NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1034651883|ref|XP_016866853|]
View 

tau-tubulin kinase 1 isoform X1 [Homo sapiens]

Protein Classification

STKc_TTBK1 and PHA03307 domain-containing protein( domain architecture ID 12995731)

STKc_TTBK1 and PHA03307 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
33-294 0e+00

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: 547.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14130      1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRP 192
Cdd:cd14130     81 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGEVRP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  193 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFL 272
Cdd:cd14130    161 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFL 240
                          250       260
                   ....*....|....*....|..
gi 1034651883  273 DHIASLDYFTKPDYQLIMSVFE 294
Cdd:cd14130    241 DHIASLDYFTKPDYQLIMSVFE 262
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
1083-1376 5.98e-07

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1083 SALSGAPRETPSEMATNSLPNGPALADGPAPVSPLEPSPEKVATISPRRHAMPGSRPRSRIpvllsEEDTGSEPSGSLSA 1162
Cdd:PHA03307   152 PPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSP-----ISASASSPAPAPGR 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1163 KERWSKRARPQQDLARLVMEKRQGrlllrlaSGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATRSR 1242
Cdd:PHA03307   227 SAADDAGASSSDSSSSESSGCGWG-------PENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPS 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1243 IPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSSRLQLQTPPGSATAADLRPKQPPGRGLGPGRAQAGARPPAPRSPR 1322
Cdd:PHA03307   300 PSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPA 379
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883 1323 LPASTSAARNASASPRSQSLsRRESPSPSHQARPGVPPPRGVPPARA----QPDGTPS 1376
Cdd:PHA03307   380 ASAGRPTRRRARAAVAGRAR-RRDATGRFPAGRPRPSPLDAGAASGAfyarYPLLTPS 436
 
Name Accession Description Interval E-value
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
33-294 0e+00

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: 547.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14130      1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRP 192
Cdd:cd14130     81 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGEVRP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  193 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFL 272
Cdd:cd14130    161 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFL 240
                          250       260
                   ....*....|....*....|..
gi 1034651883  273 DHIASLDYFTKPDYQLIMSVFE 294
Cdd:cd14130    241 DHIASLDYFTKPDYQLIMSVFE 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-275 1.66e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 127.65  E-value: 1.66e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883    34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL 109
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVikkkKIKKDRERILR-EIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   110 -QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLpstyrkcYMLDFGLARQYTn 185
Cdd:smart00220   79 cEGGDLFDLLKK--RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIlldEDGHV-------KLADFGLARQLD- 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   186 ttgdvrPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV--GMIKEKYEHRMLLKH 263
Cdd:smart00220  149 ------PGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELfkKIGKPKPPFPPPEWD 222
                           250
                    ....*....|..
gi 1034651883   264 MPSEFHLFLDHI 275
Cdd:smart00220  223 ISPEAKDLIRKL 234
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
27-240 6.01e-26

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 113.57  E-value: 6.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   27 NYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQV--LKMEVAVLKKLQGkDHVCRFIGCGRNEK 101
Cdd:COG0515      2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVlrpELAADPEARerFRREARALARLNH-PNIVRVYDVGEEDG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FNYVVMQL-QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGLA 180
Cdd:COG0515     81 RPYLVMEYvEGESLADLLRR--RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTP----DGRVKLIDFGIA 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQYTNTTgdVRPPRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:COG0515    155 RALGGAT--LTQTGTVV---GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFD 209
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
33-294 8.42e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 100.41  E-value: 8.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYE---AMDLLTRENVALKVESAQQPKQVL----------KMEVAVLKKLQGKDH--VCRFIGCG 97
Cdd:PHA02882    13 EWKIDKLIGCGGFGCVYEtqcASDHCINNQAVAKIENLENETIVMetlvynniydIDKIALWKNIHNIDHlgIPKYYGCG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   98 rneKFNYVVMQLQGRNLADLRRSQPRgtfTLSTTLRLGKQILESI--------EAIHSVGFLHRDIKPSNFAMgrlpSTY 169
Cdd:PHA02882    93 ---SFKRCRMYYRFILLEKLVENTKE---IFKRIKCKNKKLIKNImkdmlttlEYIHEHGISHGDIKPENIMV----DGN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  170 RKCYMLDFGLARQYTNTTGDVRPPRNVAGF-RGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV 248
Cdd:PHA02882   163 NRGYIIDYGIASHFIIHGKHIEYSKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNGNL 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  249 ------GMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFE 294
Cdd:PHA02882   243 ihaakcDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALIKIFD 294
Pkinase pfam00069
Protein kinase domain;
34-273 4.46e-16

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 78.82  E-value: 4.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQVLkMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQ 108
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKikkekIKKKKDKNIL-REIKILKKLNHP-NIVRLYDAFEDKDNLYLVLE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADLRRsqPRGTFTLSTTLRLGKQILEsieaihsvgflhrdikpsnfamgrlpstyrkcymldfGLARQYTNTT 187
Cdd:pfam00069   79 YvEGGSLFDLLS--EKGAFSEREAKFIMKQILE-------------------------------------GLESGSSLTT 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 gdvrpprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV-GMIKEKYEHRMLLKHMPS 266
Cdd:pfam00069  120 -----------FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYeLIIDQPYAFPELPSNLSE 188

                   ....*..
gi 1034651883  267 EFHLFLD 273
Cdd:pfam00069  189 EAKDLLK 195
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
32-187 4.47e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.13  E-value: 4.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKME--------------VAVLKklQGKDHVCrfi 94
Cdd:NF033483     7 GRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVlrpDLARDPEFVARFRreaqsaaslshpniVSVYD--VGEDGGI--- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   95 gcgrnekfNYVVMQL-QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyr 170
Cdd:NF033483    82 --------PYIVMEYvDGRTLKDYIRE--HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILItkdGRVKVT-- 149
                          170
                   ....*....|....*..
gi 1034651883  171 kcymlDFGLARQYTNTT 187
Cdd:NF033483   150 -----DFGIARALSSTT 161
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1083-1376 5.98e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1083 SALSGAPRETPSEMATNSLPNGPALADGPAPVSPLEPSPEKVATISPRRHAMPGSRPRSRIpvllsEEDTGSEPSGSLSA 1162
Cdd:PHA03307   152 PPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSP-----ISASASSPAPAPGR 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1163 KERWSKRARPQQDLARLVMEKRQGrlllrlaSGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATRSR 1242
Cdd:PHA03307   227 SAADDAGASSSDSSSSESSGCGWG-------PENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPS 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1243 IPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSSRLQLQTPPGSATAADLRPKQPPGRGLGPGRAQAGARPPAPRSPR 1322
Cdd:PHA03307   300 PSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPA 379
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883 1323 LPASTSAARNASASPRSQSLsRRESPSPSHQARPGVPPPRGVPPARA----QPDGTPS 1376
Cdd:PHA03307   380 ASAGRPTRRRARAAVAGRAR-RRDATGRFPAGRPRPSPLDAGAASGAfyarYPLLTPS 436
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
32-205 6.54e-05

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


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 47.64  E-value: 6.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGfgeiyEAMDLLTRENVA------LKVESAQQPKQVLKMEVAVLKKLQGkDHVCRFIGcGRNEKFNYV 105
Cdd:NF033442   510 GGFEVRRRLGTGS-----TSRALLVRDRDAdgeervLKVALDDEHAARLRAEAEVLGRLRH-PRIVALVE-GPLEIGGRT 582
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQ---GRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQ 182
Cdd:NF033442   583 ALLLEyagEQTLAERLRKE--GRLSLDLLERFGDDLLSAVVHLEGQGVWHRDIKPDNIGIRPRPSRTLHLVLFDFSLAGA 660
                          170       180
                   ....*....|....*....|...
gi 1034651883  183 ytnttgdvrPPRNVAGfrGTVRY 205
Cdd:NF033442   661 ---------PADNIEA--GTPGY 672
 
Name Accession Description Interval E-value
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
33-294 0e+00

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: 547.32  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14130      1 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRP 192
Cdd:cd14130     81 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGEVRP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  193 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFL 272
Cdd:cd14130    161 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFL 240
                          250       260
                   ....*....|....*....|..
gi 1034651883  273 DHIASLDYFTKPDYQLIMSVFE 294
Cdd:cd14130    241 DHIASLDYFTKPDYQLIMSVFE 262
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
33-294 5.19e-170

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: 507.67  E-value: 5.19e-170
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14129      1 RWKVLRKIGGGGFGEIYDALDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNDRFNYVVMQLQGR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRP 192
Cdd:cd14129     81 NLADLRRSQSRGTFTISTTLRLGRQILESIESIHSVGFLHRDIKPSNFAMGRFPSTCRKCYMLDFGLARQFTNSCGDVRP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  193 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFL 272
Cdd:cd14129    161 PRAVAGFRGTVRYASINAHRNREMGRHDDLWSLFYMLVEFVVGQLPWRKIKDKEQVGSIKERYEHRLMLKHLPPEFSVFL 240
                          250       260
                   ....*....|....*....|..
gi 1034651883  273 DHIASLDYFTKPDYQLIMSVFE 294
Cdd:cd14129    241 DHISGLDYFTKPDYQLLVSVFD 262
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
33-294 2.13e-168

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: 503.71  E-value: 2.13e-168
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14017      1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEVAVLKKLQGKPHFCRLIGCGRTERYNYIVMTLLGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDV-R 191
Cdd:cd14017     81 NLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERTVYILDFGLARQYTNKDGEVeR 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  192 PPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLF 271
Cdd:cd14017    161 PPRNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKLKDKEEVGKMKEKIDHEELLKGLPKEFFQI 240
                          250       260
                   ....*....|....*....|...
gi 1034651883  272 LDHIASLDYFTKPDYQLIMSVFE 294
Cdd:cd14017    241 LKHIRSLSYFDTPDYKKLHSLLE 263
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
33-293 8.00e-85

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: 278.19  E-value: 8.00e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14016      1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLEYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLLGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRKCYMLDFGLARQYTN-TTGDVR 191
Cdd:cd14016     81 SLEDLFNKCGR-KFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGL-GKNSNKVYLIDFGLAKKYRDpRTGKHI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  192 PPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDK------EQVGMIKEKYEHRMLLKHMP 265
Cdd:cd14016    159 PYREGKSLTGTARYASINAHLGIEQSRRDDLESLGYVLIYFLKGSLPWQGLKAQskkekyEKIGEKKMNTSPEELCKGLP 238
                          250       260
                   ....*....|....*....|....*...
gi 1034651883  266 SEFHLFLDHIASLDYFTKPDYQLIMSVF 293
Cdd:cd14016    239 KEFAKYLEYVRSLKFEEEPDYDYLRQLF 266
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
33-295 1.17e-52

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; 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. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 186.42  E-value: 1.17e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14125      1 KYRLGRKIGSGSFGDIYLGTNIQTGEEVAIKLESVKTKHPQLLYESKLYKILQGGVGIPNVRWYGVEGDYNVMVMDLLGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADL-----RRsqprgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrLPSTYRKCYMLDFGLARQYTNTT 187
Cdd:cd14125     81 SLEDLfnfcsRK------FSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMG-LGKKGNLVYIIDFGLAKKYRDPR 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 GDVRPP-RNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKdkeqVGMIKEKYEHRM------- 259
Cdd:cd14125    154 THQHIPyRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNRGSLPWQGLK----AATKKQKYEKISekkmstp 229
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1034651883  260 ---LLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd14125    230 ievLCKGFPSEFATYLNYCRSLRFDDKPDYSYLRRLFRD 268
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
33-293 1.58e-49

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; 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. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 176.93  E-value: 1.58e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14128      1 KYRLVRKIGSGSFGDIYLGINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrLPSTYRKCYMLDFGLARQYT-NTTGDVR 191
Cdd:cd14128     81 SLEDLFNFCSR-RFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMG-IGRHCNKLFLIDFGLAKKYRdSRTRQHI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  192 PPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQvgmiKEKYEH----------RMLL 261
Cdd:cd14128    159 PYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRGSLPWQGLKAATK----KQKYEKisekkmstpvEVLC 234
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034651883  262 KHMPSEFHLFLDHIASLDYFTKPDYQLIMSVF 293
Cdd:cd14128    235 KGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLF 266
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
34-310 1.07e-47

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; 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. CK1gamma proteins are unique within the CK1 subfamily in that they are palmitoylated at the C-termini and are anchored to the plasma membrane. CK1gamma is involved in transducing the signaling of LDL-receptor-related protein 6 (LRP6) through direct phosphorylation following Wnt stimulation, resulting in the recruitment of the scaffold protein Axin. In Xenopus embryos, CK1gamma is required during anterio-posterior patterning. In higher vertebrates, three CK1gamma (gamma1-3) isoforms exist. In mammalian cells, CK1gamma2 has been implicated in regulating the synthesis of sphingomyelin, a phospholipid that is found in the outer leaflet of the plasma membrane, by hyperphosphorylating and inactivating the ceramide transfer protein CERT. CK1gamma2 also phosphorylates the transcription factor Smad-3 resulting in its ubiquitination and degradation. It inhibits Smad-3 mediated responses of Transforming Growth Factor-beta (TGF-beta) including cell growth arrest. The CK1 gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 172.61  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKL---QGKDHVCRFIGCGrneKFNYVVMQLQ 110
Cdd:cd14126      2 FRVGKKIGCGNFGELRLGKNLYNNEHVAIKLEPMKSRAPQLHLEYRFYKLLgqaEGLPQVYYFGPCG---KYNAMVLELL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRK--CYMLDFGLARQYTNT-T 187
Cdd:cd14126     79 GPSLEDLFDLCDR-TFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGR-QSTKKQhvIHIIDFGLAKEYIDPeT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 GDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKdkeqVGMIKEKYEH---------- 257
Cdd:cd14126    157 NKHIPYREHKSLTGTARYMSINTHLGKEQSRRDDLEALGHMFMYFLRGSLPWQGLK----ADTLKERYQKigdtkratpi 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  258 RMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDW 310
Cdd:cd14126    233 EVLCENFPEEMATYLRYVRRLDFFETPDYDYLRKLFTDLFDRKGYTDDYEFDW 285
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
33-301 1.43e-43

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 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. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal 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: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 160.35  E-value: 1.43e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14127      1 HYKVGKKIGEGSFGVIFEGTNLLNGQQVAIKFEPRKSDAPQLRDEYRTYKLLAGCPGIPNVYYFGQEGLHNILVIDLLGP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRK--CYMLDFGLARQYTNT-TGD 189
Cdd:cd14127     81 SLEDLFDLCGR-KFSVKTVVMVAKQMLTRVQTIHEKNLIYRDIKPDNFLIGR-PGTKNAnvIHVVDFGMAKQYRDPkTKQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  190 VRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDK------EQVGMIKEKYEHRMLLKH 263
Cdd:cd14127    159 HIPYREKKSLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAAtnkqkyEKIGEKKQSTPIRDLCEG 238
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1034651883  264 MPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERG 301
Cdd:cd14127    239 FPEEFAQYLEYVRNLGFDETPDYDYLRGLFSKALKDLG 276
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
40-232 1.23e-40

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: 149.73  E-value: 1.23e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL-QGRNLA 115
Cdd:cd00180      1 LGKGSFGKVYKARDKETGKKVAVKVipkEKLKKLLEELLREIEILKKLNHP-NIVKLYDVFETENFLYLVMEYcEGGSLK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  116 DLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTGDVRPprn 195
Cdd:cd00180     80 DLLKEN-KGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENI----LLDSDGTVKLADFGLAKDLDSDDSLLKT--- 151
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1034651883  196 vAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEF 232
Cdd:cd00180    152 -TGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
29-293 4.36e-38

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins (VRK1, VRK2, and VRK3) while invertebrates, specifically fruit flies and nematodes, seem to carry only a single ortholog. Mutations of VRK in Drosophila and Caenorhabditis elegans showed varying phenotypes ranging from embryonic lethality to mitotic and meiotic defects resulting in sterility. In vertebrates, VRK1 is implicated in cell cycle progression and proliferation, nuclear envelope assembly, and chromatin condensation. VRK2 is involved in modulating JNK signaling. VRK3 is an inactive pseudokinase that inhibits ERK signaling. The VRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 145.12  E-value: 4.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAMDlltreNVALKVESAQqpKQVLKME----------------------VAVLKKLQG 86
Cdd:cd14015      7 VTKRQWKLGKSIGQGGFGEIYLASD-----DSTLSVGKDA--KYVVKIEphsngplfvemnfyqrvakpemIKKWMKAKK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   87 KDH--VCRFIGCG----RNEKFNYVVMQLQGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF 160
Cdd:cd14015     80 LKHlgIPRYIGSGsheyKGEKYRFLVMPRFGRDLQKIFEKNGK-RFPEKTVLQLALRILDVLEYIHENGYVHADIKASNL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  161 AMGrLPSTYRKCYMLDFGLARQYTNTTG------DVRPPRNvagfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAV 234
Cdd:cd14015    159 LLG-FGKNKDQVYLVDYGLASRYCPNGKhkeykeDPRKAHN-----GTIEFTSRDAHKGVAPSRRGDLEILGYNMLQWLC 232
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  235 GQLPWR-KIKDKEQVGMIKEKYehrM-----LLKHM------PSEFHLFLDHIASLDYFTKPDYQLIMSVF 293
Cdd:cd14015    233 GKLPWEdNLKNPEYVQKQKEKY---MddiplLLKKCfpgkdvPEELQKYLKYVASLEYEEKPDYEKLRKIL 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
34-275 1.66e-32

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 127.65  E-value: 1.66e-32
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883    34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL 109
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVikkkKIKKDRERILR-EIKILKKLK-HPNIVRLYDVFEDEDKLYLVMEY 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   110 -QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLpstyrkcYMLDFGLARQYTn 185
Cdd:smart00220   79 cEGGDLFDLLKK--RGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIlldEDGHV-------KLADFGLARQLD- 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   186 ttgdvrPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV--GMIKEKYEHRMLLKH 263
Cdd:smart00220  149 ------PGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELfkKIGKPKPPFPPPEWD 222
                           250
                    ....*....|..
gi 1034651883   264 MPSEFHLFLDHI 275
Cdd:smart00220  223 ISPEAKDLIRKL 234
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
33-240 2.94e-29

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: 118.07  E-value: 2.94e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQVLKMEVAVLKKLQGkDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd14014      1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVlrpelAEDEEFRERFLREARALARLSH-PNIVRVYDVGEDDGRPYIVM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QL-QGRNLAD-LRRsqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQ--- 182
Cdd:cd14014     80 EYvEGGSLADlLRE---RGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANI----LLTEDGRVKLTDFGIARAlgd 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  183 -YTNTTGDVrpprnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:cd14014    153 sGLTQTGSV---------LGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFD 202
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
33-274 3.01e-27

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: 112.23  E-value: 3.01e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPK---QVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVM- 107
Cdd:cd06606      1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKeVELSGDSEeelEALEREIRILSSLKHP-NIVRYLGTERTENTLNIFLe 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQytntT 187
Cdd:cd06606     80 YVPGGSLASLLKK--FGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANI----LVDSDGVVKLADFGCAKR----L 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 GDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV-GMIKEKYEHRMLLKHMPS 266
Cdd:cd06606    150 AEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAAlFKIGSSGEPPPIPEHLSE 229

                   ....*...
gi 1034651883  267 EFHLFLDH 274
Cdd:cd06606    230 EAKDFLRK 237
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
27-240 6.01e-26

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 113.57  E-value: 6.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   27 NYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQV--LKMEVAVLKKLQGkDHVCRFIGCGRNEK 101
Cdd:COG0515      2 SALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVlrpELAADPEARerFRREARALARLNH-PNIVRVYDVGEEDG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FNYVVMQL-QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGLA 180
Cdd:COG0515     81 RPYLVMEYvEGESLADLLRR--RGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTP----DGRVKLIDFGIA 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQYTNTTgdVRPPRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:COG0515    155 RALGGAT--LTQTGTVV---GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFD 209
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
33-294 8.42e-23

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 100.41  E-value: 8.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYE---AMDLLTRENVALKVESAQQPKQVL----------KMEVAVLKKLQGKDH--VCRFIGCG 97
Cdd:PHA02882    13 EWKIDKLIGCGGFGCVYEtqcASDHCINNQAVAKIENLENETIVMetlvynniydIDKIALWKNIHNIDHlgIPKYYGCG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   98 rneKFNYVVMQLQGRNLADLRRSQPRgtfTLSTTLRLGKQILESI--------EAIHSVGFLHRDIKPSNFAMgrlpSTY 169
Cdd:PHA02882    93 ---SFKRCRMYYRFILLEKLVENTKE---IFKRIKCKNKKLIKNImkdmlttlEYIHEHGISHGDIKPENIMV----DGN 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  170 RKCYMLDFGLARQYTNTTGDVRPPRNVAGF-RGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV 248
Cdd:PHA02882   163 NRGYIIDYGIASHFIIHGKHIEYSKEQKDLhRGTLYYAGLDAHNGACVTRRGDLESLGYCMLKWAGIKLPWKGFGHNGNL 242
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  249 ------GMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFE 294
Cdd:PHA02882   243 ihaakcDFIKRLHEGKIKIKNANKFIYDFIECVTKLSYEEKPDYDALIKIFD 294
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
34-242 2.77e-22

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: 97.66  E-value: 2.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM-QL 109
Cdd:cd05122      2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKinlESKEKKESILN-EIAILKKCK-HPNIVKYYGSYLKKDELWIVMeFC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMG-----RLpstyrkcymLDFGLARQYT 184
Cdd:cd05122     80 SGGSLKDLLKNTNK-TLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTsdgevKL---------IDFGLSAQLS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  185 NTTGDVRpprnvagFRGTVRYASvnahknREM---GRHD---DLWSLFYMLVEFAVGQLPWRKI 242
Cdd:cd05122    150 DGKTRNT-------FVGTPYWMA------PEViqgKPYGfkaDIWSLGITAIEMAEGKPPYSEL 200
STKc_VRK2 cd14123
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs ...
25-292 8.53e-22

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK2 exists as two alternative splice forms, A and B, which differ in their C-terminal regions. VRK2A, the predominant isoform, contains a hydrophobic tail and is anchored to the ER and mitochondria. It is expressed in all cell types. VRK2B lacks a membrane-anchor tail and is detected in the cytosol and the nucleus. Like VRK1, it can stabilize p53. VRK2B functionally replaces VRK1 in the nucleus of cell types where VRK1 is absent. VRK2 modulates hypoxia-induced stress responses by interacting with TAK1, an atypical MAPK kinase kinase which triggers cascades that activate JNK following oxidative stress. VRK2 also interacts with JIP1, a scaffold protein that assembles three consecutive members of a MAPK pathway. This interaction prevents the association of JNK with the signaling complex, leading to reduced phosphorylation and AP1-dependent transcription. The VRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271025 [Multi-domain]  Cd Length: 302  Bit Score: 97.61  E-value: 8.53e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   25 PANYVVKD----RWKVLKKIGGGGFGEIYEA---MDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFI--- 94
Cdd:cd14123      1 PEGCILTDtekkNWRLGKMIGKGGFGLIYLAspqVNVPVEDDAVHVIKVEYHENGPLFSELKFYQRAAKPDTISKWMksk 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   95 -----------GCGRNE----KFNYVVMQLQGRNLADLRrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN 159
Cdd:cd14123     81 qldylgiptywGSGLTEfngtSYRFMVMDRLGTDLQKIL-IDNGGQFKKTTVLQLGIRMLDVLEYIHENEYVHGDIKAAN 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  160 FAMGRlpSTYRKCYMLDFGLARQYT---NTTGDVRPPRNvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQ 236
Cdd:cd14123    160 LLLGY--RNPNEVYLADYGLSYRYCpngNHKEYKENPRK--GHNGTIEFTSLDAHKGVAPSRRGDLEILGYCMLHWLCGK 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  237 LPW-RKIKDKEQVGMIKEKyehrmLLKHMP-------------SEFHLFLDHIASLDYFTKPDYQLIMSV 292
Cdd:cd14123    236 LPWeQNLKNPVAVQEAKAK-----LLSNLPdsvlkwstggsssMEIAQFLSRVKDLAYDEKPDYQALKKI 300
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
35-251 1.97e-21

