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGlS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 187 ARRTIGNLSDETETMLRPG----FAPIEQYTDDNESEQGPWTDIYALGAVLRTLIVGSPP------PVSVVRSIQDTCKP 256
Cdd:cd14026  150 KWRQLSISQSRSSKSAPEGgtiiYMPPEEYEPSQKRRASVKHDIYSYAIIMWEVLSRKIPfeevtnPLQIMYSVSQGHRP 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 505383238 257 LVELMPQGYSIP----LLQAIDKALALHMEDRPQSIEefaALIEM-PV 299
Cdd:cd14026  230 DTGEDSLPVDIPhratLINLIESGWAQNPDERPSFLK---CLIELePV 274
PHA03247 PHA03247
large tegument protein UL36; Provisional
 357-412 8.30e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 39.15  E-value: 8.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505383238  357 SQETPAQTAQTPAVSPPAETSAQAETRPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:PHA03247 2792 SESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP 2847
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
 77-242 9.03e-03

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: 38.09  E-value: 9.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238  77 KAFSAGLNSFIQ-EARLLARFNHPNLLHVLRfwvQNDTA---YM-------GTLFYSGTTLSRLREEKPELineawirrM 145
Cdd:cd14184   36 KAKCCGKEHLIEnEVSILRRVKHPNIIMLIE---EMDTPaelYLvmelvkgGDLFDAITSSTKYTERDASA--------M 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505383238 146 LPMLFGAIKTIHDEGYLHRDISLDNIQIQD--NGLPVLL--DFGSARRTIGNLSDETETmlrPGFAPIEQYTddnESEQG 221
Cdd:cd14184  105 VYNLASALKYLHGLCIVHRDIKPENLLVCEypDGTKSLKlgDFGLATVVEGPLYTVCGT---PTYVAPEIIA---ETGYG 178

                        170       180
                 ....*....|....*....|.
gi 505383238 222 PWTDIYALGAVLRTLIVGSPP 242
Cdd:cd14184  179 LKVDIWAAGVITYILLCGFPP 199
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 354-412 9.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.43  E-value: 9.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505383238 354 GGDSQETPAQTAQTPA----VSPPAETSAQAETRPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:PRK07764 389 GGAGAPAAAAPSAAAAapaaAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAG 451
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
 354-412 9.64e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 38.43  E-value: 9.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505383238 354 GGDSQETPAQTAQTPAVSPPAETSAQAEtrPATADVSEPVAPPASAQQSAPPVDASPVA 412
Cdd:PRK07764 454 PSPPPAAAPSAQPAPAPAAAPEPTAAPA--PAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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