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: 95.38  E-value: 1.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKVESA--QQPKQVLKmEVAVLKKL---QGKDHVCRFIGCGRNEKFNYV--VM 107
Cdd:cd05118      2 EVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNdfRHPKAALR-EIKLLKHLndvEGHPNIVKLLDVFEHRGGNHLclVF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCymlDFGLARQYTNTT 187
Cdd:cd05118     81 ELMGMNLYELIKDYPRG-LPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQLKLA---DFGLARSFTSPP 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  188 GDVRP-PRnvaGFR------GTVRYasvnahknremGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMI 251
Cdd:cd05118    157 YTPYVaTR---WYRapevllGAKPY-----------GSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKI 213
STKc_VRK1 cd14122
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs ...
31-286 1.01e-20

Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. Vertebrates contain three VRK proteins. Human VRK1 is implicated in the regulation of many cellular processes including cell cycle progression and proliferation, stress responses, nuclear envelope assembly and chromatin condensation. It regulates cell cycle progression during the DNA replication period by inducing cyclin D1 expression. VRK1 also phosphorylates and regulates some transcription factors including p53, c-Jun, ATF2, and nuclear factor BAF. VRK1 stabilizes p53 by interfering with its mdm2-mediated degradation. Accumulation of p53, which blocks cell growth and division, is modulated by an autoregulatory loop between p53 and VRK1 (accumulated p53 downregulates VRK1). This autoregulatory loop has been found to be nonfunctional in some lung carcinomas. The VRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271024 [Multi-domain]  Cd Length: 301  Bit Score: 94.57  E-value: 1.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAmDLLTRENVA------LKVESAQ---------------QPKQVLK-MEVAVLKKLQgkd 88
Cdd:cd14122      9 KKEWKLGLPIGQGGFGRLYLA-DENSSESVGsdapyvVKVEPSDngplftelkfymraaKPDQIQKwIKSHKLKYLG--- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   89 hVCRFIGCGRNEK----FNYVVMQLQGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGR 164
Cdd:cd14122     85 -VPKYWGSGLHEKngksYRFMIMDRFGSDLQKIYEANAK-RFSRKTVLQLGLRILDILEYIHEHEYVHGDIKASNLLLSY 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  165 lpSTYRKCYMLDFGLARQYT------NTTGDVRPPRNvagfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd14122    163 --KNPDQVYLVDYGLAYRYCpegvhkEYKEDPKRCHD-----GTIEFTSIDAHKGVAPSRRGDLEILGYCMIQWLCGHLP 235
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  239 WR-KIKDKEQVGMIKEKYEHRM--LL------KHMPSEFHLFLDHIASLDYFTKPDY 286
Cdd:cd14122    236 WEdNLKDPNYVRDSKIRYRDNIseLMekcfpgKNKPGEIRKYMETVKLLGYTEKPLY 292
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
33-186 2.43e-20

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: 92.15  E-value: 2.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLqgkDH--VCRFIGCGRNEKFNYVV 106
Cdd:cd05117      1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIidkkKLKSEDEEMLRREIEILKRL---DHpnIVKLYEVFEDDKNLYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQL-QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFaMGRLPSTYRKCYMLDFGLARQYTN 185
Cdd:cd05117     78 MELcTGGELFD--RIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENI-LLASKDPDSPIKIIDFGLAKIFEE 154

                   .
gi 1034651883  186 T 186
Cdd:cd05117    155 G 155
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
33-294 1.90e-19

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: 90.09  E-value: 1.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVE--SAQQPKQVLKMEVAVLKKLQGKDHVCRFIGC----GRNEKFNYVV 106
Cdd:cd13985      1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMyfNDEEQLRVAIKEIEIMKRLCGHPNIVQYYDSailsSEGRKEVLLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVG--FLHRDIKPSNFamgrLPSTYRKCYMLDFGLA---- 180
Cdd:cd13985     81 MEYCPGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENI----LFSNTGRFKLCDFGSAtteh 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQYT--------------NTTGDVRPPRnvagfrgtvryaSVNAHKNREMGRHDDLWSL---FYMLVEFavgQLPWrkiK 243
Cdd:cd13985    157 YPLEraeevniieeeiqkNTTPMYRAPE------------MIDLYSKKPIGEKADIWALgclLYKLCFF---KLPF---D 218
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  244 DKEQVGMIKEKYehrmLLKHMPS---EFHLFLDHIASLDYFTKPD-YQLIMSVFE 294
Cdd:cd13985    219 ESSKLAIVAGKY----SIPEQPRyspELHDLIRHMLTPDPAERPDiFQVINIITK 269
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
35-267 7.67e-19

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: 88.12  E-value: 7.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLkMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL- 109
Cdd:cd13996      9 EEIELLGSGGFGSVYKVRNKVDGVTYAIKKirltEKSSASEKVL-REVKALAKLNHP-NIVRYYTAWVEEPPLYIQMELc 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLADL---RRSQPRGTFTLSttLRLGKQILESIEAIHSVGFLHRDIKPSN-FamgrLPSTYRKCYMLDFGLARQYTN 185
Cdd:cd13996     87 EGGTLRDWidrRNSSSKNDRKLA--LELFKQILKGVSYIHSKGIVHRDLKPSNiF----LDNDDLQVKIGDFGLATSIGN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  186 TTGDVRP-PRNVAG-------FRGTVRYASVNAHKNREMGRHDDLWS----LFYMLVEFAV-------------GQLP-W 239
Cdd:cd13996    161 QKRELNNlNNNNNGntsnnsvGIGTPLYASPEQLDGENYNEKADIYSlgiiLFEMLHPFKTamerstiltdlrnGILPeS 240
                          250       260
                   ....*....|....*....|....*...
gi 1034651883  240 RKIKDKEQVGMIKEkyehrmLLKHMPSE 267
Cdd:cd13996    241 FKAKHPKEADLIQS------LLSKNPEE 262
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
34-247 1.08e-18

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: 87.39  E-value: 1.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQV----LKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL 109
Cdd:cd14069      3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDcpenIKKEVCIQKMLSHK-NVVRFYGHRREGEFQYLFLEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPstyrkcyMLDFGLARQYTN 185
Cdd:cd14069     82 aSGGELFD--KIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLdenDNLK-------ISDFGLATVFRY 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  186 TTGDvrppRNVAGFRGTVRYASVNAHKNREM-GRHDDLWS----LFYMLvefaVGQLPWRKIKDKEQ 247
Cdd:cd14069    153 KGKE----RLLNKMCGTLPYVAPELLAKKKYrAEPVDVWScgivLFAML----AGELPWDQPSDSCQ 211
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
33-264 1.60e-18

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: 86.80  E-value: 1.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14003      1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIidksKLKEEIEEKIKREIEIMKLLNHP-NIIKLYEVIETENKIYLVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN---FAMGRLPSTyrkcymlDFGLARQYt 184
Cdd:cd14003     80 YaSGGELFDYIVN--NGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENillDKNGNLKII-------DFGLSNEF- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  185 ntTGDVRPprnvAGFRGTVRYAS--VNAHKNREmGRHDDLWS----LFYMLvefaVGQLPWRKIKDKEQVGMI-KEKYEH 257
Cdd:cd14003    150 --RGGSLL----KTFCGTPAYAApeVLLGRKYD-GPKADVWSlgviLYAML----TGYLPFDDDNDSKLFRKIlKGKYPI 218
                          250
                   ....*....|....*
gi 1034651883  258 --------RMLLKHM 264
Cdd:cd14003    219 pshlspdaRDLIRRM 233
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
36-243 3.06e-18

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: 86.50  E-value: 3.06e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMDLLTREnVALKV----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIG--CGRNEKFNYVVMQL 109
Cdd:cd14131      5 ILKQLGKGGSSKVYKVLNPKKKI-YALKRvdleGADEQTLQSYKNEIELLKKLKGSDRIIQLYDyeVTDEDDYLYMVMEC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM--GRLpstyrKcyMLDFGLARQY-TNT 186
Cdd:cd14131     84 GEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLvkGRL-----K--LIDFGIAKAIqNDT 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  187 TGDVRPPRnvagfRGTVRYAS------VNAHKNRE----MGRHDDLWSL---FYMLV----EFAVGQLPWRKIK 243
Cdd:cd14131    157 TSIVRDSQ-----VGTLNYMSpeaikdTSASGEGKpkskIGRPSDVWSLgciLYQMVygktPFQHITNPIAKLQ 225
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
33-239 4.44e-18

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: 85.82  E-value: 4.44e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVA-VLKKLQGKDH--VCRFIG--CGRNEKfnYVVM 107
Cdd:cd06626      1 RWQRGNKIGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIAdEMKVLEGLDHpnLVRYYGveVHREEV--YIFM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QL-QGRNLADLRRSqprgTFTLSTTL--RLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpsTYRKCYML-DFGLARQY 183
Cdd:cd06626     79 EYcQEGTLEELLRH----GRILDEAVirVYTLQLLEGLAYLHENGIVHRDIKPANIFL-----DSNGLIKLgDFGSAVKL 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  184 TNTTgDVRPPRNVAGFRGTVRYAS---VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06626    150 KNNT-TTMAPGEVNSLVGTPAYMApevITGNKGEGHGRAADIWSLGCVVLEMATGKRPW 207
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
33-251 3.91e-17

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: 82.84  E-value: 3.91e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK----VESAQQPKQVLKM---EVAVLKKLQGKDHVcRFIGCGRNEKFNYV 105
Cdd:cd06632      1 RWQKGQLLGSGSFGSVYEGFNGDTGDFFAVKevslVDDDKKSRESVKQleqEIALLSKLRHPNIV-QYYGTEREEDNLYI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQL-QGRNLADLrrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYT 184
Cdd:cd06632     80 FLEYvPGGSIHKL--LQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANI----LVDTNGVVKLADFGMAKHVE 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  185 NttgdvrpPRNVAGFRGTVRYAS--VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWrkiKDKEQVGMI 251
Cdd:cd06632    154 A-------FSFAKSFKGSPYWMApeVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAI 212
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
40-268 3.95e-17

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: 82.59  E-value: 3.95e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAmdLLTRENVALKV-----ESAQQPKQVLKmEVAVLKKLQgkdH--VCRFIGCGRNEKFNYVVMQL-QG 111
Cdd:cd13999      1 IGSGSFGEVYKG--KWRGTDVAIKKlkvedDNDELLKEFRR-EVSILSKLR---HpnIVQFIGACLSPPPLCIVTEYmPG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNfamgrlpstyrkcyML----------DFGLAR 181
Cdd:cd13999     75 GSLYDLLHKK-KIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLN--------------ILldenftvkiaDFGLSR 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  182 QYTNTTGDVRpprnvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLL 261
Cdd:cd13999    140 IKNSTTEKMT------GVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRPPIP 213

                   ....*..
gi 1034651883  262 KHMPSEF 268
Cdd:cd13999    214 PDCPPEL 220
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
32-180 4.65e-17

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


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 82.60  E-value: 4.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQV--LKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVV 106
Cdd:cd14099      1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVvpkSSLTKPKQRekLKSEIKIHRSLKHP-NIVKFHDCFEDEENVYIL 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  107 MQL-QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstyrkcYML----DFGLA 180
Cdd:cd14099     80 LELcSNGSLMELLKR--RKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDE--------NMNvkigDFGLA 148
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
35-269 6.44e-17

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 82.19  E-value: 6.44e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883    35 KVLKKIGGGGFGEIYEAM----DLLTRENVALKV----ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:smart00219    2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTlkedASEQQIEEFLR-EARIMRKLD-HPNVVKLLGVCTEEEPLYIV 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   107 MQL-QGRNLADLRRsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR---- 181
Cdd:smart00219   80 MEYmEGGDLLSYLR-KNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNC----LVGENLVVKISDFGLSRdlyd 154
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   182 -QYTNTTGDvrpprnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKYehRM 259
Cdd:smart00219  155 dDYYRKRGG----------KLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEiFTLGEQPYPGMSNEEVLEYLKNGY--RL 222
                           250
                    ....*....|.
gi 1034651883   260 LL-KHMPSEFH 269
Cdd:smart00219  223 PQpPNCPPELY 233
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
33-239 8.11e-17

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 82.02  E-value: 8.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYV 105
Cdd:cd06625      1 NWKQGKLLGQGAFGQVYLCYDADTGRELAVKQveidpINTEASKEVkaLECEIQLLKNLQ-HERIVQYYGCLQDEKSLSI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQ-LQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR--Q 182
Cdd:cd06625     80 FMEyMPGGSVKDEIKAY--GALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANI----LRDSNGNVKLGDFGASKrlQ 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  183 YTNTTGDVRPprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06625    154 TICSSTGMKS------VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPW 204
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
35-201 1.10e-16

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 81.50  E-value: 1.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLT-------RENVALK-VESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd14019      4 RIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKhIYPTSSPSRILN-ELECLERLGGSNNVSGLITAFRNEDQVVAV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQ-LQGRNLADLRRsqprgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpsTYRKCYMLDFGLArQYTN 185
Cdd:cd14019     83 LPyIEHDDFRDFYR-----KMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNR---ETGKGVLVDFGLA-QREE 153
                          170
                   ....*....|....*.
gi 1034651883  186 TTGDVRPPRnvAGFRG 201
Cdd:cd14019    154 DRPEQRAPR--AGTRG 167
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
23-237 1.10e-16

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


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 83.00  E-value: 1.10e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   23 ILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--------ESAqqpkqvlKMEVAVLKKLQGKD-----H 89
Cdd:cd14134      3 IYKPGDLLTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIirnvekyrEAA-------KIEIDVLETLAEKDpngksH 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   90 VCRFIGCgrnekFNY-----VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN--FAM 162
Cdd:cd14134     76 CVQLRDW-----FDYrghmcIVFELLGPSLYDFLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENilLVD 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  163 GRLPSTY---RKCYML----------DFGLA-------------RQYtnttgdvRPPRNVAGFRGTvrYASvnahknrem 216
Cdd:cd14134    151 SDYVKVYnpkKKRQIRvpkstdikliDFGSAtfddeyhssivstRHY-------RAPEVILGLGWS--YPC--------- 212
                          250       260
                   ....*....|....*....|.
gi 1034651883  217 grhdDLWSLFYMLVEFAVGQL 237
Cdd:cd14134    213 ----DVWSIGCILVELYTGEL 229
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
35-269 1.29e-16

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: 81.44  E-value: 1.29e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883    35 KVLKKIGGGGFGEIYEAM----DLLTRENVA---LKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:smart00221    2 TLGKKLGEGAFGEVYKGTlkgkGDGKEVEVAvktLKEDASEQQIEEFLREARIMRKLD-HPNIVKLLGVCTEEEPLMIVM 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   108 QL-QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNT 186
Cdd:smart00221   81 EYmPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNC----LVGENLVVKISDFGLSRDLYDD 156
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   187 TGDVrpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKYehRMLL-KHM 264
Cdd:smart00221  157 DYYK-----VKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEiFTLGEEPYPGMSNAEVLEYLKKGY--RLPKpPNC 229

                    ....*
gi 1034651883   265 PSEFH 269
Cdd:smart00221  230 PPELY 234
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
38-198 3.69e-16

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: 79.96  E-value: 3.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPK---QVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL-QGR 112
Cdd:cd06627      6 DLIGRGAFGSVYKGLNLNTGEFVAIKqISLEKIPKsdlKSVMGEIDLLKKLNHP-NIVKYIGSVKTKDSLYIILEYvENG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRsqPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPStyrkCYMLDFGLArqyTNTTGDVRP 192
Cdd:cd06627     85 SLASIIK--KFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGL----VKLADFGVA---TKLNEVEKD 155

                   ....*.
gi 1034651883  193 PRNVAG 198
Cdd:cd06627    156 ENSVVG 161
Pkinase pfam00069
Protein kinase domain;
34-273 4.46e-16

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 78.82  E-value: 4.46e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQVLkMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQ 108
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKikkekIKKKKDKNIL-REIKILKKLNHP-NIVRLYDAFEDKDNLYLVLE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADLRRsqPRGTFTLSTTLRLGKQILEsieaihsvgflhrdikpsnfamgrlpstyrkcymldfGLARQYTNTT 187
Cdd:pfam00069   79 YvEGGSLFDLLS--EKGAFSEREAKFIMKQILE-------------------------------------GLESGSSLTT 119
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 gdvrpprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV-GMIKEKYEHRMLLKHMPS 266
Cdd:pfam00069  120 -----------FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYeLIIDQPYAFPELPSNLSE 188

                   ....*..
gi 1034651883  267 EFHLFLD 273
Cdd:pfam00069  189 EAKDLLK 195
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
35-238 7.99e-16

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: 78.79  E-value: 7.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ-LQGR 112
Cdd:cd06614      3 KNLEKIGEGASGEVYKATDRATGKEVAIKKmRLRKQNKELIINEILIMKECK-HPNIVDYYDSYLVGDELWVVMEyMDGG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPStyrkCYMLDFGLARQYTNTtgdvRP 192
Cdd:cd06614     82 SLTDIIT-QNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGS----VKLADFGFAAQLTKE----KS 152
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034651883  193 PRN--VagfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06614    153 KRNsvV----GTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPP 196
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
31-238 3.09e-15

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: 77.81  E-value: 3.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVM 107
Cdd:cd06641      3 EELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIidlEEAEDEIEDIQQEITVLSQCDSP-YVTKYYGSYLKDTKLWIIM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 Q-LQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNT 186
Cdd:cd06641     82 EyLGGGSALDLLEPGPLDETQIATILR---EILKGLDYLHSEKKIHRDIKAANV----LLSEHGEVKLADFGVAGQLTDT 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  187 tgdvRPPRNvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06641    155 ----QIKRN--*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
40-239 6.02e-15

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: 76.44  E-value: 6.02e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKV----------------ESAQQPKQVLKMEVAVLKKLqgkDH--VCRFIGCGRNEK 101
Cdd:cd14008      1 LGRGSFGKVKLALDTETGQLYAIKIfnksrlrkrregkndrGKIKNALDDVRREIAIMKKL---DHpnIVRLYEVIDDPE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FN--YVVMQL-QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFG 178
Cdd:cd14008     78 SDklYLVLEYcEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENL----LLTADGTVKISDFG 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  179 LARQYTNTTGDVrppRNVAG---------FRGTVRYASvnahknremGRHDDLWSL---FYMLVefaVGQLPW 239
Cdd:cd14008    154 VSEMFEDGNDTL---QKTAGtpaflapelCDGDSKTYS---------GKAADIWALgvtLYCLV---FGRLPF 211
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
37-238 9.17e-15

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: 76.24  E-value: 9.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQ-LQGR 112
Cdd:cd06640      9 LERIGKGSFGEVFKGIDNRTQQVVAIKIidlEEAEDEIEDIQQEITVLSQCDSP-YVTKYYGSYLKGTKLWIIMEyLGGG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLrlgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTtgdvRP 192
Cdd:cd06640     88 SALDLLRAGPFDEFQIATML---KEILKGLDYLHSEKKIHRDIKAANV----LLSEQGDVKLADFGVAGQLTDT----QI 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034651883  193 PRNVagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06640    157 KRNT--FVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
28-182 1.04e-14

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: 77.33  E-value: 1.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   28 YVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCR---FIGCGRN 99
Cdd:cd07851     11 WEVPDRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKklsrpFQSAIHAKRTYR-ELRLLKHMKHENVIGLldvFTPASSL 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  100 EKFN--YVVMQLQGRNLADLRRSQPrgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKCYM--L 175
Cdd:cd07851     90 EDFQdvYLVTHLMGADLNNIVKCQK---LSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVN------EDCELkiL 160

                   ....*..
gi 1034651883  176 DFGLARQ 182
Cdd:cd07851    161 DFGLARH 167
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
32-238 1.20e-14

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: 75.74  E-value: 1.20e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCG-RNEKFnYVVM 107
Cdd:cd06609      1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVidlEEAEDEIEDIQQEIQFLSQCDSP-YITKYYGSFlKGSKL-WIIM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 Q-LQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNT 186
Cdd:cd06609     79 EyCGGGSVLDLLKPGPLDETYIAFILR---EVLLGLEYLHSEGKIHRDIKAANI----LLSEEGDVKLADFGVSGQLTST 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  187 TGDvrppRNVagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06609    152 MSK----RNT--FVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPP 197
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
33-193 1.47e-14

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: 75.83  E-value: 1.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ-----PKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd07832      1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKleggiPNQALR-EIKALQACQGHPYVVKLRDVFPHGTGFVLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlPSTYRKcyMLDFGLARQYTNtt 187
Cdd:cd07832     80 EYMLSSLSEVLRDEER-PLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS--STGVLK--IADFGLARLFSE-- 152

                   ....*.
gi 1034651883  188 GDVRPP 193
Cdd:cd07832    153 EDPRLY 158
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
32-184 1.87e-14

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: 75.43  E-value: 1.87e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK----VESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVM 107
Cdd:cd07833      1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKkfkeSEDDEDVKKTALREVKVLRQLRHE-NIVNLKEAFRRKGRLYLVF 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  108 QLQGRNLADLRRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYT 184
Cdd:cd07833     80 EYVERTLLELLEASPGG-LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENI----LVSESGVLKLCDFGFARALT 151
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
33-284 2.06e-14

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: 74.88  E-value: 2.06e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK--------VESAQQPKQV---LKMEVAVLKKLQgKDHVCRFIGCGRNEK 101
Cdd:cd06628      1 KWIKGALIGSGSFGSVYLGMNASSGELMAVKqvelpsvsAENKDRKKSMldaLQREIALLRELQ-HENIVQYLGSSSDAN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 F-NYVVMQLQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLA 180
Cdd:cd06628     80 HlNIFLEYVPGGSVATLLNNY--GAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANI----LVDNKGGIKISDFGIS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQ-----YTNTTGDVRPprnvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEkY 255
Cdd:cd06628    154 KKleansLSTKNNGARP-----SLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAIFKIGE-N 227
                          250       260
                   ....*....|....*....|....*....
gi 1034651883  256 EHRMLLKHMPSEFHLFLDHIASLDYFTKP 284
Cdd:cd06628    228 ASPTIPSNISSEARDFLEKTFEIDHNKRP 256
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
37-259 2.30e-14

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: 74.84  E-value: 2.30e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEA----MDLLTRENVALKV--ESAQQPKQV-LKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL 109
Cdd:pfam07714    4 GEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTlkEGADEEEREdFLEEASIMKKLDHP-NIVKLLGVCTQGEPLYIVTEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLAD-LRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR------ 181
Cdd:pfam07714   83 mPGGDLLDfLRKHKRK--LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNC----LVSENLVVKISDFGLSRdiyddd 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  182 QYTNTTGDVRPprnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKYehRM 259
Cdd:pfam07714  157 YYRKRGGGKLP----------IKWMAPESLKDGKFTSKSDVWSFGVLLWEiFTLGEQPYPGMSNEEVLEFLEDGY--RL 223
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
33-241 3.13e-14

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: 74.31  E-value: 3.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--------ESAQQPKQVLKM-EVAVLKKLQGKDHVCRFIGCGRNEKFN 103
Cdd:cd13993      1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKClyksgpnsKDGNDFQKLPQLrEIDLHRRVSRHPNIITLHDVFETEVAI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQL--QGrNLADLRRSqpRGTFTLSTTL--RLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCymlDFGL 179
Cdd:cd13993     81 YIVLEYcpNG-DLFEAITE--NRIYVGKTELikNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEGTVKLC---DFGL 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  180 ArqytnTTGDVRPPRNVagfrGTVRYAS----VNAHKNREM--GRHDDLWSLFYMLVEFAVGQLPWRK 241
Cdd:cd13993    155 A-----TTEKISMDFGV----GSEFYMApecfDEVGRSLKGypCAAGDIWSLGIILLNLTFGRNPWKI 213
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
40-253 3.14e-14

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: 74.37  E-value: 3.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK--VESAQQPKQVLKMEVAVLKKLQGKDHVcRFIGCGRNEKFNYVVM-QLQGRNLAD 116
Cdd:cd06624     16 LGKGTFGVVYAARDLSTQVRIAIKeiPERDSREVQPLHEEIALHSRLSHKNIV-QYLGSVSEDGFFKIFMeQVPGGSLSA 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  117 LRRSQPRGTFTLSTTLRL-GKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYML-DFGLARQYtnttGDVRPpr 194
Cdd:cd06624     95 LLRSKWGPLKDNENTIGYyTKQILEGLKYLHDNKIVHRDIKGDNV----LVNTYSGVVKIsDFGTSKRL----AGINP-- 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  195 NVAGFRGTVRYAS--VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKE----QVGMIKE 253
Cdd:cd06624    165 CTETFTGTLQYMApeVIDKGQRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQaamfKVGMFKI 229
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
37-239 4.62e-14

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: 74.32  E-value: 4.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQ-LQGR 112
Cdd:cd06642      9 LERIGKGSFGEVYKGIDNRTKEVVAIKIidlEEAEDEIEDIQQEITVLSQCDSP-YITRYYGSYLKGTKLWIIMEyLGGG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTtgdvRP 192
Cdd:cd06642     88 SALDLLKPGPLEETYIATILR---EILKGLDYLHSERKIHRDIKAANV----LLSEQGDVKLADFGVAGQLTDT----QI 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1034651883  193 PRNVagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06642    157 KRNT--FVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
34-178 5.78e-14

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: 73.46  E-value: 5.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQP--KQVLKmEVAVLKKL-----QGKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd14133      1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDylDQSLD-EIRLLELLnkkdkADKYHIVRLKDVFYFKNHLCIV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  107 MQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKC--YMLDFG 178
Cdd:cd14133     80 FELLSQNLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENI----LLASYSRCqiKIIDFG 149
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
35-193 8.46e-14

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: 73.34  E-value: 8.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKvesaqqpkqvlKM--------------EVAVLKKLQGKDHVCR----FIgc 96
Cdd:cd07830      2 KVIKQLGDGTFGSVYLARNKETGELVAIK-----------KMkkkfysweecmnlrEVKSLRKLNEHPNIVKlkevFR-- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   97 grnEKFN-YVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYML 175
Cdd:cd07830     69 ---ENDElYFVFEYMEGNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENL----LVSGPEVVKIA 141
                          170
                   ....*....|....*...
gi 1034651883  176 DFGLARQYTNttgdvRPP 193
Cdd:cd07830    142 DFGLAREIRS-----RPP 154
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
35-240 8.89e-14

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: 73.40  E-value: 8.89e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ------PKQVlKMEVAVLKKLqgkDH--VCRFIGCGRNEKFNYVV 106
Cdd:cd05581      4 KFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHiikekkVKYV-TIEKEVLSRL---AHpgIVKLYYTFQDESKLYFV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQL-QGRNLAD-LRRsqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpsTYRKCyMLDFGLARQYT 184
Cdd:cd05581     80 LEYaPNGDLLEyIRK---YGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDE---DMHIK-ITDFGTAKVLG 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  185 NT-----------TGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:cd05581    153 PDsspestkgdadSQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFR 219
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
32-208 9.84e-14

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: 73.89  E-value: 9.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQGKDhVCRFI--------GCGR 98
Cdd:cd07866      8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKkilMHNEKDgfPITALR-EIKILKKLKHPN-VVPLIdmaverpdKSKR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   99 NEKFNYVVMQLQGRNLADLRrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFG 178
Cdd:cd07866     86 KRGSVYMVTPYMDHDLSGLL-ENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANI----LIDNQGILKIADFG 160
                          170       180       190
                   ....*....|....*....|....*....|
gi 1034651883  179 LARQYTnttgDVRPPRNVAGFRGTVRYASV 208
Cdd:cd07866    161 LARPYD----GPPPNPKGGGGGGTRKYTNL 186
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
30-243 1.71e-13

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: 72.03  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ-----PKqvLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNY 104
Cdd:cd14078      1 LLKYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgddlPR--VKTEIEALKNLSHQ-HICRLYHVIETDNKIF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQL-QGRNLAD-------LRRSQPRGTFtlsttlrlgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLD 176
Cdd:cd14078     78 MVLEYcPGGELFDyivakdrLSEDEARVFF---------RQIVSAVAYVHSQGYAHRDLKPENL----LLDEDQNLKLID 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  177 FGLARQytnttgdvrpPRNVAGFR-----GTVRYASVNAHKNRE-MGRHDDLWSLFYMLVEFAVGQLP---------WRK 241
Cdd:cd14078    145 FGLCAK----------PKGGMDHHletccGSPAYAAPELIQGKPyIGSEADVWSMGVLLYALLCGFLPfdddnvmalYRK 214

                   ..
gi 1034651883  242 IK 243
Cdd:cd14078    215 IQ 216
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
30-182 2.19e-13

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: 73.16  E-value: 2.19e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESaqQPKQVL------KMEVAVLKKLQGKDHVCR---FIGCGRNE 100
Cdd:cd07878     13 VPERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLS--RPFQSLiharrtYRELRLLKHMKHENVIGLldvFTPATSIE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFN--YVVMQLQGRNLADLRRSQprgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKCYM--LD 176
Cdd:cd07878     91 NFNevYLVTNLMGADLNNIVKCQ---KLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVN------EDCELriLD 161

                   ....*.
gi 1034651883  177 FGLARQ 182
Cdd:cd07878    162 FGLARQ 167
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
34-239 2.65e-13

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 71.59  E-value: 2.65e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN---EKFN 103
Cdd:cd06653      4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQvpfdpDSQETSKEVnaLECEIQLLKNLR-HDRIVQYYGCLRDpeeKKLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQLQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQ- 182
Cdd:cd06653     83 IFVEYMPGGSVKDQLKAY--GALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANI----LRDSAGNVKLGDFGASKRi 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  183 ---YTNTTGdvrpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06653    157 qtiCMSGTG-------IKSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
33-187 4.05e-13

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: 70.95  E-value: 4.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQVLKmEVAVLKKLqgkDHVC--RFIGCGRNEKFNYV 105
Cdd:cd08215      1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEidlsnMSEKEREEALN-EVKLLSKL---KHPNivKYYESFEENGKLCI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQL-QGRNLADL--RRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN---FAMGRLpstyrKcymL-DFG 178
Cdd:cd08215     77 VMEYaDGGDLAQKikKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNiflTKDGVV-----K---LgDFG 148

                   ....*....
gi 1034651883  179 LARQYTNTT 187
Cdd:cd08215    149 ISKVLESTT 157
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
27-183 4.92e-13

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


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 71.42  E-value: 4.92e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   27 NYVVK----DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVlKMEVAVLKKLQGKDHVCRFIGCGRNEK- 101
Cdd:cd14132      9 NLNVEwgsqDDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKI-KREIKILQNLRGGPNIVKLLDVVKDPQs 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 ------FNYVvmqlqgrNLADLRRSQPrgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpsTYRKCYML 175
Cdd:cd14132     88 ktpsliFEYV-------NNTDFKTLYP--TLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDH---EKRKLRLI 155

                   ....*...
gi 1034651883  176 DFGLARQY 183
Cdd:cd14132    156 DWGLAEFY 163
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
32-192 5.21e-13

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: 71.63  E-value: 5.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEK--FN- 103
Cdd:cd07865     12 SKYEKLAKIGQGTFGEVFKARHRKTGQIVALKkvlMENEKEgfPITALR-EIKILQLLK-HENVVNLIEICRTKAtpYNr 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 -----YVVMQLQGRNLADLRrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPstyrkcyML 175
Cdd:cd07865     90 ykgsiYLVFEFCEHDLAGLL-SNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILItkdGVLK-------LA 161
                          170
                   ....*....|....*..
gi 1034651883  176 DFGLARQYTNTTGDVRP 192
Cdd:cd07865    162 DFGLARAFSLAKNSQPN 178
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
34-275 5.30e-13

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 70.84  E-value: 5.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN--EKFNY 104
Cdd:cd06652      4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQvqfdpESPETSKEVnaLECEIQLLKNLL-HERIVQYYGCLRDpqERTLS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQLQ-GRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQY 183
Cdd:cd06652     83 IFMEYMpGGSIKDQLKSY--GALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANI----LRDSVGNVKLGDFGASKRL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  184 TNTTGDVRPPRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKH 263
Cdd:cd06652    157 QTICLSGTGMKSVT---GTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPAH 233
                          250
                   ....*....|..
gi 1034651883  264 MPSEFHLFLDHI 275
Cdd:cd06652    234 VSDHCRDFLKRI 245
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
27-178 8.95e-13

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 71.04  E-value: 8.95e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   27 NYVVKD----RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQVLkMEVAVLKKLQGKD-----HVCRFIg 95
Cdd:cd14210      4 KVVLGDhiayRYEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIirNKKRFHQQAL-VEVKILKHLNDNDpddkhNIVRYK- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   96 cgrnEKFNY-----VVMQLQGRNLADLRRSQP-RGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgRLPSTY 169
Cdd:cd14210     82 ----DSFIFrghlcIVFELLSINLYELLKSNNfQG-LSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILL-KQPSKS 155

                   ....*....
gi 1034651883  170 RkCYMLDFG 178
Cdd:cd14210    156 S-IKVIDFG 163
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
35-185 9.75e-13

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: 70.29  E-value: 9.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEK-------- 101
Cdd:cd07840      2 EKIAQIGEGTYGQVYKARNKKTGELVALKkirMENEKEgfPITAIR-EIKLLQKLD-HPNVVRLKEIVTSKGsakykgsi 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 ---FNYVVMQLQGrnLADlrrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyrkcyml 175
Cdd:cd07840     80 ymvFEYMDHDLTG--LLD----NPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILInndGVLKLA------- 146
                          170
                   ....*....|
gi 1034651883  176 DFGLARQYTN 185
Cdd:cd07840    147 DFGLARPYTK 156
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
37-184 1.32e-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. 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: 69.82  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKVesaqqpkqvLKM-------------EVAVLKKLQgKDHVCRFIGCGRNEKFN 103
Cdd:cd07829      4 LEKLGEGTYGVVYKAKDKKTGEIVALKK---------IRLdneeegipstalrEISLLKELK-HPNIVKLLDVIHTENKL 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQLQGRNLADLRRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstyrkcYML----DFGL 179
Cdd:cd07829     74 YLVFEYCDQDLKKYLDKRPGP-LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINR--------DGVlklaDFGL 144

                   ....*
gi 1034651883  180 ARQYT 184
Cdd:cd07829    145 ARAFG 149
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
40-181 1.94e-12

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: 68.79  E-value: 1.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQ--QPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ-LQGRNL 114
Cdd:cd14009      1 IGRGSFATVWKGRHKQTGEVVAIKEISRKklNKKLQenLESEIAILKSIK-HPNIVRLYDVQKTEDFIYLVLEyCAGGDL 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  115 AD-LRRsqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYML---DFGLAR 181
Cdd:cd14009     80 SQyIRK---RGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNL----LLSTSGDDPVLkiaDFGFAR 143
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
30-287 1.98e-12

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 70.45  E-value: 1.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCR---FIGCGRNEK 101
Cdd:cd07877     15 VPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKklsrpFQSIIHAKRTYR-ELRLLKHMKHENVIGLldvFTPARSLEE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FN--YVVMQLQGRNLADLRRSQprgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKCYM--LDF 177
Cdd:cd07877     94 FNdvYLVTHLMGADLNNIVKCQ---KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVN------EDCELkiLDF 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  178 GLARQytntTGDvrpprNVAGFRGTVRYASVN-----AHKNREMgrhdDLWSLFYMLVEFAVGQ--LPWRKIKDKEQVGM 250
Cdd:cd07877    165 GLARH----TDD-----EMTGYVATRWYRAPEimlnwMHYNQTV----DIWSVGCIMAELLTGRtlFPGTDHIDQLKLIL 231
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1034651883  251 IKEKYEHRMLLKHMPSefHLFLDHIASLDYFTKPDYQ 287
Cdd:cd07877    232 RLVGTPGAELLKKISS--ESARNYIQSLTQMPKMNFA 266
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
33-239 2.31e-12

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: 68.83  E-value: 2.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK----VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFnYVVMQ 108
Cdd:cd08225      1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKeidlTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRL-FIVME 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADlRRSQPRGT-FTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTYRKCYMLDFGLARQYTNT 186
Cdd:cd08225     80 YcDGGDLMK-RINRQRGVlFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIF---LSKNGMVAKLGDFGIARQLNDS 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  187 TGDVRPprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd08225    156 MELAYT------CVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPF 202
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
30-181 2.87e-12

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 68.55  E-value: 2.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKDHVcRFIGCGRNEKFNYVV 106
Cdd:cd14083      1 IRDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCidkKALKGKEDSLENEIAVLRKIKHPNIV-QLLDIYESKSHLYLV 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  107 MQL-QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFaMGRLPSTYRKCYMLDFGLAR 181
Cdd:cd14083     80 MELvTGGELFD--RIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENL-LYYSPDEDSKIMISDFGLSK 152
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
32-238 5.52e-12

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: 67.66  E-value: 5.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd14002      1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFipKRGKSEKELrnLRQEIEILRKLN-HPNIIEMLDSFETKKEFVVVT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QL-QG---RNLADlrrsqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGLARQY 183
Cdd:cd14002     80 EYaQGelfQILED------DGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGK----GGVVKLCDFGFARAM 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  184 TNTTGDVRpprnvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd14002    150 SCNTLVLT------SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPP 198
K-ycf53 COG5752
Signaling protein combining a Ser/Thr protein kinase domain and the GUN4/Ycf53 ...
31-239 5.55e-12

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


Pssm-ID: 444462 [Multi-domain]  Cd Length: 466  Bit Score: 69.65  E-value: 5.55e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMD--LLTRENVALK--------VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNE 100
Cdd:COG5752     31 KERYRAIKPLGQGGFGRTFLAVDedIPSHPHCVIKqfyfpeqgPSSFQKAVELFRQEAVRLDELGKHPQIPELLAYFEQD 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQL-QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFaMGRlpSTYRKCYMLDFGL 179
Cdd:COG5752    111 QRLYLVQEFiEGQTLAQ--ELEKKGVFSESQIWQLLKDLLPVLQFIHSRNVIHRDIKPANI-IRR--RSDGKLVLIDFGV 185
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  180 ARQYTNT----TGDV------RPPRNVagfRGTVRYASvnahknremgrhdDLWSLFYMLVEFAVGQLPW 239
Cdd:COG5752    186 AKLLTITallqTGTIigtpeyMAPEQL---RGKVFPAS-------------DLYSLGVTCIYLLTGVSPF 239
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
40-198 5.71e-12

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 67.52  E-value: 5.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIG-CGRNEKFNYVVMQLQGRNLADLR 118
Cdd:cd14065      1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLKEVKLMRRLS-HPNILRFIGvCVKDNKLNFITEYVNGGTLEELL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  119 RSqPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNfAMGRLPSTYRKCYMLDFGLARQ---YTNTTGDVRPPRN 195
Cdd:cd14065     80 KS-MDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKN-CLVREANRGRNAVVADFGLAREmpdEKTKKPDRKKRLT 157

                   ...
gi 1034651883  196 VAG 198
Cdd:cd14065    158 VVG 160
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
34-239 5.91e-12

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: 67.85  E-value: 5.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAM----DLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKDHVcRFIGCGRNEKFNYVV 106
Cdd:cd06631      3 WKKGNVLGKGAYGTVYCGLtstgQLIAVKQVELDTsdkEKAEKEYEKLQEEVDLLKTLKHVNIV-GYLGTCLEDNVVSIF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQ-LQGRNLAD-LRR--SQPRGTFTLSTtlrlgKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKcyMLDFGLARQ 182
Cdd:cd06631     82 MEfVPGGSIASiLARfgALEEPVFCRYT-----KQILEGVAYLHNNNVIHRDIKGNNIML--MPNGVIK--LIDFGCAKR 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  183 YTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06631    153 LCINLSSGSQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPW 209
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
34-186 6.35e-12

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


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 68.07  E-value: 6.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQGKDH--------VCRFIGCGRNE 100
Cdd:cd07838      1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKkvrVPLSEEgiPLSTIR-EIALLKQLESFEHpnvvrlldVCHGPRTDREL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFnYVVMQLQGRNLAD-LRRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGL 179
Cdd:cd07838     80 KL-TLVFEHVDQDLATyLDKCPKPG-LPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNI----LVTSDGQVKLADFGL 153

                   ....*..
gi 1034651883  180 ARQYTNT 186
Cdd:cd07838    154 ARIYSFE 160
PK_VRK3 cd14124
Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to ...
86-289 7.06e-12

Pseudokinase domain of Vaccinia Related Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. VRKs were initially discovered due to its similarity to vaccinia virus B1R STK, which is important for viral replication. They play important roles in cell signaling, nuclear envelope dynamics, apoptosis, and stress responses. Vertebrates contain three VRK proteins. VRK3 is an inactive pseudokinase that is unable to bind ATP. It achieves its regulatory function through protein-protein interactions. It negatively regulates ERK signaling by binding directly and enhancing the activity of the MAPK phosphatase VHR (vaccinia H1-related), which dephosphorylates and inactivates ERK. The VRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271026 [Multi-domain]  Cd Length: 298  Bit Score: 67.95  E-value: 7.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   86 GKDHVCRFIG---C---GRNEKFNYVVMQLQGRNLADLRrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN 159
Cdd:cd14124     74 KKLHSTDLLGipsCvgfGVHDSYRFLVFPSLGQSLQSAL-DEGKGVLSEKAVLQLACRLLDALEFIHENEYVHGDITAEN 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  160 FAMGrlPSTYRKCYMLDFGLARQYTNTTGDVRpprNVAGFR----GTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVG 235
Cdd:cd14124    153 IFVD--PEDQSEVYLAGYGFAFRYCPGGKHVE---YREGSRspheGDIEFISLDSHKGAGPSRRSDLQSLGYCMLKWLTG 227
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  236 QLPWRKIK-DKEQVGMIKEKY--------EHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLI 289
Cdd:cd14124    228 SLPWSNLLhNTEDIMKQKERFmddvpgflGPCFHQKKVSEALQKYLKVVMALQYEEKPDYAML 290
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
29-295 7.77e-12

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: 67.37  E-value: 7.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAMdLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd05072      4 IPRESIKLVKKLGAGQFGEVWMGY-YNNSTKVAVKtLKPGTMSVQAFLEEANLMKTLQ-HDKLVRLYAVVTKEEPIYIIT 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGR-NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR----- 181
Cdd:cd05072     82 EYMAKgSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANV----LVSESLMCKIADFGLARviedn 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  182 QYTNTTGDVRPprnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVEFAV-GQLPWRKIKDKEQVGMIKEKYehRM- 259
Cdd:cd05072    158 EYTAREGAKFP----------IKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGY--RMp 225
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1034651883  260 LLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd05072    226 RMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDD 261
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
32-183 9.31e-12

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: 67.63  E-value: 9.31e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQGKDHV-CRFIGCGRNEKFNYV 105
Cdd:cd07843      5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKklkMEKEKEgfPITSLR-EINILLKLQHPNIVtVKEVVVGSNLDKIYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQGRNLADL--RRSQPrgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLpstyRKCymlDFGLA 180
Cdd:cd07843     84 VMEYVEHDLKSLmeTMKQP---FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLnnrGIL----KIC---DFGLA 153

                   ...
gi 1034651883  181 RQY 183
Cdd:cd07843    154 REY 156
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
33-182 9.78e-12

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: 67.94  E-value: 9.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKD--HVCRFIGCGRNEKFN-- 103
Cdd:cd07834      1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKkisnvFDDLIDAKRILR-EIKILRHLKHENiiGLLDILRPPSPEEFNdv 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQLQGRNLADLRRSQPRGT------FTLsttlrlgkQILESIEAIHSVGFLHRDIKPSNFAmgrlpsTYRKCYM--L 175
Cdd:cd07834     80 YIVTELMETDLHKVIKSPQPLTddhiqyFLY--------QILRGLKYLHSAGVIHRDLKPSNIL------VNSNCDLkiC 145

                   ....*..
gi 1034651883  176 DFGLARQ 182
Cdd:cd07834    146 DFGLARG 152
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
40-254 9.94e-12

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: 66.77  E-value: 9.94e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVL--KMEVAVLKKLQgkdhvCRFIGCGR-----NEKFnYVVMQ- 108
Cdd:cd05123      1 LGKGSFGKVLLVRKKDTGKLYAMKVlrkKEIIKRKEVEhtLNERNILERVN-----HPFIVKLHyafqtEEKL-YLVLDy 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTyrkcymlDFGLAR---- 181
Cdd:cd05123     75 VPGGELFS--HLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENIlldSDGHIKLT-------DFGLAKelss 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  182 --QYTNTtgdvrpprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEK 254
Cdd:cd05123    146 dgDRTYT------------FCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKS 208
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
33-184 1.07e-11

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 67.29  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKM----EVAVLKKLQGKDH--------VCRFIGCGRNE 100
Cdd:cd07863      1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLstvrEVALLKRLEAFDHpnivrlmdVCATSRTDRET 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQLQGRNLADLRRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLA 180
Cdd:cd07863     81 KVTLVFEHVDQDLRTYLDKVPPPG-LPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENI----LVTSGGQVKLADFGLA 155

                   ....
gi 1034651883  181 RQYT 184
Cdd:cd07863    156 RIYS 159
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
30-182 1.08e-11

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: 68.05  E-value: 1.08e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCR---FIGCGRNEK 101
Cdd:cd07880     13 VPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKklyrpFQSELFAKRAYR-ELRLLKHMKHENVIGLldvFTPDLSLDR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FN--YVVMQLQGRNLADL----RRSQPRGTFtlsttlrLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKCYM- 174
Cdd:cd07880     92 FHdfYLVMPFMGTDLGKLmkheKLSEDRIQF-------LVYQMLKGLKYIHAAGIIHRDLKPGNLAVN------EDCELk 158

                   ....*....
gi 1034651883  175 -LDFGLARQ 182
Cdd:cd07880    159 iLDFGLARQ 167
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
33-239 1.09e-11

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: 66.73  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK------VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd14098      1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKqivkrkVAGNDKNLQLFQREINILKSLE-HPGIVRLIDWYEDDQHIYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQL-QGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLAR-QYT 184
Cdd:cd14098     80 MEYvEGGDLMDFIMAW--GAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVK--ISDFGLAKvIHT 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  185 NTTgdvrpprnVAGFRGTVRYAS---VNAHKNREMGRHD---DLWSLFYMLVEFAVGQLPW 239
Cdd:cd14098    156 GTF--------LVTFCGTMAYLApeiLMSKEQNLQGGYSnlvDMWSVGCLVYVMLTGALPF 208
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
38-240 1.70e-11

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: 66.99  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQL-QGRNLad 116
Cdd:cd14179     13 KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQR-EIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELlKGGEL-- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  117 LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRKCYMLDFGLARqytnttgdVRPPRN- 195
Cdd:cd14179     90 LERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTD-ESDNSEIKIIDFGFAR--------LKPPDNq 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034651883  196 ---VAGFrgTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:cd14179    161 plkTPCF--TLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQ 206
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
33-189 2.26e-11

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


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 66.02  E-value: 2.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL-Q 110
Cdd:cd14087      2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKmIETKCRGREVCESELNVLRRVR-HTNIIQLIEVFETKERVYMVMELaT 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  111 GRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRKCYMLDFGLArqYTNTTGD 189
Cdd:cd14087     81 GGELFD--RIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYH-PGPDSKIMITDFGLA--STRKKGP 154
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
38-281 3.17e-11

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: 65.33  E-value: 3.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKM--EVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd14189      7 RLLGKGGFARCYEMTDLATNKTYAVKViphSRVAKPHQREKIvnEIELHRDLHHK-HVVKFSHHFEDAENIYIFLELCSR 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 -NLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGLARQYTNttgdvr 191
Cdd:cd14189     86 kSLAHIWKA--RHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFI----NENMELKVGDFGLAARLEP------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  192 PPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKE-KY----------EHRM- 259
Cdd:cd14189    154 PEQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQvKYtlpaslslpaRHLLa 233
                          250       260
                   ....*....|....*....|...
gi 1034651883  260 -LLKHMPSEfHLFLDHIASLDYF 281
Cdd:cd14189    234 gILKRNPGD-RLTLDQILEHEFF 255
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
40-182 3.32e-11

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: 65.36  E-value: 3.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPKQV------LKMEVAVLKKLQGKdHVCRFIGCGRNE---KFnYVVMQLQ 110
Cdd:cd14119      1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIpngeanVKREIQILRRLNHR-NVIKLVDVLYNEekqKL-YMVMEYC 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  111 GRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyrkcymlDFGLARQ 182
Cdd:cd14119     79 VGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLttdGTLKIS-------DFGVAEA 146
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
32-187 4.47e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.13  E-value: 4.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKME--------------VAVLKklQGKDHVCrfi 94
Cdd:NF033483     7 GRYEIGERIGRGGMAEVYLAKDTRLDRDVAVKVlrpDLARDPEFVARFRreaqsaaslshpniVSVYD--VGEDGGI--- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   95 gcgrnekfNYVVMQL-QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyr 170
Cdd:NF033483    82 --------PYIVMEYvDGRTLKDYIRE--HGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILItkdGRVKVT-- 149
                          170
                   ....*....|....*..
gi 1034651883  171 kcymlDFGLARQYTNTT 187
Cdd:NF033483   150 -----DFGIARALSSTT 161
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
35-253 5.26e-11

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: 64.42  E-value: 5.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKV------ESAQQPKQvLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14007      3 EIGKPLGKGKFGNVYLAREKKSGFIVALKVisksqlQKSGLEHQ-LRREIEIQSHLRHP-NILRLYGYFEDKKRIYLILE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGR-NLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTt 187
Cdd:cd14007     81 YAPNgELYKELKKQKR--FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENI----LLGSNGELKLADFGWSVHAPSN- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  188 gdvrpPRNVagFRGTVRYASvnahknREM---GRHD---DLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKE 253
Cdd:cd14007    154 -----RRKT--FCGTLDYLP------PEMvegKEYDykvDIWSLGVLCYELLVGKPPFESKSHQETYKRIQN 212
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
34-239 5.84e-11

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: 64.76  E-value: 5.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPK--------QVLKMEVAVLKKLQgKDHVCRFIGCGRNE-KFNY 104
Cdd:cd06630      2 WLKGPLLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSsseqeevvEAIREEIRMMARLN-HPNIVRMLGATQHKsHFNI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQLQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpSTYRKCYMLDFGLA-RQY 183
Cdd:cd06630     81 FVEWMAGGSVASLLSKY--GAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVD---STGQRLRIADFGAAaRLA 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  184 TNTTGdvrpprnvAG-----FRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06630    156 SKGTG--------AGefqgqLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPW 208
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
32-183 8.27e-11

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 64.84  E-value: 8.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ-----PKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:PLN00009     2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQedegvPSTAIR-EISLLKEMQ-HGNIVRLQDVVHSEKRLYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLADLRRSQPrgtfTLSTTLRLGK----QILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRkcyMLDFGLARQ 182
Cdd:PLN00009    80 FEYLDLDLKKHMDSSP----DFAKNPRLIKtylyQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNALK---LADFGLARA 152

                   .
gi 1034651883  183 Y 183
Cdd:PLN00009   153 F 153
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
34-180 8.45e-11

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 64.96  E-value: 8.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQP--KQVLkMEVAVLKKL------QGKDHVCR----FIGCGRnek 101
Cdd:cd14212      1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVLKNKPAyfRQAM-LEIAILTLLntkydpEDKHHIVRlldhFMHHGH--- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 fNYVVMQLQGRNLADL-RRSQPRGtftLSTTL--RLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFG 178
Cdd:cd14212     77 -LCIVFELLGVNLYELlKQNQFRG---LSLQLirKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPEIK--LIDFG 150

                   ..
gi 1034651883  179 LA 180
Cdd:cd14212    151 SA 152
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
37-183 1.01e-10

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: 64.45  E-value: 1.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVMQLQG 111
Cdd:cd07860      5 VEKIGEGTYGVVYKARNKLTGEVVALKkirldTETEGVPSTAIR-EISLLKELNHPN-IVKLLDVIHTENKLYLVFEFLH 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  112 RNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQY 183
Cdd:cd07860     83 QDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNL----LINTEGAIKLADFGLARAF 150
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
34-272 1.02e-10

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: 64.03  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPK---QVLKMEVAVLKKLQGKD--HVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd06917      3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDddvSDIQKEVALLSQLKLGQpkNIIKYYGSYLKGPSLWIIMD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTT 187
Cdd:cd06917     83 YcEGGSIRTLMRAGPIAERYIAVIMR---EVLVALKFIHKDGIIHRDIKAANI----LVTNTGNVKLCDFGVAASLNQNS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 gdvrppRNVAGFRGTVRY-ASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPS 266
Cdd:cd06917    156 ------SKRSTFVGTPYWmAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSKPPRLEGNGYSP 229

                   ....*.
gi 1034651883  267 EFHLFL 272
Cdd:cd06917    230 LLKEFV 235
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
30-185 1.02e-10

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 64.24  E-value: 1.02e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd14166      1 IRETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCikKSPLSRDSSLENEIAVLKRIK-HENIVTLEDIYESTTHYYLVM 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  108 QL-QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFaMGRLPSTYRKCYMLDFGLARQYTN 185
Cdd:cd14166     80 QLvSGGELFD--RILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENL-LYLTPDENSKIMITDFGLSKMEQN 155
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
32-195 1.04e-10

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: 64.44  E-value: 1.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKM----EVAVLKKLQGKDHVC------------RFig 95
Cdd:cd07864      7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPItairEIKILRQLNHRSVVNlkeivtdkqdalDF-- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   96 cgRNEKFN-YVVMQLQGRNLADLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYM 174
Cdd:cd07864     85 --KKDKGAfYLVFEYMDHDLMGLLESG-LVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILL----NNKGQIKL 157
                          170       180
                   ....*....|....*....|.
gi 1034651883  175 LDFGLARQYTNTtgDVRPPRN 195
Cdd:cd07864    158 ADFGLARLYNSE--ESRPYTN 176
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
34-162 1.06e-10

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: 64.12  E-value: 1.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV------ESAQQpkQVLKmEVAVLKKLqgkDH--VCRFIGC--------- 96
Cdd:cd14048      8 FEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRirlpnnELARE--KVLR-EVRALAKL---DHpgIVRYFNAwlerppegw 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883   97 --GRNEKFNYVVMQL-QGRNLAD-LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN--FAM 162
Cdd:cd14048     82 qeKMDEVYLYIQMQLcRKENLKDwMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNvfFSL 153
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
31-239 1.11e-10

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: 63.79  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKM-EVAVLKKLQGKDHVCRFIGCGRNEKFnYVVMQ 108
Cdd:cd06647      6 KKKYTRFEKIGQGASGTVYTAIDVATGQEVAIKqMNLQQQPKKELIInEILVMRENKNPNIVNYLDSYLVGDEL-WVVME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 -LQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLARQYTntt 187
Cdd:cd06647     85 yLAGGSLTDVVTETCMDEGQIAAVCR---ECLQALEFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGFCAQIT--- 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  188 gdvrPPRNV-AGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06647    155 ----PEQSKrSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 203
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
38-269 1.42e-10

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: 63.33  E-value: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAM---DLLTRENVALKV----ESAQQPKQVLKmEVAVLKKLqGKDHVCRFIGCGRNEKFNYVVMQL- 109
Cdd:cd00192      1 KKLGEGAFGEVYKGKlkgGDGKTVDVAVKTlkedASESERKDFLK-EARVMKKL-GHPNVVRLLGVCTEEEPLYLVMEYm 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QG------RNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQ 182
Cdd:cd00192     79 eGGdlldflRKSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNC----LVGEDLVVKISDFGLSRD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  183 ------YTNTTGDVRPprnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKY 255
Cdd:cd00192    155 iydddyYRKKTGGKLP----------IRWMAPESLKDGIFTSKSDVWSFGVLLWEiFTLGATPYPGLSNEEVLEYLRKGY 224
                          250
                   ....*....|....*
gi 1034651883  256 ehRMLL-KHMPSEFH 269
Cdd:cd00192    225 --RLPKpENCPDELY 237
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
34-275 1.55e-10

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


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 63.56  E-value: 1.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDL-----LTRENVALKVESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRN--EKFNY 104
Cdd:cd06651      9 WRRGKLLGQGAFGRVYLCYDVdtgreLAAKQVQFDPESPETSKEVsaLECEIQLLKNLQ-HERIVQYYGCLRDraEKTLT 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQ-LQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQY 183
Cdd:cd06651     88 IFMEyMPGGSVKDQLKAY--GALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANI----LRDSAGNVKLGDFGASKRL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  184 TNTTGDVRPPRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKH 263
Cdd:cd06651    162 QTICMSGTGIRSVT---GTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSH 238
                          250
                   ....*....|..
gi 1034651883  264 MPSEFHLFLDHI 275
Cdd:cd06651    239 ISEHARDFLGCI 250
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
34-269 1.70e-10

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


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 63.04  E-value: 1.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLK--MEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14081      3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIvnkEKLSKESVLMKveREIAIMKLIE-HPNVLKLYDVYENKKYLYLVLE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 -LQGRNLAD-LRRsqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARqytnt 186
Cdd:cd14081     82 yVSGGELFDyLVK---KGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENL----LLDEKNNIKIADFGMAS----- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  187 tgdVRPPRNVA-GFRGTVRYAS--VNAHKNREmGRHDDLWSLFYMLVEFAVGQLPWrkikDKEQVGMIKEKYEHRMLlkH 263
Cdd:cd14081    150 ---LQPEGSLLeTSCGSPHYACpeVIKGEKYD-GRKADIWSCGVILYALLVGALPF----DDDNLRQLLEKVKRGVF--H 219

                   ....*.
gi 1034651883  264 MPSEFH 269
Cdd:cd14081    220 IPHFIS 225
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
30-256 1.84e-10

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: 63.12  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQV-LKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd14167      1 IRDIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCiaKKALEGKETsIENEIAVLHKIK-HPNIVALDDIYESGGHLYLI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQL-QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyRKCYMLDFGLARqyTN 185
Cdd:cd14167     80 MQLvSGGELFD--RIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYSLDED-SKIMISDFGLSK--IE 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  186 TTGDVrpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDK---EQVgmIKEKYE 256
Cdd:cd14167    155 GSGSV-----MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAklfEQI--LKAEYE 221
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
34-231 2.03e-10

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: 63.28  E-value: 2.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKqvLKMEVAVLKKLqgkDH--VCRFIGC--------------- 96
Cdd:cd14047      8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEK--AEREVKALAKL---DHpnIVRYNGCwdgfdydpetsssns 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   97 -GRNEKFNYVVMQL--QG--RNLADLRRSQPRGTFTlstTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRK 171
Cdd:cd14047     83 sRSKTKCLFIQMEFceKGtlESWIEKRNGEKLDKVL---ALEIFEQITKGVEYIHSKKLIHRDLKPSNI----FLVDTGK 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  172 CYMLDFGLArqyTNTTGDVRPPRNvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE 231
Cdd:cd14047    156 VKIGDFGLV---TSLKNDGKRTKS----KGTLSYMSPEQISSQDYGKEVDIYALGLILFE 208
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
37-231 2.15e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 63.30  E-value: 2.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQpKQVLKM--EVAVLKKLQGK----------DHVCRFIgcgrnek 101
Cdd:cd14049     11 IARLGKGGYGKVYKVRNKLDGQYYAIKkilIKKVTK-RDCMKVlrEVKVLAGLQHPnivgyhtawmEHVQLML------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 fnYVVMQLQGRNLADL-----RRSQPRGTFT-------LSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTY 169
Cdd:cd14049     83 --YIQMQLCELSLWDWivernKRPCEEEFKSapytpvdVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIF---LHGSD 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  170 RKCYMLDFGLA--------RQYTNTTGdVRPPRNVAGFrGTVRYASVNAHKNREMGRHDDLWSLFYMLVE 231
Cdd:cd14049    158 IHVRIGDFGLAcpdilqdgNDSTTMSR-LNGLTHTSGV-GTCLYAAPEQLEGSHYDFKSDMYSIGVILLE 225
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
28-183 2.20e-10

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 63.92  E-value: 2.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   28 YVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESA----QQPKQVLKmEVAVLKKLQGKDHVC-----RFIGCG 97
Cdd:cd07855      1 FDVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKkIPNAfdvvTTAKRTLR-ELKILRHFKHDNIIAirdilRPKVPY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   98 RNEKFNYVVMQLQGRNLADLRRS-QPrgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN-------------FAMG 163
Cdd:cd07855     80 ADFKDVYVVLDLMESDLHHIIHSdQP---LTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNllvnencelkigdFGMA 156
                          170       180
                   ....*....|....*....|...
gi 1034651883  164 RLPSTY---RKCYMLDFGLARQY 183
Cdd:cd07855    157 RGLCTSpeeHKYFMTEYVATRWY 179
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
30-159 2.29e-10

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: 63.29  E-value: 2.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKveSAQQPKQVLKMEVAVLKKLqgkDH--VCRFI------GCGRNEK 101
Cdd:cd14137      2 VEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIK--KVLQDKRYKNRELQIMRRL---KHpnIVKLKyffyssGEKKDEV 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FNYVVMQLQGRNLADLRRSQPRGTFTLSTTL-RL-GKQILESIEAIHSVGFLHRDIKPSN 159
Cdd:cd14137     77 YLNLVMEYMPETLYRVIRHYSKNKQTIPIIYvKLySYQLFRGLAYLHSLGICHRDIKPQN 136
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
40-238 2.71e-10

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: 62.62  E-value: 2.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQ------QPKQVLKmEVAVLKKLQGkDHVCRFIGCGRNEKFNYVVMQ-LQGR 112
Cdd:cd05579      1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRdmirknQVDSVLA-ERNILSQAQN-PFVVKLYYSFQGKKNLYLVMEyLPGG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTyrkcymlDFGLAR-------- 181
Cdd:cd05579     79 DLYSLLENV--GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNIlidANGHLKLT-------DFGLSKvglvrrqi 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  182 -QYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd05579    150 kLSIQKKSNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPP 207
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
33-251 2.86e-10

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: 62.78  E-value: 2.86e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VE----SAQQPKQVLKMEVAVLKK----LQGKDH--VCRFIGCGRNEK 101
Cdd:cd06629      2 KWVKGELIGKGTYGRVYLAMNATTGEMLAVKqVElpktSSDRADSRQKTVVDALKSeidtLKDLDHpnIVQYLGFEETED 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 F-----NYV----VMQLqgrnladLRRsqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKC 172
Cdd:cd06629     82 YfsiflEYVpggsIGSC-------LRK---YGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNI----LVDLEGIC 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  173 YMLDFGLARQYTNTTGdvrpprNVAG--FRGTVRYASVNAHKNREMGRHD--DLWSLFYMLVEFAVGQLPWrkiKDKEQV 248
Cdd:cd06629    148 KISDFGISKKSDDIYG------NNGAtsMQGSVFWMAPEVIHSQGQGYSAkvDIWSLGCVVLEMLAGRRPW---SDDEAI 218

                   ...
gi 1034651883  249 GMI 251
Cdd:cd06629    219 AAM 221
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
38-256 3.65e-10

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: 62.60  E-value: 3.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQ-VLKMEVAVLKKLQGKDHVcrfigcGRNEKFN-----YVVMQL 109
Cdd:cd14169      9 EKLGEGAFSEVVLAQERGSQRLVALKCipKKALRGKEaMVENEIAVLRRINHENIV------SLEDIYEspthlYLAMEL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFaMGRLPSTYRKCYMLDFGLARqytnttg 188
Cdd:cd14169     83 vTGGELFD--RIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENL-LYATPFEDSKIMISDFGLSK------- 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  189 dVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMI-KEKYE 256
Cdd:cd14169    153 -IEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQIlKAEYE 220
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
36-254 3.80e-10

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: 62.28  E-value: 3.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL-QGRNL 114
Cdd:cd06612      7 ILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEIIKEISILKQCD-SPYIVKYYGSYFKNTDLWIVMEYcGAGSV 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADLRRSQPRgTFT---LSTTLrlgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTGDvr 191
Cdd:cd06612     86 SDIMKITNK-TLTeeeIAAIL---YQTLKGLEYLHSNKKIHRDIKAGNI----LLNEEGQAKLADFGVSGQLTDTMAK-- 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  192 ppRNVagFRGTVRYAS--VNAHKNremgrHD---DLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEK 254
Cdd:cd06612    156 --RNT--VIGTPFWMApeVIQEIG-----YNnkaDIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNK 214
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
34-239 4.36e-10

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: 61.97  E-value: 4.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALK------VESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd08228      4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKkvqifeMMDAKARQDCVK-EIDLLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRR--SQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGLARQYTN 185
Cdd:cd08228     83 LADAGDLSQMIKyfKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI----TATGVVKLGDLGLGRFFSS 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  186 TTGDVRpprnvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd08228    159 KTTAAH------SLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF 206
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
32-230 4.42e-10

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: 62.03  E-value: 4.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ----------PKQVLKMEVAVLKKLqgkDHVC-----RFIgc 96
Cdd:cd14084      6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrreinKPRNIETEIEILKKL---SHPCiikieDFF-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   97 gRNEKFNYVVMQL-QGRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTYRKCYM- 174
Cdd:cd14084     81 -DAEDDYYIVLELmEGGELFDRVVSNKR--LKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVL---LSSQEEECLIk 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  175 -LDFGLARqytnTTGDVRPPRNVAgfrGTVRYAS---VNAHKNREMGRHDDLWSL----FYMLV 230
Cdd:cd14084    155 iTDFGLSK----ILGETSLMKTLC---GTPTYLApevLRSFGTEGYTRAVDCWSLgvilFICLS 211
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
33-195 7.78e-10

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: 61.82  E-value: 7.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKM----EVAVLKKLQgKDHVCRFIGCGRNEKFNYV 105
Cdd:cd07841      1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKkikLGERKEAKDGINFtalrEIKLLQELK-HPNIIGLLDVFGHKSNINL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQGRNLADLRRSqPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTyrkcymlDFGLARQ 182
Cdd:cd07841     80 VFEFMETDLEKVIKD-KSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLliaSDGVLKLA-------DFGLARS 151
                          170
                   ....*....|...
gi 1034651883  183 YTNttgdvrPPRN 195
Cdd:cd07841    152 FGS------PNRK 158
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
37-192 8.09e-10

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: 62.00  E-value: 8.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKM----EVAVLKKLQGKDHV-CRFIGCGRNEKFNYVVMQLQG 111
Cdd:cd07845     12 LNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGIPIsslrEITLLLNLRHPNIVeLKEVVVGKHLDSIFLVMEYCE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpsTYRKCYML-DFGLARQYTNTTGDV 190
Cdd:cd07845     92 QDLASLLDNMPT-PFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLL-----TDKGCLKIaDFGLARTYGLPAKPM 165

                   ..
gi 1034651883  191 RP 192
Cdd:cd07845    166 TP 167
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
40-253 8.33e-10

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: 61.10  E-value: 8.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQ---QPKQVLKM--EVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL-QGRN 113
Cdd:cd14187     15 LGKGGFAKCYEITDADTKEVFAGKIVPKSlllKPHQKEKMsmEIAIHRSLAHQ-HVVGFHGFFEDNDFVYVVLELcRRRS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 LADL--RR---SQPRGTFTLsttlrlgKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGLArqyTNTTG 188
Cdd:cd14187     94 LLELhkRRkalTEPEARYYL-------RQIILGCQYLHRNRVIHRDLKLGNLFL----NDDMEVKIGDFGLA---TKVEY 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  189 DVRPPRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKE 253
Cdd:cd14187    160 DGERKKTLC---GTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKK 221
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
35-238 1.04e-09

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 61.07  E-value: 1.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQvLKMEVAVLKKlQGKDHVCRFIGCGRNEKFNYVVMQL- 109
Cdd:cd06623      4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKihvdGDEEFRKQ-LLRELKTLRS-CESPYVVKCYGAFYKEGEISIVLEYm 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSV-GFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTG 188
Cdd:cd06623     82 DGGSLADLLKKV--GKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNL----LINSKGEVKIADFGISKVLENTLD 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034651883  189 dvrpprNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06623    156 ------QCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFP 199
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
33-180 1.17e-09

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: 60.80  E-value: 1.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLqgkDH--VCRFIgcgrnEKFN---- 103
Cdd:cd14095      1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIidkAKCKGKEHMIENEVAILRRV---KHpnIVQLI-----EEYDtdte 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 -YVVMQL-QGRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPStYRKCYML-DFGLA 180
Cdd:cd14095     73 lYLVMELvKGGDLFDAITSSTK--FTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHED-GSKSLKLaDFGLA 149
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
31-239 1.25e-09

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: 61.28  E-value: 1.25e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ- 108
Cdd:cd06654     19 KKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRqMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEy 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLARQYTNTTG 188
Cdd:cd06654     99 LAGGSLTDVVTETCMDEGQIAAVCR---ECLQALEFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGFCAQITPEQS 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  189 dvrpprNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06654    172 ------KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPY 216
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
77-254 1.33e-09

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: 61.16  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   77 EVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ-LQGRNLadLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDI 155
Cdd:cd14092     48 EVQLLRLCQGHPNIVKLHEVFQDELHTYLVMElLRGGEL--LERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  156 KPSN--FAMGRLPSTYRkcyMLDFGLARqytnttgdVRP---PRNVAGFrgTVRYAS--VNAHKNREMGRHD--DLWSLF 226
Cdd:cd14092    126 KPENllFTDEDDDAEIK---IVDFGFAR--------LKPenqPLKTPCF--TLPYAApeVLKQALSTQGYDEscDLWSLG 192
                          170       180
                   ....*....|....*....|....*...
gi 1034651883  227 YMLVEFAVGQLPWRKIKDKEQVGMIKEK 254
Cdd:cd14092    193 VILYTMLSGQVPFQSPSRNESAAEIMKR 220
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
30-190 1.35e-09

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: 61.43  E-value: 1.35e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK--VESAQQPKQVLKM--EVAVLKKLQGKDHVCR---FIGCGRNEkf 102
Cdd:cd07856      8 ITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKkiMKPFSTPVLAKRTyrELKLLKHLRHENIISLsdiFISPLEDI-- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 nYVVMQLQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKC--YMLDFGLA 180
Cdd:cd07856     86 -YFVTELLGTDLHRLLTSRPLEKQFIQYFLY---QILRGLKYVHSAGVIHRDLKPSNILVN------ENCdlKICDFGLA 155
                          170
                   ....*....|.
gi 1034651883  181 R-QYTNTTGDV 190
Cdd:cd07856    156 RiQDPQMTGYV 166
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
12-235 1.47e-09

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 61.98  E-value: 1.47e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   12 TNMSGGGEQADILPA--NYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKvESAQQPkQVLKMEVAVLKKLQG--- 86
Cdd:PTZ00036    44 NNAGEDEDEEKMIDNdiNRSPNKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIK-KVLQDP-QYKNRELLIMKNLNHini 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   87 ---KDHVcrFIGCGR-NEK--FNYVVMQLQGRNLADLRRSQPRGTFTLSTTL-RL-GKQILESIEAIHSVGFLHRDIKPS 158
Cdd:PTZ00036   122 iflKDYY--YTECFKkNEKniFLNVVMEFIPQTVHKYMKHYARNNHALPLFLvKLySYQLCRALAYIHSKFICHRDLKPQ 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  159 NFAMGRLPSTYRKCymlDFGLArqytnttgdvrppRNVAGFRGTVRYASVNAHKNREM-------GRHDDLWSLFYMLVE 231
Cdd:PTZ00036   200 NLLIDPNTHTLKLC---DFGSA-------------KNLLAGQRSVSYICSRFYRAPELmlgatnyTTHIDLWSLGCIIAE 263

                   ....
gi 1034651883  232 FAVG 235
Cdd:PTZ00036   264 MILG 267
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
32-240 1.74e-09

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: 60.53  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQP---KQV--LKMEVAVLKKLQgkdH--VCRFIGCGRNEKFNY 104
Cdd:cd05612      1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVirlKQEqhVHNEKRVLKEVS---HpfIIRLFWTEHDQRFLY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQ-LQGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLARQY 183
Cdd:cd05612     78 MLMEyVPGGELFSYLRN--SGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDK--EGHIK--LTDFGFAKKL 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  184 TNTTGDVrpprnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:cd05612    152 RDRTWTL---------CGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFF 199
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
43-241 1.80e-09

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 60.02  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   43 GGFGEIYEAMDLLTRENVALKVESAQQPKQVlkmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQLQ--GRNLADLRRS 120
Cdd:cd13995     15 GAFGKVYLAQDTKTKKRMACKLIPVEQFKPS---DVEIQACFR-HENIAELYGALLWEETVHLFMEAGegGSVLEKLESC 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  121 QPRGTFTLsttLRLGKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTyrKCYMLDFGLARQYTNttgDVRPPRNVagfR 200
Cdd:cd13995     91 GPMREFEI---IWVTKHVLKGLDFLHSKNIIHHDIKPSNIV---FMST--KAVLVDFGLSVQMTE---DVYVPKDL---R 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1034651883  201 GTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRK 241
Cdd:cd13995    157 GTEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVR 197
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
40-200 1.85e-09

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 59.97  E-value: 1.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMdlLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCrFIGCGRNEKFnyVVMQLQGRNLADLRR 119
Cdd:cd14068      2 LGDGGFGSVYRAV--YRGEDVAVKIFNKHTSFRLLRQELVVLSHLHHPSLVA-LLAAGTAPRM--LVMELAPKGSLDALL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  120 SQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLpstYRKCYML----DFGLArQYTNTTGdVRPPRN 195
Cdd:cd14068     77 QQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTL---YPNCAIIakiaDYGIA-QYCCRMG-IKTSEG 151

                   ....*
gi 1034651883  196 VAGFR 200
Cdd:cd14068    152 TPGFR 156
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
30-256 1.88e-09

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 60.36  E-value: 1.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLK-KIGGGGFGEIY--EAMDLLTREN---VALKV--ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIG-CGRNE 100
Cdd:cd05092      2 IKRRDIVLKwELGEGAFGKVFlaECHNLLPEQDkmlVAVKAlkEATESARQDFQREAELLTVLQ-HQHIVRFYGvCTEGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQLQGRNLADLRRS-------------QPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlps 167
Cdd:cd05092     81 PLIMVFEYMRHGDLNRFLRShgpdakildggegQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQ--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  168 tYRKCYMLDFGLAR-----QYTNTTGDVRPPrnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRK 241
Cdd:cd05092    158 -GLVVKIGDFGMSRdiystDYYRVGGRTMLP---------IRWMPPESILYRKFTTESDIWSFGVVLWEiFTYGKQPWYQ 227
                          250
                   ....*....|....*
gi 1034651883  242 IKDKEQVGMIKEKYE 256
Cdd:cd05092    228 LSNTEAIECITQGRE 242
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
35-259 2.52e-09

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: 59.67  E-value: 2.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAmdLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQGKDHVCrFIGCGRNEKFNYVVMQLQGR- 112
Cdd:cd05039      9 KLGELIGKGEFGDVMLG--DYRGQKVAVKClKDDSTAAQAFLAEASVMTTLRHPNLVQ-LLGVVLEGNGLYIVTEYMAKg 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTnttgdvrp 192
Cdd:cd05039     86 SLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNV----LVSEDNVAKVSDFGLAKEAS-------- 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  193 pRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKYehRM 259
Cdd:cd05039    154 -SNQDGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEiYSFGRVPYPRIPLKDVVPHVEKGY--RM 218
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
31-259 2.59e-09

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 59.76  E-value: 2.59e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMdLLTRENVALKV-ESAQQPKQ-VLKMEVAVLKKLQGKDHVCRFIGCGRNEKFnYVVMQ 108
Cdd:cd05148      5 REEFTLERKLGSGYFGEVWEGL-WKNRVRVAIKIlKSDDLLKQqDFQKEVQALKRLRHKHLISLFAVCSVGEPV-YIITE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L--QGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPStyrkCYMLDFGLARQYTN- 185
Cdd:cd05148     83 LmeKGSLLAFLRSPEGQ-VLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLV----CKVADFGLARLIKEd 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  186 --TTGDVRPPrnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKYehRM 259
Cdd:cd05148    158 vyLSSDKKIP---------YKWTAPEAASHGTFSTKSDVWSFGILLYEmFTYGQVPYPGMNNHEVYDQITAGY--RM 223
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
34-159 2.67e-09

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: 59.98  E-value: 2.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALK--VESAQQPKQVLKM-EVAVLKKLQGKDHVCRFIGCGRNEKFNYV--VMQ 108
Cdd:cd07831      1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKcmKKHFKSLEQVNNLrEIQALRRLSPHPNILRLIEVLFDRKTGRLalVFE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  109 LQGRNLADLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN 159
Cdd:cd07831     81 LMDMNLYELIKGR-KRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPEN 130
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
30-253 2.93e-09

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 60.41  E-value: 2.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLT-RENVALKV-ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNY--- 104
Cdd:cd14214     11 LQERYEIVGDLGEGTFGKVVECLDHARgKSQVALKIiRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSDWFNFhgh 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 --VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCY--------- 173
Cdd:cd14214     91 mcIAFELLGKNTFEFLKENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILF--VNSEFDTLYnesksceek 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  174 --------MLDFGLA---RQYTNT---TGDVRPPRNVAgfrgtvryasvnahknrEMGRHD--DLWSLFYMLVEFAVGQL 237
Cdd:cd14214    169 svkntsirVADFGSAtfdHEHHTTivaTRHYRPPEVIL-----------------ELGWAQpcDVWSLGCILFEYYRGFT 231
                          250
                   ....*....|....*.
gi 1034651883  238 PWRKIKDKEQVGMIKE 253
Cdd:cd14214    232 LFQTHENREHLVMMEK 247
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
35-239 3.05e-09

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 59.76  E-value: 3.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQpKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKfNYVVMQL 109
Cdd:cd06620      8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKVihidaKSSVR-KQILR-ELQILHECH-SPYIVSFYGAFLNEN-NNIIICM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLADLRRSQPR-GTFTLSTTLRLGKQILESIEAIHSV-GFLHRDIKPSNFAM---GRLpstyRKCymlDFGLARQYT 184
Cdd:cd06620     84 EYMDCGSLDKILKKkGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVnskGQI----KLC---DFGVSGELI 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  185 NTTGDVrpprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06620    157 NSIADT--------FVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPF 203
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
40-225 3.18e-09

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 59.35  E-value: 3.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQ--VLKMEVAVLKKLQGKDHVCRFIGCGRNEKFnYVVMQLQGRNLA 115
Cdd:cd14082     11 LGSGQFGIVYGGKHRKTGRDVAIKVidKLRFPTKQesQLRNEVAILQQLSHPGVVNLECMFETPERV-FVVMEKLHGDML 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  116 DLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTyRKCymlDFGLARqytnTTGDVRP 192
Cdd:cd14082     90 EMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVllaSAEPFPQV-KLC---DFGFAR----IIGEKSF 161
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1034651883  193 PRNVAgfrGTVRYASVNAHKNREMGRHDDLWSL 225
Cdd:cd14082    162 RRSVV---GTPAYLAPEVLRNKGYNRSLDMWSV 191
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
35-256 3.19e-09

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 59.22  E-value: 3.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEI----YEAmdlltrENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVcRFIGCGRNEKFN-YVVMQL 109
Cdd:cd05082      9 KLLQTIGKGEFGDVmlgdYRG------NKVAVKCIKNDATAQAFLAEASVMTQLRHSNLV-QLLGVIVEEKGGlYIVTEY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGR-NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTG 188
Cdd:cd05082     82 MAKgSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNV----LVSEDNVAKVSDFGLTKEASSTQD 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  189 DVRPPrnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKYE 256
Cdd:cd05082    158 TGKLP---------VKWTAPEALREKKFSTKSDVWSFGILLWEiYSFGRVPYPRIPLKDVVPRVEKGYK 217
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
32-239 3.41e-09

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: 60.79  E-value: 3.41e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd05622     73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVM 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 Q-LQGRNLADLRRSQ--PRGTFTLSTTlrlgkQILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLARQyT 184
Cdd:cd05622    153 EyMPGGDLVNLMSNYdvPEKWARFYTA-----EVVLALDAIHSMGFIHRDVKPDNMLLDK--SGHLK--LADFGTCMK-M 222
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  185 NTTGDVRPPRNVagfrGTVRYASVNAHKNR----EMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd05622    223 NKEGMVRCDTAV----GTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLVGDTPF 277
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
32-247 3.53e-09

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: 60.38  E-value: 3.53e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAqqpKQVLKME--------------------VAVLKKLQGKDHVc 91
Cdd:cd05573      1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRK---SDMLKREqiahvraerdiladadspwiVRLHYAFQDEDHL- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   92 rfigcgrnekfnYVVMQ-LQGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMG------- 163
Cdd:cd05573     77 ------------YLVMEyMPGGDLMNLLIK--YDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDadghikl 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  164 -------RLPSTYRKCYMLDFGLARQYTNTTGDVRPPRNVAGFR-----GTVRYASVNAHKNREMGRHDDLWSLFYMLVE 231
Cdd:cd05573    143 adfglctKMNKSGDRESYLNDSVNTLFQDNVLARRRPHKQRRVRaysavGTPDYIAPEVLRGTGYGPECDWWSLGVILYE 222
                          250       260
                   ....*....|....*....|....*
gi 1034651883  232 FAVGQLP---------WRKIKDKEQ 247
Cdd:cd05573    223 MLYGFPPfysdslvetYSKIMNWKE 247
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
31-239 4.10e-09

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: 59.74  E-value: 4.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ- 108
Cdd:cd06656     18 KKKYTRFEKIGQGASGTVYTAIDIATGQEVAIKqMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEy 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLARQYTNTTG 188
Cdd:cd06656     98 LAGGSLTDVVTETCMDEGQIAAVCR---ECLQALDFLHSNQVIHRDIKSDNILLGMDGSV----KLTDFGFCAQITPEQS 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  189 dvrpprNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06656    171 ------KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
33-240 4.62e-09

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: 58.96  E-value: 4.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQV-----LKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd14663      1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmveqIKREIAIMKLLRHPNIVELHEVMATKTKIFFVME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTyrkcymlDFGLarqyT 184
Cdd:cd14663     81 LVTGGELFS--KIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLlldEDGNLKIS-------DFGL----S 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  185 NTTGDVRPPRNVAGFRGTVRYASVNAHKNREM-GRHDDLWS----LFYMLvefaVGQLPWR 240
Cdd:cd14663    148 ALSEQFRQDGLLHTTCGTPNYVAPEVLARRGYdGAKADIWScgviLFVLL----AGYLPFD 204
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
33-240 6.50e-09

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: 58.56  E-value: 6.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVES----AQQPKQVLKMEVAVLKKLQgKDHVCRFigcgrNEKFN----- 103
Cdd:cd08530      1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNlgslSQKEREDSVNEIRLLASVN-HPNIIRY-----KEAFLdgnrl 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQL-QGRNLADL--RRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRkcyMLDFG-- 178
Cdd:cd08530     75 CIVMEYaPFGDLSKLisKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSA-GDLVK---IGDLGis 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  179 --LARQYTNTTgdvrpprnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:cd08530    151 kvLKKNLAKTQ------------IGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFE 202
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
35-181 7.38e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 58.76  E-value: 7.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEI----YEAMDLLTRENVA---LKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd05080      7 KKIRDLGEGHFGKVslycYDPTNDGTGEMVAvkaLKADCGPQHRSGWKQEIDILKTLY-HENIVKYKGCCSEQGGKSLQL 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  108 QLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGLAR 181
Cdd:cd05080     86 IMEYVPLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDN----DRLVKIGDFGLAK 155
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
36-267 7.42e-09

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: 58.53  E-value: 7.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL-QG 111
Cdd:cd14046     10 ELQVLGKGAFGQVVKVRNKLDGRYYAIKkikLRSESKNNSRILREVMLLSRLN-HQHVVRYYQAWIERANLYIQMEYcEK 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN-FAMGRlpstyRKCYMLDFGLA----RQYTNT 186
Cdd:cd14046     89 STLRDLIDSG--LFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNiFLDSN-----GNVKIGDFGLAtsnkLNVELA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  187 TGDVRPPRNVAGFR--------GTVRYASVNAHKNREmGRHD---DLWSL----FYMLVEFAVG---------------Q 236
Cdd:cd14046    162 TQDINKSTSAALGSsgdltgnvGTALYVAPEVQSGTK-STYNekvDMYSLgiifFEMCYPFSTGmervqiltalrsvsiE 240
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1034651883  237 LP--WRKIKDKEQVGMIkekyehRMLLKHMPSE 267
Cdd:cd14046    241 FPpdFDDNKHSKQAKLI------RWLLNHDPAK 267
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
34-290 8.21e-09

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: 58.48  E-value: 8.21e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGC-------GRNEKFnYV 105
Cdd:cd06636     18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVmDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAfikksppGHDDQL-WL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQGR-NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYT 184
Cdd:cd06636     97 VMEFCGAgSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNV----LLTENAEVKLVDFGVSAQLD 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  185 NTTGDvrppRNVagFRGTVRYAS--VNAHKNREMGRHD---DLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRM 259
Cdd:cd06636    173 RTVGR----RNT--FIGTPYWMApeVIACDENPDATYDyrsDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPKL 246
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1034651883  260 LLKHMPSEFHLFLDHIASLDYFTKPDYQLIM 290
Cdd:cd06636    247 KSKKWSKKFIDFIEGCLVKNYLSRPSTEQLL 277
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
37-239 8.79e-09

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: 58.26  E-value: 8.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQV--LKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ-LQ 110
Cdd:cd05611      1 LKPISKGAFGSVYLAKKRSTGDYFAIKVlkkSDMIAKNQVtnVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEyLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADLrrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTyrkcymlDFGLARqytntT 187
Cdd:cd05611     81 GGDCASL--IKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLlidQTGHLKLT-------DFGLSR-----N 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  188 GDVRppRNVAGFRGTVRY---ASVNAHKNREMGrhdDLWSLFYMLVEFAVGQLPW 239
Cdd:cd05611    147 GLEK--RHNKKFVGTPDYlapETILGVGDDKMS---DWWSLGCVIFEFLFGYPPF 196
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
40-254 9.16e-09

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: 58.09  E-value: 9.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFG--EIYEAMDLLTRENVALKV-------ESAQQPKQVLKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYV-VMQL 109
Cdd:cd13994      1 IGKGATSvvRIVTKKNPRSGVLYAVKEyrrrddeSKRKDYVKRLTSEYIISSKLHHP-NIVKVLDLCQDLHGKWClVMEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYtNTTG 188
Cdd:cd13994     80 cPGGDLFTLIEKA--DSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENI----LLDEDGVLKLTDFGTAEVF-GMPA 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  189 DVRPPRNvAGFRGTVRYASVNAHKNREM-GRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEK 254
Cdd:cd13994    153 EKESPMS-AGLCGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFTGRFPWRSAKKSDSAYKAYEK 218
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
37-243 9.56e-09

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 58.35  E-value: 9.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKmEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQLQGR 112
Cdd:cd06619      6 QEILGHGNGGTVYKAYHLLTRRILAVKVipldITVELQKQIMS-ELEILYKCDSP-YIIGFYGAFFVENRISICTEFMDG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSQPRGTFTlsttlRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTGDVrp 192
Cdd:cd06619     84 GSLDVYRKIPEHVLG-----RIAVAVVKGLTYLWSLKILHRDVKPSNM----LVNTRGQVKLCDFGVSTQLVNSIAKT-- 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  193 prnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIK 243
Cdd:cd06619    153 ------YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQ 197
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
40-183 9.64e-09

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


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 58.00  E-value: 9.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPKQ--VLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADl 117
Cdd:cd14193     12 LGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEkeEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGGELFD- 90
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  118 RRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLARQY 183
Cdd:cd14193     91 RIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILC--VSREANQVKIIDFGLARRY 154
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
40-181 1.33e-08

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 57.38  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMdllTREN----VALKVESAQ---QPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ-LQG 111
Cdd:cd14120      1 IGHGAFAVVFKGR---HRKKpdlpVAIKCITKKnlsKSQNLLGKEIKILKELS-HENVVALLDCQETSSSVYLVMEyCNG 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  112 RNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM----GRLPSTYR-KCYMLDFGLAR 181
Cdd:cd14120     77 GDLAD--YLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsGRKPSPNDiRLKIADFGFAR 149
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
39-187 1.33e-08

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: 57.43  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   39 KIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQVLKmEVAVLKKLQGKDHVcRFIG-CGRNEKFnYVVMQLQGR-NL 114
Cdd:cd05052     13 KLGGGQYGEVYEGVWKKYNLTVAVKTlkEDTMEVEEFLK-EAAVMKEIKHPNLV-QLLGvCTREPPF-YIITEFMPYgNL 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  115 ADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyrKCYML---DFGLARQYTNTT 187
Cdd:cd05052     90 LDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVG-------ENHLVkvaDFGLSRLMTGDT 158
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
34-254 1.34e-08

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: 57.46  E-value: 1.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV--------ESAQQPKQvLKMEV---------AVLKKLQGKDHVCRFIGC 96
Cdd:cd14077      3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIiprasnagLKKEREKR-LEKEIsrdirtireAALSSLLNHPHICRLRDF 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   97 GRNEKFNYVVMQ-LQGRNLAD-------LRRSQPRgtftlsttlRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPST 168
Cdd:cd14077     82 LRTPNHYYMLFEyVDGGQLLDyiishgkLKEKQAR---------KFARQIASALDYLHRNSIVHRDLKIENI----LISK 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  169 YRKCYMLDFGLARQYtnttgdvRPPRNVAGFRGTVRYAS---VNAhkNREMGRHDDLWSLFYMLVEFAVGQLPWrkikDK 245
Cdd:cd14077    149 SGNIKIIDFGLSNLY-------DPRRLLRTFCGSLYFAApelLQA--QPYTGPEVDVWSFGVVLYVLVCGKVPF----DD 215

                   ....*....
gi 1034651883  246 EQVGMIKEK 254
Cdd:cd14077    216 ENMPALHAK 224
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
32-290 1.56e-08

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: 57.27  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTREnVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQ 110
Cdd:cd05112      4 SELTFVQEIGSGQFGLVHLGYWLNKDK-VAIKtIREGAMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFME 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLAR-----QYTN 185
Cdd:cd05112     83 HGCLSDYLRTQ-RGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGE--NQVVK--VSDFGMTRfvlddQYTS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  186 TTGDVRPprnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKyeHRMLLKHM 264
Cdd:cd05112    158 STGTKFP----------VKWSSPEVFSFSRYSSKSDVWSFGVLMWEvFSEGKIPYENRSNSEVVEDINAG--FRLYKPRL 225
                          250       260
                   ....*....|....*....|....*..
gi 1034651883  265 -PSEFHLFLDHIASLDYFTKPDYQLIM 290
Cdd:cd05112    226 aSTHVYEIMNHCWKERPEDRPSFSLLL 252
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
36-242 1.56e-08

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: 57.40  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMDLLTRENVALK--------VESAQQPKQV--LKMEVAVLKKLQGKDH--VCRFIGCGRNEKFN 103
Cdd:cd14004      4 ILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkerilVDTWVRDRKLgtVPLEIHILDTLNKRSHpnIVKLLDFFEDDEFY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQLQGR--NLADLRRSQPRGTFTLSTTLRlgKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTYRkCYMLDFGLAR 181
Cdd:cd14004     84 YLVMEKHGSgmDLFDFIERKPNMDEKEAKYIF--RQVADAVKHLHDQGIVHRDIKDENVI---LDGNGT-IKLIDFGSAA 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  182 QYTNTTGDVrpprnvagFRGTVRYASVNAHK-NREMGRHDDLWSLFYMLVEFAVGQLPWRKI 242
Cdd:cd14004    158 YIKSGPFDT--------FVGTIDYAAPEVLRgNPYGGKEQDIWALGVLLYTLVFKENPFYNI 211
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
31-239 1.71e-08

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: 57.81  E-value: 1.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKM-EVAVLKKLQGKDhVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd06655     18 KKKYTRYEKIGQGASGTVFTAIDVATGQEVAIKqINLQKQPKKELIInEILVMKELKNPN-IVNFLDSFLVGDELFVVME 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 -LQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLARQYTNTT 187
Cdd:cd06655     97 yLAGGSLTDVVTETCMDEAQIAAVCR---ECLQALEFLHANQVIHRDIKSDNVLLGMDGSV----KLTDFGFCAQITPEQ 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  188 GdvrpprNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06655    170 S------KRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPY 215
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
33-239 1.78e-08

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


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 57.14  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ--PKQVLKM--EVAVLKKLqgkDH--VCRFIGCGRNEKFNYVV 106
Cdd:cd14072      1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQlnPSSLQKLfrEVRIMKIL---NHpnIVKLFEVIETEKTLYLV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQL-QGRNLAD-------LRRSQPRGTFtlsttlrlgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFG 178
Cdd:cd14072     78 MEYaSGGEVFDylvahgrMKEKEARAKF---------RQIVSAVQYCHQKRIVHRDLKAENL----LLDADMNIKIADFG 144
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  179 LARQYTnttgdvrPPRNVAGFRGTVRYASVNAHKNREM-GRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14072    145 FSNEFT-------PGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLVSGSLPF 199
pknD PRK13184
serine/threonine-protein kinase PknD;
33-180 2.01e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 59.01  E-value: 2.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK------VESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVV 106
Cdd:PRK13184     3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKkiredlSENPLLKKRFLR-EAKIAADLIHPGIVPVYSICSDGDPVYYTM 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLADLRRS----------QPRGTfTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLD 176
Cdd:PRK13184    82 PYIEGYTLKSLLKSvwqkeslskeLAEKT-SVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGL----FGEVVILD 156

                   ....
gi 1034651883  177 FGLA 180
Cdd:PRK13184   157 WGAA 160
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
32-184 2.03e-08

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 57.54  E-value: 2.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEK----- 101
Cdd:cd07837      1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKktrleMEEEGVPSTALR-EVSLLQMLSQSIYIVRLLDVEHVEEngkpl 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 ----FNYVVMQLqgRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkCYMLDF 177
Cdd:cd07837     80 lylvFEYLDTDL--KKFIDSYGRGPHNPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGL---LKIADL 154

                   ....*..
gi 1034651883  178 GLARQYT 184
Cdd:cd07837    155 GLGRAFT 161
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
33-277 2.22e-08

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: 57.13  E-value: 2.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK--VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQ 110
Cdd:cd14036      1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKrlLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSAASIGKEESDQGQAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADL---------RRSQPRGTFTLSTTLRLGKQILESIEAIH--SVGFLHRDIKPSNFAMGRlPSTYRKCymlDFGL 179
Cdd:cd14036     81 YLLLTELckgqlvdfvKKVEAPGPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGN-QGQIKLC---DFGS 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  180 ArqytntTGDVRPPRN--VAGFRGTVR----------YAS---VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWrkiKD 244
Cdd:cd14036    157 A------TTEAHYPDYswSAQKRSLVEdeitrnttpmYRTpemIDLYSNYPIGEKQDIWALGCILYLLCFRKHPF---ED 227
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1034651883  245 KEQVGMIKEKYehrmLLKHMPSEFHLFLDHIAS 277
Cdd:cd14036    228 GAKLRIINAKY----TIPPNDTQYTVFHDLIRS 256
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
35-181 2.43e-08

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 57.73  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALK------VESAQQPKQVLkME------------VAVLKKLQGKDHVcrfigc 96
Cdd:cd05600     14 QILTQVGQGGYGSVFLARKKDTGEICALKimkkkvLFKLNEVNHVL-TErdiltttnspwlVKLLYAFQDPENV------ 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   97 grnekfnYVVMQLQgrnladlrrsqPRGTF-TLSTTLRLGK---------QILESIEAIHSVGFLHRDIKPSNF---AMG 163
Cdd:cd05600     87 -------YLAMEYV-----------PGGDFrTLLNNSGILSeeharfyiaEMFAAISSLHQLGYIHRDLKPENFlidSSG 148
                          170
                   ....*....|....*...
gi 1034651883  164 RLPSTyrkcymlDFGLAR 181
Cdd:cd05600    149 HIKLT-------DFGLAS 159
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
33-238 2.47e-08

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 56.90  E-value: 2.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VE-----SAQQPKQVLKmEVAVLKKLqgkDH--VCRFIGCGRNEKFNY 104
Cdd:cd08224      1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKkVQifemmDAKARQDCLK-EIDLLQQL---NHpnIIKYLASFIENNELN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQL-QGRNLADL---RRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPstyrkcyMLDF 177
Cdd:cd08224     77 IVLELaDAGDLSRLikhFKKQKR-LIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVfitANGVVK-------LGDL 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  178 GLARQYTNTTgdvrpprnVAGFR--GTVRYASvnAHKNREMGRH--DDLWSLFYMLVEFAVGQLP 238
Cdd:cd08224    149 GLGRFFSSKT--------TAAHSlvGTPYYMS--PERIREQGYDfkSDIWSLGCLLYEMAALQSP 203
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
40-238 3.09e-08

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 56.46  E-value: 3.09e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK------VESAQQPKQVlKMEVAVLKKLqgkDH--VCRFIGCGRNEKFNYVVMQL-Q 110
Cdd:cd05572      1 LGVGGFGRVELVQLKSKGRTFALKcvkkrhIVQTRQQEHI-FSEKEILEEC---NSpfIVKLYRTFKDKKYLYMLMEYcL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLARQ-------Y 183
Cdd:cd05572     77 GGELWTILRD--RGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDS--NGYVK--LVDFGFAKKlgsgrktW 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  184 TnttgdvrpprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd05572    151 T--------------FCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPP 191
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
38-259 3.26e-08

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: 56.14  E-value: 3.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTREnVALKV--ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIG-CGRNEKFnYVVMQLQGR-N 113
Cdd:cd05034      1 KKLGAGQFGEVWMGVWNGTTK-VAVKTlkPGTMSPEAFLQ-EAQIMKKLR-HDKLVQLYAvCSDEEPI-YIVTELMSKgS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 LADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPStyrkCYMLDFGLARQYTNttgDVRPP 193
Cdd:cd05034     77 LLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNV----CKVADFGLARLIED---DEYTA 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  194 RNVAGFrgTVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKYehRM 259
Cdd:cd05034    150 REGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLYEiVTYGRVPYPGMTNREVLEQVERGY--RM 212
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
34-239 3.42e-08

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: 57.32  E-value: 3.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ- 108
Cdd:cd05621     54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLlskfEMIKRSDSAFFWEERDIMAFANSPWVVQLFCAFQDDKYLYMVMEy 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLADLRRSQ--PRGTFTLSTTlrlgkQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGLARQyTNT 186
Cdd:cd05621    134 MPGGDLVNLMSNYdvPEKWAKFYTA-----EVVLALDAIHSMGLIHRDVKPDNMLLDK----YGHLKLADFGTCMK-MDE 203
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  187 TGDVRPPRNVagfrGTVRYASVNAHKNR----EMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd05621    204 TGMVHCDTAV----GTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLVGDTPF 256
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
34-238 3.49e-08

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 56.16  E-value: 3.49e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQqPK---QVLKMEVAVLKKLQGKDHVcRFIGC-GRNEKFnYVVMQL 109
Cdd:cd06613      2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLE-PGddfEIIQQEISMLKECRHPNIV-AYFGSyLRRDKL-WIVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLADLRrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpsTYRKCYML-DFGLARQYTNTT 187
Cdd:cd06613     79 cGGGSLQDIY--QVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILL-----TEDGDVKLaDFGVSAQLTATI 151
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  188 GDvrppRNvaGFRGTVRYASVNAHKNREMGRHD---DLWSLFYMLVEFAVGQLP 238
Cdd:cd06613    152 AK----RK--SFIGTPYWMAPEVAAVERKGGYDgkcDIWALGITAIELAELQPP 199
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
34-238 3.78e-08

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


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 56.15  E-value: 3.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ-PKQV----LKMEVAVLKKLQGKDHVCrFIGCGRNEKFNYVVMQ 108
Cdd:cd14162      2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKaPEDYlqkfLPREIEVIKGLKHPNLIC-FYEAIETTSRVYIIME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyrkcymlDFGLARQyT 184
Cdd:cd14162     81 LaENGDLLDYIRKN--GALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLdknNNLKIT-------DFGFARG-V 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  185 NTTGDVRPPRNVAgFRGTVRYASvnahknREMGR-------HDDLWSLFYMLVEFAVGQLP 238
Cdd:cd14162    151 MKTKDGKPKLSET-YCGSYAYAS------PEILRgipydpfLSDIWSMGVVLYTMVYGRLP 204
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
30-193 4.30e-08

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 56.80  E-value: 4.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK--------VESAQQPKQvlkmEVAVLKKLQGKDHVCRFIGCGR--N 99
Cdd:cd07852      5 ILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKkifdafrnATDAQRTFR----EIMFLQELNDHPNIIKLLNVIRaeN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  100 EKFNYVV---MQlqgrnlADLrrsqprgtftlSTTLRLG-----------KQILESIEAIHSVGFLHRDIKPSNFamgrL 165
Cdd:cd07852     81 DKDIYLVfeyME------TDL-----------HAVIRANiledihkqyimYQLLKALKYLHSGGVIHRDLKPSNI----L 139
                          170       180
                   ....*....|....*....|....*...
gi 1034651883  166 PSTYRKCYMLDFGLARQYTNTTGDVRPP 193
Cdd:cd07852    140 LNSDCRVKLADFGLARSLSQLEEDDENP 167
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
30-181 4.46e-08

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 56.83  E-value: 4.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQgKDHVCRFIG------CGR 98
Cdd:cd07879     13 LPERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIKklsrpFQSEIFAKRAYR-ELTLLKHMQ-HENVIGLLDvftsavSGD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   99 NEKFNYVVMQLQGRNLADLRRSQprgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKCYM--LD 176
Cdd:cd07879     91 EFQDFYLVMPYMQTDLQKIMGHP----LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVN------EDCELkiLD 160

                   ....*
gi 1034651883  177 FGLAR 181
Cdd:cd07879    161 FGLAR 165
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
33-159 4.48e-08

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: 56.15  E-value: 4.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKmEVAVLKKLQGK------DHvcRFIGCGRNEKFN 103
Cdd:cd13986      1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKkilCHSKEDVKEAMR-EIENYRLFNHPnilrllDS--QIVKEAGGKKEV 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  104 YVVMQLQGR-NLADL--RRSQPRGTFTLSTTLRLGKQILESIEAIHS---VGFLHRDIKPSN 159
Cdd:cd13986     78 YLLLPYYKRgSLQDEieRRLVKGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGN 139
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
37-181 4.54e-08

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: 56.14  E-value: 4.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQLQG 111
Cdd:cd07835      4 LEKIGEGTYGVVYKARDKLTGEIVALKkirLETEDEgvPSTAIR-EISLLKELN-HPNIVRLLDVVHSENKLYLVFEFLD 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd07835     82 LDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNL----LIDTEGALKLADFGLAR 147
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
40-159 4.89e-08

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: 56.13  E-value: 4.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAmdllTREN---VALKV---ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ-LQGR 112
Cdd:cd14066      1 IGSGGFGTVYKG----VLENgtvVAVKRlneMNCAASKKEFLTELEMLGRLR-HPNLVRLLGYCLESDEKLLVYEyMPNG 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  113 NLAD-LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFL---HRDIKPSN 159
Cdd:cd14066     76 SLEDrLHCHKGSPPLPWPQRLKIAKGIARGLEYLHEECPPpiiHGDIKSSN 126
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
32-236 5.00e-08

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: 56.28  E-value: 5.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK--VESAQQpKQVLKM---EVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd07846      1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKkfLESEDD-KMVKKIamrEIKMLKQLR-HENLVNLIEVFRRKKRWYLV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLADLRRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQ---- 182
Cdd:cd07846     79 FEFVDHTVLDDLEKYPNG-LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENI----LVSQSGVVKLCDFGFARTlaap 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  183 ---YTN--TTGDVRPPRNVAgfrGTVRYasvnahknremGRHDDLWSLFYMLVEFAVGQ 236
Cdd:cd07846    154 gevYTDyvATRWYRAPELLV---GDTKY-----------GKAVDVWAVGCLVTEMLTGE 198
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
33-181 6.15e-08

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: 56.27  E-value: 6.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKveSAQQPKQ-VLKMEVA----VLKKLQGKDHVCRFIGCGRNEK----FN 103
Cdd:cd07850      1 RYQNLKPIGSGAQGIVCAAYDTVTGQNVAIK--KLSRPFQnVTHAKRAyrelVLMKLVNHKNIIGLLNVFTPQKsleeFQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 --YVVMQLQGRNLA-----DLrrSQPRGTFTLSttlrlgkQILESIEAIHSVGFLHRDIKPSNFAMgRLPSTYRkcyMLD 176
Cdd:cd07850     79 dvYLVMELMDANLCqviqmDL--DHERMSYLLY-------QMLCGIKHLHSAGIIHRDLKPSNIVV-KSDCTLK---ILD 145

                   ....*
gi 1034651883  177 FGLAR 181
Cdd:cd07850    146 FGLAR 150
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
30-256 6.20e-08

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 55.82  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVesaqQPKQVLK-------MEVAVLKKLQgKDHVCRFIGCGRNEKF 102
Cdd:cd14168      8 IKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKC----IPKKALKgkessieNEIAVLRKIK-HENIVALEDIYESPNH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 NYVVMQL-QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFaMGRLPSTYRKCYMLDFGLAR 181
Cdd:cd14168     83 LYLVMQLvSGGELFD--RIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENL-LYFSQDEESKIMISDFGLSK 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  182 QytNTTGDVrpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDK---EQVgmIKEKYE 256
Cdd:cd14168    160 M--EGKGDV-----MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSklfEQI--LKADYE 228
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
32-236 7.42e-08

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: 55.77  E-value: 7.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK----VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd07848      1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKkfkdSEENEEVKETTLRELKMLRTLK-QENIVELKEAFRRRGKLYLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRRSQPRGTFTLSTTLRLgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTT 187
Cdd:cd07848     80 EYVEKNMLELLEEMPNGVPPEKVRSYI-YQLIKAIHWCHKNDIVHRDIKPENL----LISHNDVLKLCDFGFARNLSEGS 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1034651883  188 GdvrppRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQ 236
Cdd:cd07848    155 N-----ANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQ 198
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
34-290 8.38e-08

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 55.50  E-value: 8.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGC-------GRNEKFnYV 105
Cdd:cd06637      8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVmDVTGDEEEEIKQEINMLKKYSHHRNIATYYGAfikknppGMDDQL-WL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQGR-NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYT 184
Cdd:cd06637     87 VMEFCGAgSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNV----LLTENAEVKLVDFGVSAQLD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  185 NTTGDvrppRNVagFRGTVRYAS--VNAHKNREMGRHD---DLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRM 259
Cdd:cd06637    163 RTVGR----RNT--FIGTPYWMApeVIACDENPDATYDfksDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRL 236
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1034651883  260 LLKHMPSEFHLFLDHIASLDYFTKPDYQLIM 290
Cdd:cd06637    237 KSKKWSKKFQSFIESCLVKNHSQRPSTEQLM 267
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
32-239 8.51e-08

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 55.42  E-value: 8.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQvlkmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQL 109
Cdd:cd14175      1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVidKSKRDPSE----EIEILLRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLAD--LRR---SQPRGTFTLSTtlrlgkqILESIEAIHSVGFLHRDIKPSNF----AMGRlPSTYRKCymlDFGL 179
Cdd:cd14175     77 mRGGELLDkiLRQkffSEREASSVLHT-------ICKTVEYLHSQGVVHRDLKPSNIlyvdESGN-PESLRIC---DFGF 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  180 ARQYTNTTGDVRPPRNVAGFrgtvryASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14175    146 AKQLRAENGLLMTPCYTANF------VAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPF 199
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
31-246 9.08e-08

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: 55.01  E-value: 9.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVA---LKVESAQQpKQVLKMEVAVLKKLqgkdHVCRFIGC--GRNEKFNyV 105
Cdd:cd14191      1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAgkfFKAYSAKE-KENIRQEISIMNCL----HHPKLVQCvdAFEEKAN-I 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQGRNLADLRRSQPRGTFTLST--TLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLARQY 183
Cdd:cd14191     75 VMVLEMVSGGELFERIIDEDFELTEreCIKYMRQISEGVEYIHKQGIVHLDLKPENIMC--VNKTGTKIKLIDFGLARRL 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  184 TNtTGDVRPprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKE 246
Cdd:cd14191    153 EN-AGSLKV------LFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNE 208
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
34-239 9.21e-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: 54.87  E-value: 9.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPK---QVLKMEVAVLKKLQgkdHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14186      3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMidKKAMQKAgmvQRVRNEVEIHCQLK---HPSILELYNYFEDSNYVYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLADLRR--SQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTnt 186
Cdd:cd14186     80 LEMCHNGEMSRylKNRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNL----LLTRNMNIKIADFGLATQLK-- 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  187 tgdvRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14186    154 ----MPHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPF 202
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
40-275 9.87e-08

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 55.02  E-value: 9.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYE-----------AMDLLTRENVAlkvesaqQPKQVLKMEVAVLKKLQGKDHVCRFigcGRNEKFN--YVV 106
Cdd:cd14202     10 IGHGAFAVVFKgrhkekhdlevAVKCINKKNLA-------KSQTLLGKEIKILKELKHENIVALY---DFQEIANsvYLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQL-QGRNLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM----GRLPSTYRKCYML-DFGLA 180
Cdd:cd14202     80 MEYcNGGDLADYLHT--MRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysgGRKSNPNNIRIKIaDFGFA 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQYTNTTgdvrpprNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEqvgmIKEKYE-HRM 259
Cdd:cd14202    158 RYLQNNM-------MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD----LRLFYEkNKS 226
                          250
                   ....*....|....*.
gi 1034651883  260 LLKHMPSEFHLFLDHI 275
Cdd:cd14202    227 LSPNIPRETSSHLRQL 242
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
30-181 1.01e-07

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 55.77  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKM--EVAVLKKLQGKDHVCRF-IGCGRN-EKFN- 103
Cdd:cd07849      3 VGPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKkISPFEHQTYCLRTlrEIKILLRFKHENIIGILdIQRPPTfESFKd 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 -YVVMQLQGRNLADLRRSQPRGT-----FTLsttlrlgkQILESIEAIHSVGFLHRDIKPSNFAmgrLPST--YRKCyml 175
Cdd:cd07849     83 vYIVQELMETDLYKLIKTQHLSNdhiqyFLY--------QILRGLKYIHSANVLHRDLKPSNLL---LNTNcdLKIC--- 148

                   ....*.
gi 1034651883  176 DFGLAR 181
Cdd:cd07849    149 DFGLAR 154
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
36-182 1.03e-07

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 55.33  E-value: 1.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMDLLTRENVALKVEsaQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQL-QGRNL 114
Cdd:cd14091      4 IKEEIGKGSYSVCKRCIHKATGKEYAVKII--DKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELlRGGEL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  115 AD--LRRSQprgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN--FA-MGRLPSTYRKCymlDFGLARQ 182
Cdd:cd14091     82 LDriLRQKF----FSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNilYAdESGDPESLRIC---DFGFAKQ 147
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
29-159 1.12e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 55.28  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKL-------QGKDHVCRFIG----C 96
Cdd:cd14136      7 VYNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVvKSAQHYTEAALDEIKLLKCVreadpkdPGREHVVQLLDdfkhT 86
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883   97 GRNEKFNYVVMQLQGRNLADL-RRSQPRGtFTLSTTLRLGKQILESIEAIHSV-GFLHRDIKPSN 159
Cdd:cd14136     87 GPNGTHVCMVFEVLGPNLLKLiKRYNYRG-IPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPEN 150
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
36-248 1.15e-07

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 55.04  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMdllTRENVALKVESAQQPK----QVLKMEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVMQLQG 111
Cdd:cd14149     16 LSTRIGSGSFGTVYKGK---WHGDVAVKILKVVDPTpeqfQAFRNEVAVLRKTRHVN-ILLFMGYMTKDNLAIVTQWCEG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLARQYTNTTGDvr 191
Cdd:cd14149     92 SSLYKHLHVQ-ETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTV----KIGDFGLATVKSRWSGS-- 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  192 ppRNVAGFRGTVRYAS---VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV 248
Cdd:cd14149    165 --QQVEQPTGSILWMApevIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQI 222
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
34-239 1.21e-07

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: 54.82  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYE-----------AMDLLTRENVALKVESAQQPKQVLKM--EVAVLKKLQGKDHVCRFIGCGRNE 100
Cdd:cd08528      2 YAVLELLGSGAFGCVYKvrkksngqtllALKEINMTNPAFGRTEQERDKSVGDIisEVNIIKEQLRHPNIVRYYKTFLEN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQL-QGRNLADLRRS--QPRGTFTLSTTLRLGKQILESIEAIH-SVGFLHRDIKPSNFAMGrlpsTYRKCYMLD 176
Cdd:cd08528     82 DRLYIVMELiEGAPLGEHFSSlkEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLG----EDDKVTITD 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  177 FGLARQytnttgDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd08528    158 FGLAKQ------KGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPF 214
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
40-272 1.36e-07

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 54.63  E-value: 1.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLL-TRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKDHVCRFigcGRNEKFN--YVVMQL-QGR 112
Cdd:cd14201     14 VGHGAFAVVFKGRHRKkTDWEVAIKSinkKNLSKSQILLGKEIKILKELQHENIVALY---DVQEMPNsvFLVMEYcNGG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTYR--KCYMLDFGLARQYTNTT 187
Cdd:cd14201     91 DLADYL--QAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyaSRKKSSVSgiRIKIADFGFARYLQSNM 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 gdvrpprNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKiKDKEQVGMIKEKyeHRMLLKHMPSE 267
Cdd:cd14201    169 -------MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQA-NSPQDLRMFYEK--NKNLQPSIPRE 238

                   ....*
gi 1034651883  268 FHLFL 272
Cdd:cd14201    239 TSPYL 243
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
33-188 1.38e-07

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 55.17  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKD-----HVcrFIGCGRNE-K 101
Cdd:cd07859      1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKkindvFEHVSDATRILR-EIKLLRLLRHPDiveikHI--MLPPSRREfK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FNYVVMQLQGRNLADLRRSQPRGT-----FTLSttlrlgkQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLD 176
Cdd:cd07859     78 DIYVVFELMESDLHQVIKANDDLTpehhqFFLY-------QLLRALKYIHTANVFHRDLKPKNI----LANADCKLKICD 146
                          170
                   ....*....|..
gi 1034651883  177 FGLARQYTNTTG 188
Cdd:cd07859    147 FGLARVAFNDTP 158
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
32-188 1.40e-07

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 54.62  E-value: 1.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGC-------GRNEKFn 103
Cdd:cd06608      6 GIFELVEVIGEGTYGKVYKARHKKTGQLAAIKImDIIEDEEEEIKLEINILRKFSNHPNIATFYGAfikkdppGGDDQL- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQL-QGRNLADLRRSqprgtftlstTLRLGKQILESI------EAIHSVGFL------HRDIKPSNFamgrLPSTYR 170
Cdd:cd06608     85 WLVMEYcGGGSVTDLVKG----------LRKKGKRLKEEWiayilrETLRGLAYLhenkviHRDIKGQNI----LLTEEA 150
                          170
                   ....*....|....*...
gi 1034651883  171 KCYMLDFGLARQYTNTTG 188
Cdd:cd06608    151 EVKLVDFGVSAQLDSTLG 168
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
29-295 1.42e-07

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 54.51  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYeaMDLLT-RENVALKV--ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYV 105
Cdd:cd05067      4 VPRETLKLVERLGAGQFGEVW--MGYYNgHTKVAIKSlkQGSMSPDAFLA-EANLMKQLQ-HQRLVRLYAVVTQEPIYII 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTN 185
Cdd:cd05067     80 TEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANI----LVSDTLSCKIADFGLARLIED 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  186 TTGDVRpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAV-GQLPWRKIKDKEQVGMIKEKYehRMLL-KH 263
Cdd:cd05067    156 NEYTAR-----EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNLERGY--RMPRpDN 228
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034651883  264 MPSEFHLFLDHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd05067    229 CPEELYQLMRLCWKERPEDRPTFEYLRSVLED 260
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
33-231 1.94e-07

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: 53.97  E-value: 1.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQVLK--MEVAVLKKLqgkDH--VCRFIGCG-RNEKF 102
Cdd:cd08222      1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKVlkeisVGELQPDETVDanREAKLLSKL---DHpaIVKFHDSFvEKESF 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 NYVVMQLQGRNLADLRRS--QPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpstyrKCYML---DF 177
Cdd:cd08222     78 CIVTEYCEGGDLDDKISEykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL--------KNNVIkvgDF 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  178 GLARQYTNTTgDVrpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE 231
Cdd:cd08222    150 GISRILMGTS-DL-----ATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYE 197
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
32-241 2.09e-07

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: 53.90  E-value: 2.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKDHV---CRFIGcgRNEKfnYV 105
Cdd:cd06610      1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRidlEKCQTSMDELRKEIQAMSQCNHPNVVsyyTSFVV--GDEL--WL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQ-LQGRNLADL-RRSQPRGTF---TLSTTLrlgKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLA 180
Cdd:cd06610     77 VMPlLSGGSLLDImKSSYPRGGLdeaIIATVL---KEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSV----KIADFGVS 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  181 RQYTNTTGDVRPPRNVagFRGTVRY-ASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRK 241
Cdd:cd06610    150 ASLATGGDRTRKVRKT--FVGTPCWmAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYSK 209
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
40-240 2.10e-07

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 54.42  E-value: 2.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVE---SAQQPKQVLKMEVAVLKKLQGKDHVCRF-IGCGRNEKFNYVVMQL-QGRNL 114
Cdd:cd13988      1 LGQGATANVFRGRHKKTGDLYAVKVFnnlSFMRPLDVQMREFEVLKKLNHKNIVKLFaIEEELTTRHKVLVMELcPCGSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADLRrSQPRGTFTLSTT--LRLGKQILESIEAIHSVGFLHRDIKPSNFaMGRLPSTYRKCYML-DFGLARQYtnttGDVR 191
Cdd:cd13988     81 YTVL-EEPSNAYGLPESefLIVLRDVVAGMNHLRENGIVHRDIKPGNI-MRVIGEDGQSVYKLtDFGAAREL----EDDE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  192 PprnVAGFRGTVRY--------ASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:cd13988    155 Q---FVSLYGTEEYlhpdmyerAVLRKDHQKKYGATVDLWSIGVTFYHAATGSLPFR 208
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
31-295 2.12e-07

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: 53.88  E-value: 2.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRW-------KVLKKIGGGGFGEIYEAMdLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKF 102
Cdd:cd05073      3 KDAWeipreslKLEKKLGAGQFGEVWMAT-YNKHTKVAVKtMKPGSMSVEAFLAEANVMKTLQ-HDKLVKLHAVVTKEPI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 NYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQ 182
Cdd:cd05073     81 YIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANI----LVSASLVCKIADFGLARV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  183 YTNTTGDVRpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEF-AVGQLPWRKIKDKEQVGMIKEKYehRM-L 260
Cdd:cd05073    157 IEDNEYTAR-----EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIvTYGRIPYPGMSNPEVIRALERGY--RMpR 229
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1034651883  261 LKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd05073    230 PENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDD 264
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
40-242 2.26e-07

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 53.89  E-value: 2.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAM----DLLTR-------ENVALKVESAQQPKQVLKM-EVAVLKKLQG----KDHVCRFIGCGRNEKFN 103
Cdd:cd14146      2 IGVGGFGKVYRATwkgqEVAVKaarqdpdEDIKATAESVRQEAKLFSMlRHPNIIKLEGvcleEPNLCLVMEFARGGTLN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQLQGRNLA-DLRRSQPRGTFTLSTTLRLGKQILESiEAIhsVGFLHRDIKPSNFAMGRLPSTYRKC----YMLDFG 178
Cdd:cd14146     82 RALAAANAAPGPrRARRIPPHILVNWAVQIARGMLYLHE-EAV--VPILHRDLKSSNILLLEKIEHDDICnktlKITDFG 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  179 LARQYTNTTGdvrpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKI 242
Cdd:cd14146    159 LAREWHRTTK--------MSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI 214
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
32-180 2.35e-07

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: 53.88  E-value: 2.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ---PKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14184      1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKccgKEHLIENEVSILRRVK-HPNIIMLIEEMDTPAELYLVME 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  109 L-QGRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLA 180
Cdd:cd14184     80 LvKGGDLFDAITSSTK--YTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKSLKLGDFGLA 150
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
40-181 2.49e-07

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: 53.67  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKV-----ESAQqpKQVLKmEVAVLKKLQGKdHVCRFIGC-GRNEKFNYVVMQLQGRN 113
Cdd:cd14154      1 LGKGFFGQAIKVTHRETGEVMVMKElirfdEEAQ--RNFLK-EVKVMRSLDHP-NVLKFIGVlYKDKKLNLITEYIPGGT 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  114 LADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd14154     77 LKDVLKDMAR-PLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNC----LVREDKTVVVADFGLAR 139
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
36-239 2.99e-07

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: 53.57  E-value: 2.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMDLLTRENVALK-VE----SAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL- 109
Cdd:cd08529      4 ILNKLGKGSFGVVYKVVRKVDGRVYALKqIDisrmSRKMREEAID-EARVLSKLN-SPYVIKYYDSFVDKGKLNIVMEYa 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGLARQYTNTTgd 189
Cdd:cd08529     82 ENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFL----DKGDNVKIGDLGVAKILSDTT-- 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  190 vrpprNVAG-FRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd08529    156 -----NFAQtIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPF 201
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
29-295 3.06e-07

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: 53.53  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAMdLLTRENVALKV--ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd05070      6 IPRESLQLIKRLGNGQFGEVWMGT-WNGNTKVAIKTlkPGTMSPESFLE-EAQIMKKLK-HDKLVQLYAVVSEEPIYIVT 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpsTYRKCYMLDFGLARQYTNT 186
Cdd:cd05070     83 EYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVG----NGLICKIADFGLARLIEDN 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  187 TGDVRpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAV-GQLPWRKIKDKEQVGMIKEKYehRM-LLKHM 264
Cdd:cd05070    159 EYTAR-----QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGY--RMpCPQDC 231
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1034651883  265 PSEFHLFLDHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd05070    232 PISLHELMIHCWKKDPEERPTFEYLQGFLED 262
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
33-181 3.15e-07

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 54.01  E-value: 3.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKmEVAVLKKLQgKDHVCRF---IGCGRNE------ 100
Cdd:cd07854      6 RYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKkivLTDPQSVKHALR-EIKIIRRLD-HDNIVKVyevLGPSGSDltedvg 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 ---KFN--YVVMQLQGrnlADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKCYML 175
Cdd:cd07854     84 sltELNsvYIVQEYME---TDLANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFIN------TEDLVL 154

                   ....*....
gi 1034651883  176 ---DFGLAR 181
Cdd:cd07854    155 kigDFGLAR 163
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
35-164 3.33e-07

Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 and BubR1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Bub1 (Budding uninhibited by benzimidazoles 1), BubR1, and similar proteins. They contain an N-terminal Bub1/Mad3 homology domain essential for Cdc20 binding and a C-terminal kinase domain. Bub1 and BubR1 are involved in SAC, a surveillance system that delays metaphase to anaphase transition by blocking the activity of APC/C (the anaphase promoting complex) until all chromosomes achieve proper attachments to the mitotic spindle, to avoid chromosome missegregation. Impaired SAC leads to genomic instabilities and tumor development. Bub1 and BubR1 facilitate the localization of SAC proteins to kinetochores and regulate kinetochore-microtubule (K-MT) attachments. Repression studies of Bub1 and BubR1 show that they exert an additive effect in misalignment phenotypes and may function cooperatively or in parallel pathways in regulating K-MT attachments. The Bub1/BubR1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 53.51  E-value: 3.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDL---LTRENVALKVESAQQPKQVLKMEvAVLKKLQGKDHVCRFIGCGRNEKFN---YVVMQ 108
Cdd:cd13981      3 VISKELGEGGYASVYLAKDDdeqSDGSLVALKVEKPPSIWEFYICD-QLHSRLKNSRLRESISGAHSAHLFQdesILVMD 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L--QGR--NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGR 164
Cdd:cd13981     82 YssQGTllDVVNKMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLRL 141
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
27-159 3.36e-07

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 53.86  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   27 NYVVK------DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQP--KQVlKMEVAVLKKLQGKD-----HVCRF 93
Cdd:cd14226      2 DYIVKngekwmDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAflNQA-QIEVRLLELMNKHDtenkyYIVRL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883   94 IGcgrneKFNY-----VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHS--VGFLHRDIKPSN 159
Cdd:cd14226     81 KR-----HFMFrnhlcLVFELLSYNLYDLLRNTNFRGVSLNLTRKFAQQLCTALLFLSTpeLSIIHCDLKPEN 148
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
33-183 3.44e-07

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 53.59  E-value: 3.44e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVM 107
Cdd:cd07839      1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKrvrLDDDDEgvPSSALR-EICLLKELKHKN-IVRLYDVLHSDKKLTLVF 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  108 QLQGRnlaDLRR--SQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQY 183
Cdd:cd07839     79 EYCDQ---DLKKyfDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNL----LINKNGELKLADFGLARAF 149
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
33-264 3.48e-07

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: 53.05  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL 109
Cdd:cd08219      1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKeirLPKSSSAVEDSRKEAVLLAKMK-HPNIVAFKESFEADGHLYIVMEY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGLARQYTNttg 188
Cdd:cd08219     80 cDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFL----TQNGKVKLGDFGSARLLTS--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  189 dvrPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP-----WRKIKDKEQVGMIKE-----KYEHR 258
Cdd:cd08219    153 ---PGAYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPfqansWKNLILKVCQGSYKPlpshySYELR 229

                   ....*.
gi 1034651883  259 MLLKHM 264
Cdd:cd08219    230 SLIKQM 235
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
36-248 3.61e-07

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


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 53.10  E-value: 3.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMdllTRENVALKVESAQQPK----QVLKMEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVMQLQG 111
Cdd:cd14150      4 MLKRIGTGSFGTVFRGK---WHGDVAVKILKVTEPTpeqlQAFKNEMQVLRKTRHVN-ILLFMGFMTRPNFAIITQWCEG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNL-ADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLARQYTNTTGDv 190
Cdd:cd14150     80 SSLyRHLHVTETR--FDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTV----KIGDFGLATVKTRWSGS- 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  191 rppRNVAGFRGTVRYAS---VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV 248
Cdd:cd14150    153 ---QQVEQPSGSILWMApevIRMQDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQI 210
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
26-181 3.88e-07

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 53.88  E-value: 3.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   26 ANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDhVCRFIGCGRNE 100
Cdd:cd07876     15 STFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKklsrpFQNQTHAKRAYR-ELVLLKCVNHKN-IISLLNVFTPQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 K----FN--YVVMQLQGRNLAD---LRRSQPRGTFTLSttlrlgkQILESIEAIHSVGFLHRDIKPSNFAMgRLPSTYRk 171
Cdd:cd07876     93 KsleeFQdvYLVMELMDANLCQvihMELDHERMSYLLY-------QMLCGIKHLHSAGIIHRDLKPSNIVV-KSDCTLK- 163
                          170
                   ....*....|
gi 1034651883  172 cyMLDFGLAR 181
Cdd:cd07876    164 --ILDFGLAR 171
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
35-253 4.03e-07

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: 52.93  E-value: 4.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIG--CGRNEKFNYVVMQ 108
Cdd:cd08217      3 EVLETIGKGSFGTVRKVRRKSDGKILVWKEidygKMSEKEKQQLVSEVNILRELK-HPNIVRYYDriVDRANTTLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADL--RRSQPRGTFTLSTTLRLGKQILESIEAIHSVG-----FLHRDIKPSNFAMgrlpsTYRKCYML-DFGL 179
Cdd:cd08217     82 YcEGGDLAQLikKCKKENQYIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFL-----DSDNNVKLgDFGL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  180 AR------QYTNTtgdvrpprnvagFRGTVRYAS---VNAHKNREmgrHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGM 250
Cdd:cd08217    157 ARvlshdsSFAKT------------YVGTPYYMSpelLNEQSYDE---KSDIWSLGCLIYELCALHPPFQAANQLELAKK 221

                   ...
gi 1034651883  251 IKE 253
Cdd:cd08217    222 IKE 224
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
38-185 4.35e-07

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 53.61  E-value: 4.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKM---------------EVAVLKKLQGK---DHVCRFIgcgr 98
Cdd:PTZ00024    15 AHLGEGTYGKVEKAYDTLTGKIVAIKkVKIIEISNDVTKDrqlvgmcgihfttlrELKIMNEIKHEnimGLVDVYV---- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   99 NEKFNYVVMQLQGRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFG 178
Cdd:PTZ00024    91 EGDFINLVMDIMASDLKKVVDRKIR--LTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFI----NSKGICKIADFG 164

                   ....*..
gi 1034651883  179 LARQYTN 185
Cdd:PTZ00024   165 LARRYGY 171
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
30-180 4.43e-07

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: 53.07  E-value: 4.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFnYVV 106
Cdd:cd14183      4 ISERYKVGRTIGDGNFAVVKECVERSTGREYALKIinkSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTEL-YLV 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  107 MQL-QGRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLA 180
Cdd:cd14183     83 MELvKGGDLFDAITSTNK--YTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLA 155
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
40-251 4.58e-07

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 53.04  E-value: 4.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVA---LKVESAQQPKQVlKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLAD 116
Cdd:cd14192     12 LGGGRFGQVHKCTELSTGLTLAakiIKVKGAKEREEV-KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  117 lRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLARQYtnttgdvRPPRNV 196
Cdd:cd14192     91 -RITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILC--VNSTGNQIKIIDFGLARRY-------KPREKL 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  197 AGFRGTVRYASVNAHKNREMGRHDDLWS---LFYMLVEfavGQLPWRKIKDKEQVGMI 251
Cdd:cd14192    161 KVNFGTPEFLAPEVVNYDFVSFPTDMWSvgvITYMLLS---GLSPFLGETDAETMNNI 215
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
40-248 4.77e-07

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 52.78  E-value: 4.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMdllTRENVALKVESAQQPK----QVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQLQGRNL- 114
Cdd:cd14062      1 IGSGSFGTVYKGR---WHGDVAVKKLNVTDPTpsqlQAFKNEVAVLRKTR-HVNILLFMGYMTKPQLAIVTQWCEGSSLy 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN-FAMGRLpstyrKCYMLDFGLARQYT--NTTGDVR 191
Cdd:cd14062     77 KHLHVLETK--FEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNiFLHEDL-----TVKIGDFGLATVKTrwSGSQQFE 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  192 PPrnvagfRGTV--------RYASVNAHKNremgrHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV 248
Cdd:cd14062    150 QP------TGSIlwmapeviRMQDENPYSF-----QSDVYAFGIVLYELLTGQLPYSHINNRDQI 203
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
33-244 4.80e-07

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 53.56  E-value: 4.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTREN--VALK-VESAQQPKQVLKM---EVAVLKKLQG-KDHVCRF-IGCGRNEKFN- 103
Cdd:cd07857      1 RYELIKELGQGAYGIVCSARNAETSEEetVAIKkITNVFSKKILAKRalrELKLLRHFRGhKNITCLYdMDIVFPGNFNe 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 -YVVMQLQGRNLADLRRS-QPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNF---AMGRLpstyRKCymlDFG 178
Cdd:cd07857     81 lYLYEELMEADLHQIIRSgQPLTDAHFQSFIY---QILCGLKYIHSANVLHRDLKPGNLlvnADCEL----KIC---DFG 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  179 LARQYTNTTGDVRPprNVAGFRGTVRY-ASVNAHKNREMGRHDDLWSLFYMLVEFaVGQLPWRKIKD 244
Cdd:cd07857    151 LARGFSENPGENAG--FMTEYVATRWYrAPEIMLSFQSYTKAIDVWSVGCILAEL-LGRKPVFKGKD 214
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
32-239 4.94e-07

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: 52.65  E-value: 4.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQV-----LKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd14116      5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAgvehqLRREVEIQSHLR-HPNILRLYGYFHDATRVYLI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLAdLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpsTYRKCYMLDFGLARQytnt 186
Cdd:cd14116     84 LEYAPLGTV-YRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLG----SAGELKIADFGWSVH---- 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  187 tgdvRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14116    155 ----APSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPF 203
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
33-235 5.05e-07

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 53.60  E-value: 5.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKL--QGKDHVCRFIGCGRNEKF-NYVVM- 107
Cdd:cd14224     66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKmVRNEKRFHRQAAEEIRILEHLkkQDKDNTMNVIHMLESFTFrNHICMt 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 -QLQGRNLADL-RRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLA----- 180
Cdd:cd14224    146 fELLSMNLYELiKKNKFQG-FSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSGIK--VIDFGSScyehq 222
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  181 RQYTNTTGDV-RPPRNVAGfrgtVRYasvnahknremGRHDDLWSLFYMLVEFAVG 235
Cdd:cd14224    223 RIYTYIQSRFyRAPEVILG----ARY-----------GMPIDMWSFGCILAELLTG 263
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1083-1376 5.98e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 54.41  E-value: 5.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1083 SALSGAPRETPSEMATNSLPNGPALADGPAPVSPLEPSPEKVATISPRRHAMPGSRPRSRIpvllsEEDTGSEPSGSLSA 1162
Cdd:PHA03307   152 PPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSP-----ISASASSPAPAPGR 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1163 KERWSKRARPQQDLARLVMEKRQGrlllrlaSGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATRSR 1242
Cdd:PHA03307   227 SAADDAGASSSDSSSSESSGCGWG-------PENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPS 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1243 IPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSSRLQLQTPPGSATAADLRPKQPPGRGLGPGRAQAGARPPAPRSPR 1322
Cdd:PHA03307   300 PSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPA 379
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883 1323 LPASTSAARNASASPRSQSLsRRESPSPSHQARPGVPPPRGVPPARA----QPDGTPS 1376
Cdd:PHA03307   380 ASAGRPTRRRARAAVAGRAR-RRDATGRFPAGRPRPSPLDAGAASGAfyarYPLLTPS 436
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
29-178 6.07e-07

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 53.17  E-value: 6.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKD----RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQVLkMEVAVLKKLQGKDhvcrfigcgRNEKF 102
Cdd:cd14225     36 VLHDhiayRYEILEVIGKGSFGQVVKALDHKTNEHVAIKIirNKKRFHHQAL-VEVKILDALRRKD---------RDNSH 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 NYVVM--------------QLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPST 168
Cdd:cd14225    106 NVIHMkeyfyfrnhlcitfELLGMNLYELIKKNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQS 185
                          170
                   ....*....|
gi 1034651883  169 YRKcyMLDFG 178
Cdd:cd14225    186 SIK--VIDFG 193
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
36-190 6.12e-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: 52.57  E-value: 6.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEA--MDLLTRENVALKV-ESAQQPKQVLKM----EVAVLKKLQGKD--HVCRFIGcgRNEKFnYVV 106
Cdd:cd14080      4 LGKTIGEGSYSKVKLAeyTKSGLKEKVACKIiDKKKAPKDFLEKflprELEILRKLRHPNiiQVYSIFE--RGSKV-FIF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRnlAD-LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTN 185
Cdd:cd14080     81 MEYAEH--GDlLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENI----LLDSNNNVKLSDFGFARLCPD 154

                   ....*
gi 1034651883  186 TTGDV 190
Cdd:cd14080    155 DDGDV 159
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
26-181 6.26e-07

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 53.17  E-value: 6.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   26 ANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQGKDHVCR---FIGCG 97
Cdd:cd07874     11 STFTVLKRYQNLKPIGSGAQGIVCAAYDAVLDRNVAIKklsrpFQNQTHAKRAYR-ELVLMKCVNHKNIISLlnvFTPQK 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   98 RNEKFN--YVVMQLQGRNLAD---LRRSQPRGTFTLSttlrlgkQILESIEAIHSVGFLHRDIKPSNFAMgRLPSTYRkc 172
Cdd:cd07874     90 SLEEFQdvYLVMELMDANLCQviqMELDHERMSYLLY-------QMLCGIKHLHSAGIIHRDLKPSNIVV-KSDCTLK-- 159

                   ....*....
gi 1034651883  173 yMLDFGLAR 181
Cdd:cd07874    160 -ILDFGLAR 167
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
38-253 6.30e-07

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: 52.32  E-value: 6.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAV-LKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR- 112
Cdd:cd14188      7 KVLGKGGFAKCYEMTDLTTNKVYAAKIiphSRVSKPHQREKIDKEIeLHRILHHKHVVQFYHYFEDKENIYILLEYCSRr 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGLARQYtNTTGDVRp 192
Cdd:cd14188     87 SMAHILKA--RKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFI----NENMELKVGDFGLAARL-EPLEHRR- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  193 pRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKE 253
Cdd:cd14188    159 -RTIC---GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIRE 215
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
40-249 6.31e-07

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: 52.28  E-value: 6.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK-------VESAQQPKQV-LKMEVAVLKKlqgkdhvcrfIGCGrnekFNYVVMQLQG 111
Cdd:cd14100      8 LGSGGFGSVYSGIRVADGAPVAIKhvekdrvSEWGELPNGTrVPMEIVLLKK----------VGSG----FRGVIRLLDW 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLAD-----LRRSQP----------RGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRkcyMLD 176
Cdd:cd14100     74 FERPDsfvlvLERPEPvqdlfdfiteRGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGELK---LID 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  177 FGLARQYTNTTgdvrpprnVAGFRGTVRYASVNAHK-NREMGRHDDLWSLFYMLVEFAVGQLPWRkiKDKEQVG 249
Cdd:cd14100    151 FGSGALLKDTV--------YTDFDGTRVYSPPEWIRfHRYHGRSAAVWSLGILLYDMVCGDIPFE--HDEEIIR 214
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
35-290 7.38e-07

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


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 52.35  E-value: 7.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMD-----LLTRENVALKVESAQQpKQVLkMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL 109
Cdd:cd06605      4 EYLGELGEGNGGVVSKVRHrpsgqIMAVKVIRLEIDEALQ-KQIL-RELDVLHKCNSP-YIVGFYGAFYSEGDISICMEY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLAD--LRRSQPRGTFTLSttlRLGKQILESIEAIHSV-GFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNT 186
Cdd:cd06605     81 MDGGSLDkiLKEVGRIPERILG---KIAVAVVKGLIYLHEKhKIIHRDVKPSNI----LVNSRGQVKLCDFGVSGQLVDS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  187 tgdvrpprnVAG-FRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIkDKEQVGMIKE------KYEHRM 259
Cdd:cd06605    154 ---------LAKtFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPP-NAKPSMMIFEllsyivDEPPPL 223
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1034651883  260 LLKHM-PSEFHLFLDHIASLDYFTKPDYQLIM 290
Cdd:cd06605    224 LPSGKfSPDFQDFVSQCLQKDPTERPSYKELM 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
32-184 7.51e-07

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 52.21  E-value: 7.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQLQ 110
Cdd:cd14108      2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKfIPVRAKKKTSARRELALLAELD-HKSIVRFHDAFEKRRVVIIVTELC 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  111 GRNLadLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlPSTYRKCYMLDFGLARQYT 184
Cdd:cd14108     81 HEEL--LERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMA--DQKTDQVRICDFGNAQELT 150
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
22-181 7.55e-07

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 53.12  E-value: 7.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   22 DILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK---------VESAQQPKQVLKMEVAVLKKLQGKDHVcr 92
Cdd:cd07875     14 EIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKklsrpfqnqTHAKRAYRELVLMKCVNHKNIIGLLNV-- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   93 FIGCGRNEKFN--YVVMQLQGRNLAD---LRRSQPRGTFTLSttlrlgkQILESIEAIHSVGFLHRDIKPSNFAMgRLPS 167
Cdd:cd07875     92 FTPQKSLEEFQdvYIVMELMDANLCQviqMELDHERMSYLLY-------QMLCGIKHLHSAGIIHRDLKPSNIVV-KSDC 163
                          170
                   ....*....|....
gi 1034651883  168 TYRkcyMLDFGLAR 181
Cdd:cd07875    164 TLK---ILDFGLAR 174
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
40-178 8.27e-07

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: 49.75  E-value: 8.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQP--KQVLKMEVAVLKKLQGKD-HVCRFIGCGRNEKFNYVVMQLqgrnLAD 116
Cdd:cd13968      1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNNeeGEDLESEMDILRRLKGLElNIPKVLVTEDVDGPNILLMEL----VKG 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  117 LRRSQPRGTFTLS--TTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFG 178
Cdd:cd13968     77 GTLIAYTQEEELDekDVESIMYQLAECMRLLHSFHLIHRDLNNDNI----LLSEDGNVKLIDFG 136
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
77-245 9.13e-07

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 52.57  E-value: 9.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   77 EVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ-LQGRNLadLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDI 155
Cdd:cd14180     50 EVAALRLCQSHPNIVALHEVLHDQYHTYLVMElLRGGEL--LDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  156 KPSNFAMGRlPSTYRKCYMLDFGLARqytnttgdVRP----PRNVAGFrgTVRYASVNAHKNREMGRHDDLWSLFYMLVE 231
Cdd:cd14180    128 KPENILYAD-ESDGAVLKVIDFGFAR--------LRPqgsrPLQTPCF--TLQYAAPELFSNQGYDESCDLWSLGVILYT 196
                          170
                   ....*....|....
gi 1034651883  232 FAVGQLPWRKIKDK 245
Cdd:cd14180    197 MLSGQVPFQSKRGK 210
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
76-198 9.90e-07

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 51.89  E-value: 9.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   76 MEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTL---RLGKQILESIEAIHSVGFLH 152
Cdd:cd13982     43 REVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAASLQDLVESPRESKLFLRPGLepvRLLRQIASGLAHLHSLNIVH 122
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1034651883  153 RDIKPSNFAMGRLPSTYRKCYML-DFGLARQYTNTTGDVRPPRNVAG 198
Cdd:cd13982    123 RDLKPQNILISTPNAHGNVRAMIsDFGLCKKLDVGRSSFSRRSGVAG 169
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
33-184 1.16e-06

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


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 51.96  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDL------LTRENVALKVESAQQPKQVLKmEVAVLKKLQGKDH--------VCRFIGCGR 98
Cdd:cd07862      2 QYECVAEIGEGAYGKVFKARDLknggrfVALKRVRVQTGEEGMPLSTIR-EVAVLRHLETFEHpnvvrlfdVCTVSRTDR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   99 NEKFNYVVMQLQgRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFG 178
Cdd:cd07862     81 ETKLTLVFEHVD-QDLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNI----LVTSSGQIKLADFG 155

                   ....*.
gi 1034651883  179 LARQYT 184
Cdd:cd07862    156 LARIYS 161
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
33-243 1.17e-06

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: 51.62  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQ----QPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd13997      1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPfrgpKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQME 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGR-NLAD-LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPStyrkCYMLDFGLARQyTNT 186
Cdd:cd13997     81 LCENgSLQDaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGT----CKIGDFGLATR-LET 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  187 TGDVRpprnvagfRGTVRY-ASVNAHKNREMGRHDDLWSLFYMLVEFAVG-QLP-----WRKIK 243
Cdd:cd13997    156 SGDVE--------EGDSRYlAPELLNENYTHLPKADIFSLGVTVYEAATGePLPrngqqWQQLR 211
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
40-205 1.18e-06

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


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 51.69  E-value: 1.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK-VESAQ----QPKQVLKmEVAVLKKLqGKDHVCRFIGCGRNEKFNYVVMQ-LQGRN 113
Cdd:cd13978      1 LGSGGFGTVSKARHVSWFGMVAIKcLHSSPncieERKALLK-EAEKMERA-RHSYVLPLLGVCVERRSLGLVMEyMENGS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 LADL--RRSQPrgtFTLSTTLRLGKQILESIEAIHSV--GFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTGD 189
Cdd:cd13978     79 LKSLleREIQD---VPWSLRFRIIHEIALGMNFLHNMdpPLLHHDLKPENI----LLDNHFHVKISDFGLSKLGMKSISA 151
                          170
                   ....*....|....*.
gi 1034651883  190 VRpPRNVAGFRGTVRY 205
Cdd:cd13978    152 NR-RRGTENLGGTPIY 166
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1069-1350 1.20e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 53.31  E-value: 1.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1069 GLALSGLNGAEIEGSALSGAPRETPSEMATNSLPNGPALADGPAPVSPlepspekvATISPRRHAMPGSRPRSRIPVLLS 1148
Cdd:PRK07003   365 GGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAP--------KAAAAAAATRAEAPPAAPAPPATA 436
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1149 EEDTGSEPSGSLSAkerwSKRARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAA 1228
Cdd:PRK07003   437 DRGDDAADGDAPVP----AKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARA 512
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1229 L--PRKSGRAAATRSRIPRpigLRMPMPvAAQQPASRSHGAAPALDTaITSSRLQLQTPPGSATAADLRPKQPPgrglgp 1306
Cdd:PRK07003   513 PaaASREDAPAAAAPPAPE---ARPPTP-AAAAPAARAGGAAAALDV-LRNAGMRVSSDRGARAAAAAKPAAAP------ 581
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883 1307 graqAGARPPAPR-------SPRLPASTSAARNASASPRSQSLSRRESPSP 1350
Cdd:PRK07003   582 ----AAAPKPAAPrvavqvpTPRARAATGDAPPNGAARAEQAAESRGAPPP 628
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
32-239 1.27e-06

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 51.94  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQvlkmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQL 109
Cdd:cd14178      3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIidKSKRDPSE----EIEILLRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLAD--LRR---SQPRGTFTLSTtlrlgkqILESIEAIHSVGFLHRDIKPSNF----AMGRlPSTYRKCymlDFGL 179
Cdd:cd14178     79 mRGGELLDriLRQkcfSEREASAVLCT-------ITKTVEYLHSQGVVHRDLKPSNIlymdESGN-PESIRIC---DFGF 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  180 ARQYTNTTGDVRPPRNVAGFrgtvryASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14178    148 AKQLRAENGLLMTPCYTANF------VAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPF 201
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
32-230 1.33e-06

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


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 51.65  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPK----QVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd14086      1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSardhQKLEREARICRLLK-HPNIVRLHDSISEEGFHYLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QL--QGRNLADLrrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMG-RLPSTYRKcyMLDFGLARQyt 184
Cdd:cd14086     80 DLvtGGELFEDI---VAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLAsKSKGAAVK--LADFGLAIE-- 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034651883  185 nTTGDvrpPRNVAGFRGTVRYASVNAHKNREMGRHDDLWS----LFYMLV 230
Cdd:cd14086    153 -VQGD---QQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWAcgviLYILLV 198
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
32-189 1.41e-06

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: 51.60  E-value: 1.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK--VESAQQP--KQVLKMEVAVLKKLQGKDHVcRFIGCGRNEKFNYVVM 107
Cdd:cd07847      1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKkfVESEDDPviKKIALREIRMLKQLKHPNLV-NLIEVFRRKRKLHLVF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRRSQPRGTFTLSTTlRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRKCymlDFGLARQYTNTT 187
Cdd:cd07847     80 EYCDHTVLNELEKNPRGVPEHLIK-KIIWQTLQAVNFCHKHNCIHRDVKPENILITK-QGQIKLC---DFGFARILTGPG 154

                   ..
gi 1034651883  188 GD 189
Cdd:cd07847    155 DD 156
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
40-230 1.70e-06

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


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 51.07  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPK--QVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADl 117
Cdd:cd14190     12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKdkEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFE- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  118 RRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLARQYtnttgdvRPPRNVA 197
Cdd:cd14190     91 RIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILC--VNRTGHQVKIIDFGLARRY-------NPREKLK 161
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1034651883  198 GFRGTVRYASVNAHKNREMGRHDDLWSL---FYMLV 230
Cdd:cd14190    162 VNFGTPEFLSPEVVNYDQVSFPTDMWSMgviTYMLL 197
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
29-181 1.85e-06

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: 51.23  E-value: 1.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAMDL-LTRENVALKVE--------SAQQPKQVLkMEVAVLKKLqgkDH--VCRFIGCG 97
Cdd:cd05036      3 VPRKNLTLIRALGQGAFGEVYEGTVSgMPGDPSPLQVAvktlpelcSEQDEMDFL-MEALIMSKF---NHpnIVRCIGVC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   98 RNEKFNYVVMQL-QGRNLAD-LRRSQPR----GTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRK 171
Cdd:cd05036     79 FQRLPRFILLELmAGGDLKSfLRENRPRpeqpSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTC-KGPGRV 157
                          170
                   ....*....|
gi 1034651883  172 CYMLDFGLAR 181
Cdd:cd05036    158 AKIGDFGMAR 167
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
37-183 2.06e-06

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: 51.27  E-value: 2.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQ--PKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEK----FNYVVM 107
Cdd:cd07861      5 IEKIGEGTYGVVYKGRNKKTGQIVAMKkirLESEEEgvPSTAIR-EISLLKELQHPNIVCLEDVLMQENRlylvFEFLSM 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  108 QLQgRNLADLRRSQPRGTFTLSTTLrlgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQY 183
Cdd:cd07861     84 DLK-KYLDSLPKGKYMDAELVKSYL---YQILQGILFCHSRRVLHRDLKPQNL----LIDNKGVIKLADFGLARAF 151
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
32-259 2.10e-06

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: 50.87  E-value: 2.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRW-------KVLKKIGGGGFGEIYEAMDLLTREnVALKV--ESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKF 102
Cdd:cd05068      1 DQWeidrkslKLLRKLGSGQFGEVWEGLWNNTTP-VAVKTlkPGTMDPEDFLR-EAQIMKKLRHPKLIQLYAVCTLEEPI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 nYVVMQL--QGRNLADLRRsqPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGLA 180
Cdd:cd05068     79 -YIITELmkHGSLLEYLQG--KGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGE----NNICKVADFGLA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQYTNTtgDVRPPRNVAGFrgTVRYASVNAHKNREMGRHDDLWS---LFYMLVEFavGQLPWRKIKDKEQVGMIKEKYeh 257
Cdd:cd05068    152 RVIKVE--DEYEAREGAKF--PIKWTAPEAANYNRFSIKSDVWSfgiLLTEIVTY--GRIPYPGMTNAEVLQQVERGY-- 223

                   ..
gi 1034651883  258 RM 259
Cdd:cd05068    224 RM 225
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
32-292 2.11e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 52.43  E-value: 2.11e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVES----AQQPKQVLKMEVAVLKKLQGKD---HVCRFIGCGrNEKFnY 104
Cdd:PTZ00266    13 NEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISyrglKEREKSQLVIEVNVMRELKHKNivrYIDRFLNKA-NQKL-Y 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQLQgrNLADLRRSQPR-----GTFTLSTTLRLGKQILESIEAIHSVG-------FLHRDIKPSNFAMGRLPSTYRKC 172
Cdd:PTZ00266    91 ILMEFC--DAGDLSRNIQKcykmfGKIEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTGIRHIGKI 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  173 YMLDFGLARQYTNTTGDVRPPRNVA------GFRGTVRYAS--VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKD 244
Cdd:PTZ00266   169 TAQANNLNGRPIAKIGDFGLSKNIGiesmahSCVGTPYYWSpeLLLHETKSYDDKSDMWALGCIIYELCSGKTPFHKANN 248
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  245 KEQvgMIKE-KYEHRMLLKHMPSEFHLFLDHIASLDYFTKPD------YQLIMSV 292
Cdd:PTZ00266   249 FSQ--LISElKRGPDLPIKGKSKELNILIKNLLNLSAKERPSalqclgYQIIKNV 301
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
40-242 2.37e-06

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 50.51  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMdlLTRENVALKVESAQQPKQVLKMEVAVLKKLqgkDH--VCRFIGCGRNEKFNYVVMQ-LQGRNLAD 116
Cdd:cd14058      1 VGRGSFGVVCKAR--WRNQIVAVKIIESESEKKAFEVEVRQLSRV---DHpnIIKLYGACSNQKPVCLVMEyAEGGSLYN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  117 -LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVG---FLHRDIKPSNFAMGRLPSTYRKCymlDFGLA-RQYTNTTGDvr 191
Cdd:cd14058     76 vLHGKEPKPIYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTVLKIC---DFGTAcDISTHMTNN-- 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  192 pprnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKI 242
Cdd:cd14058    151 --------KGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHI 193
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
30-189 2.51e-06

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 51.22  E-value: 2.51e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGR---NEK 101
Cdd:cd07858      3 VDTKYVPIKPIGRGAYGIVCSAKNSETNEKVAIKkianaFDNRIDAKRTLR-EIKLLRHLD-HENVIAIKDIMPpphREA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FN--YVVMQLQGRNLAD-LRRSQPrgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstyRKC--YMLD 176
Cdd:cd07858     81 FNdvYIVYELMDTDLHQiIRSSQT---LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLN------ANCdlKICD 151
                          170
                   ....*....|...
gi 1034651883  177 FGLARQyTNTTGD 189
Cdd:cd07858    152 FGLART-TSEKGD 163
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
38-295 2.54e-06

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: 50.30  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTrENVALKV--ESAQQPKQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFnYVVMQLQGR-NL 114
Cdd:cd14203      1 VKLGQGCFGEVWMGTWNGT-TKVAIKTlkPGTMSPEAFLE-EAQIMKKLR-HDKLVQLYAVVSEEPI-YIVTEFMSKgSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMG-RLpstyrKCYMLDFGLAR-----QYTnttg 188
Cdd:cd14203     77 LDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGdNL-----VCKIADFGLARliednEYT---- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  189 dvrpPRNVAGFrgTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAV-GQLPWRKIKDKEQVGMIKEKYehRMLL-KHMPS 266
Cdd:cd14203    148 ----ARQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGY--RMPCpPGCPE 219
                          250       260
                   ....*....|....*....|....*....
gi 1034651883  267 EFHLFLDHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd14203    220 SLHELMCQCWRKDPEERPTFEYLQSFLED 248
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
38-225 2.63e-06

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: 50.63  E-value: 2.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVL-KMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLAD 116
Cdd:cd14104      6 EELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLvKKEISILNIARHRNILRLHESFESHEELVMIFEFISGVDIFE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  117 lRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLARQytnttgdVRPPRNV 196
Cdd:cd14104     86 -RITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIK--IIEFGQSRQ-------LKPGDKF 155
                          170       180
                   ....*....|....*....|....*....
gi 1034651883  197 AGFRGTVRYASVNAHKNREMGRHDDLWSL 225
Cdd:cd14104    156 RLQYTSAEFYAPEVHQHESVSTATDMWSL 184
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
29-295 2.84e-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: 50.84  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLK-------KIGGGGFGEIYEAM-DLLTRENVALKVESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCgrNE 100
Cdd:cd05069      2 LAKDAWEIPReslrldvKLGQGCFGEVWMGTwNGTTKVAIKTLKPGTMMPEAFLQ-EAQIMKKLRHDKLVPLYAVV--SE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQLQGR-NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGL 179
Cdd:cd05069     79 EPIYIVTEFMGKgSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGD----NLVCKIADFGL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  180 ARQYTNTTGDVRpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAV-GQLPWRKIKDKEQVGMIKEKYehR 258
Cdd:cd05069    155 ARLIEDNEYTAR-----QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGY--R 227
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1034651883  259 MLLKH-MPSEFHLFLDHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd05069    228 MPCPQgCPESLHELMKLCWKKDPDERPTFEYIQSFLED 265
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
40-184 2.89e-06

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: 50.34  E-value: 2.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL-QGRNLadL 117
Cdd:cd14006      1 LGRGRFGVVKRCIEKATGREFAAKfIPKRDKKKEAVLREISILNQLQ-HPRIIQLHEAYESPTELVLILELcSGGEL--L 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  118 RRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLARQYT 184
Cdd:cd14006     78 DRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILL--ADRPSPQIKIIDFGLARKLN 142
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
38-251 3.01e-06

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


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 50.43  E-value: 3.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLL---TRENVALKV----ESAQQPKQVLKmEVAVLKKLqgkDHVC--RFIGCGRNEKFnYVVMQ 108
Cdd:cd05060      1 KELGHGNFGSVRKGVYLMksgKEVEVAVKTlkqeHEKAGKKEFLR-EASVMAQL---DHPCivRLIGVCKGEPL-MLVME 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L--QGRNLADLRRsqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR----- 181
Cdd:cd05060     76 LapLGPLLKYLKK---RREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNV----LLVNRHQAKISDFGMSRalgag 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  182 --QYTNTTGDVRPPRnvagfrgtvRYA--SVNAHKnreMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMI 251
Cdd:cd05060    149 sdYYRATTAGRWPLK---------WYApeCINYGK---FSSKSDVWSYGVTLWEaFSYGAKPYGEMKGPEVIAML 211
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
38-230 3.04e-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: 50.62  E-value: 3.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL-QGR 112
Cdd:cd14097      7 RKLGQGSFGVVIEATHKETQTKWAIKKinreKAGSSAVKLLEREVDILKHVN-HAHIIHLEEVFETPKRMYLVMELcEDG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRL---PSTYRKCYMLDFGLARQYTNTTGD 189
Cdd:cd14097     86 ELKELL--LRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidNNDKLNIKVTDFGLSVQKYGLGED 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034651883  190 VrpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSL---FYMLV 230
Cdd:cd14097    164 M-----LQETCGTPIYMAPEVISAHGYSQQCDIWSIgviMYMLL 202
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
40-191 3.14e-06

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 50.30  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVA---LKVESAQQpKQVLKMEVAVLKKLQgkdHVcRFIGC-----GRNEkfnyVVM---- 107
Cdd:cd14103      1 LGRGKFGTVYRCVEKATGKELAakfIKCRKAKD-REDVRNEIEIMNQLR---HP-RLLQLydafeTPRE----MVLvmey 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 ----QLQGRNLADlrrsqprgTFTLS--TTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLAR 181
Cdd:cd14103     72 vaggELFERVVDD--------DFELTerDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIK--IIDFGLAR 141
                          170
                   ....*....|
gi 1034651883  182 QYtNTTGDVR 191
Cdd:cd14103    142 KY-DPDKKLK 150
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
25-238 3.34e-06

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: 50.84  E-value: 3.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   25 PANYVVKDR-----WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESaqqpkqvlKMEVavLKKlqgKDHVC----RFIG 95
Cdd:cd05596     14 PVNEITKLRmnaedFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLS--------KFEM--IKR---SDSAFfweeRDIM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   96 CGRN-------------EKFNYVVMQ-LQGRNLADLrrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF- 160
Cdd:cd05596     81 AHANsewivqlhyafqdDKYLYMVMDyMPGGDLVNL---MSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMl 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  161 --AMGRLPstyrkcyMLDFGLARQyTNTTGDVRPPRNVagfrGTVRYASVNAHKNRE----MGRHDDLWSLFYMLVEFAV 234
Cdd:cd05596    158 ldASGHLK-------LADFGTCMK-MDKDGLVRSDTAV----GTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLV 225

                   ....
gi 1034651883  235 GQLP 238
Cdd:cd05596    226 GDTP 229
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
35-179 3.67e-06

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 50.04  E-value: 3.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAmdlLTRENVALK---VESAQQPK-QVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL- 109
Cdd:cd14063      3 EIKEVIGKGRFGRVHRG---RWHGDVAIKllnIDYLNEEQlEAFKEEVAAYKNTR-HDNLVLFMGACMDPPHLAIVTSLc 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  110 QGRNLADLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN--FAMGRLPSTyrkcymlDFGL 179
Cdd:cd14063     79 KGRTLYSLIHER-KEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNifLENGRVVIT-------DFGL 142
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
31-238 3.77e-06

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: 50.04  E-value: 3.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQ--VLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd06645     10 QEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDfaVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKcyMLDFGLARQYTNTTG 188
Cdd:cd06645     90 CGGGSLQDIYHVT--GPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILL--TDNGHVK--LADFGVSAQITATIA 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  189 DVRpprnvaGFRGTVRYASVNAHKNREMGRHD---DLWSLFYMLVEFAVGQLP 238
Cdd:cd06645    164 KRK------SFIGTPYWMAPEVAAVERKGGYNqlcDIWAVGITAIELAELQPP 210
PHA03247 PHA03247
large tegument protein UL36; Provisional
1093-1394 4.89e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 4.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1093 PSEMATNSLPNGPAlaDGPAPVSPLEPSPEKVATISPrrhamPGSRPRSRipvllseedtGSEPSGSLSAKERWSKRARP 1172
Cdd:PHA03247  2592 PPQSARPRAPVDDR--GDPRGPAPPSPLPPDTHAPDP-----PPPSPSPA----------ANEPDPHPPPTVPPPERPRD 2654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1173 QQDLARlVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAAlPRKSGRAAATRSRiPRPIGLRMP 1252
Cdd:PHA03247  2655 DPAPGR-VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPE-PAPHALVSATPLP-PGPAAARQA 2731
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1253 MPVAAQQPASRSHGAAPALDTAIT--SSRLQLQTPPGSATAADlRPKQPPGRGLGPGRAQAGARPPAPRSPRLPASTSAA 1330
Cdd:PHA03247  2732 SPALPAAPAPPAVPAGPATPGGPArpARPPTTAGPPAPAPPAA-PAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAA 2810
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883 1331 RNA--SASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAqPDGTPSPGG--SKKGPRGKLQAQRAT 1394
Cdd:PHA03247  2811 VLApaAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLP-LGGSVAPGGdvRRRPPSRSPAAKPAA 2877
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
38-239 5.26e-06

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: 49.82  E-value: 5.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQvlkmEVAVLKKLQGKDHVCRFI---------GCGRNEKFNYVVMQ 108
Cdd:cd14070      8 RKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKK----DSYVTKNLRREGRIQQMIrhpnitqllDILETENSYYLVME 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLarqyTNTT 187
Cdd:cd14070     84 LcPGGNLMH--RIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENL----LLDENDNIKLIDFGL----SNCA 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  188 GDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14070    154 GILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPF 205
PHA03247 PHA03247
large tegument protein UL36; Provisional
1097-1384 5.45e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.48  E-value: 5.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1097 ATNSLPNGPALADGPAPVSPLEPSPEKVATisPRRHAMPGSRPRSRIPVLLSEEDTGSEPSGSLSAKERW-------SKR 1169
Cdd:PHA03247  2634 AANEPDPHPPPTVPPPERPRDDPAPGRVSR--PRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPppppptpEPA 2711
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1170 ARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRksGRAAATRSRIPRPIGL 1249
Cdd:PHA03247  2712 PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPA--APAAGPPRRLTRPAVA 2789
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1250 -------RMPMPVAAQQPASRSHGAAPALDTAITSSRLqLQTPPGSATAADLRPKQPP------GRGLGPG-----RAQA 1311
Cdd:PHA03247  2790 slsesreSLPSPWDPADPPAAVLAPAAALPPAASPAGP-LPPPTSAQPTAPPPPPGPPppslplGGSVAPGgdvrrRPPS 2868
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883 1312 GARPPAPRSPRLPASTSAARNA-SASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSPGGSKKGP 1384
Cdd:PHA03247  2869 RSPAAKPAAPARPPVRRLARPAvSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPP 2942
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
31-260 5.77e-06

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


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 49.97  E-value: 5.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEI-----------YEAMDLLTRENVALKVES-AQQPKQVL-----KMEVAVLKKLQGKDHVCRF 93
Cdd:cd05632      1 KNTFRQYRVLGKGGFGEVcacqvratgkmYACKRLEKKRIKKRKGESmALNEKQILekvnsQFVVNLAYAYETKDALCLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   94 --IGCGRNEKFNYVVMQLQGrnladlrrsqprgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRK 171
Cdd:cd05632     81 ltIMNGGDLKFHIYNMGNPG--------------FEEERALFYAAEILCGLEDLHRENTVYRDLKPENI----LLDDYGH 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  172 CYMLDFGLArqytnttgdVRPPRN--VAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQvg 249
Cdd:cd05632    143 IRISDLGLA---------VKIPEGesIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVK-- 211
                          250
                   ....*....|.
gi 1034651883  250 miKEKYEHRML 260
Cdd:cd05632    212 --REEVDRRVL 220
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
34-292 6.45e-06

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: 49.64  E-value: 6.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALK------VESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd08229     26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKkvqifdLMDAKARADCIK-EIDLLKQLNHPNVIKYYASFIEDNELNIVLE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRR--SQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGLARQYTN 185
Cdd:cd08229    105 LADAGDLSRMIKhfKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFI----TATGVVKLGDLGLGRFFSS 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  186 TTGDVRpprnvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWrkIKDKEQVGMIKEKYEH----RMLL 261
Cdd:cd08229    181 KTTAAH------SLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF--YGDKMNLYSLCKKIEQcdypPLPS 252
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1034651883  262 KHMPSEFHLFLDHIASLDYFTKPDYQLIMSV 292
Cdd:cd08229    253 DHYSEELRQLVNMCINPDPEKRPDITYVYDV 283
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
40-244 6.48e-06

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 49.46  E-value: 6.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPKQ--------VLKMEVAVLKKL---QGKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14101      8 LGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklpgvnPVPNEVALLQSVgggPGHRGVIRLLDWFEIPEGFLLVLE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 --LQGRNLADLrrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCY-MLDFGlarqytn 185
Cdd:cd14101     88 rpQHCQDLFDY--ITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENI----LVDLRTGDIkLIDFG------- 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  186 tTGDVRPPRNVAGFRGTVRYAS---VNAHKNREMGRhdDLWSLFYMLVEFAVGQLPWRKIKD 244
Cdd:cd14101    155 -SGATLKDSMYTDFDGTRVYSPpewILYHQYHALPA--TVWSLGILLYDMVCGDIPFERDTD 213
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
33-233 6.84e-06

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: 49.42  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEiyeamdlltrenvALKVESAQQPKQVL-------KM----------EVAVLKKLQGKDHVcrfig 95
Cdd:cd08218      1 KYVRIKKIGEGSFGK-------------ALLVKSKEDGKQYVikeinisKMspkereesrkEVAVLSKMKHPNIV----- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   96 cGRNEKFN-----YVVMQL-QGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstY 169
Cdd:cd08218     63 -QYQESFEengnlYIVMDYcDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTK----D 137
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  170 RKCYMLDFGLARQYTNTTGDVRPprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFA 233
Cdd:cd08218    138 GIIKLGDFGIARVLNSTVELART------CIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMC 195
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
40-246 6.98e-06

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: 49.53  E-value: 6.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKMEVAVLKKLqgkDHVCRFIGCGRNEKFNYVV-----MQLQG 111
Cdd:cd14039      1 LGTGGFGNVCLYQNQETGEKIAIKscrLELSVKNKDRWCHEIQIMKKL---NHPNVVKACDVPEEMNFLVndvplLAMEY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRR--SQPRGTFTL--STTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM----GRLPSTyrkcyMLDFGLARqy 183
Cdd:cd14039     78 CSGGDLRKllNKPENCCGLkeSQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqeinGKIVHK-----IIDLGYAK-- 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  184 tnttgDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP---------W-RKIKDKE 246
Cdd:cd14039    151 -----DLDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPflhnlqpftWhEKIKKKD 218
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
37-238 7.21e-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: 49.66  E-value: 7.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKV------ESAQQPKQVLKmEVAVLKKLQGKDHVcRFIGCGRNEKFNYVVMQLQ 110
Cdd:cd06635     30 LREIGHGSFGAVYFARDVRTSEVVAIKKmsysgkQSNEKWQDIIK-EVKFLQRIKHPNSI-EYKGCYLREHTAWLVMEYC 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADLRRSQPRGTFTLSTTlRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRkcyMLDFGLArqytnttgDV 190
Cdd:cd06635    108 LGSASDLLEVHKKPLQEIEIA-AITHGALQGLAYLHSHNMIHRDIKAGNILLTE-PGQVK---LADFGSA--------SI 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  191 RPPRNvaGFRGTVRYASVNAHKNREMGRHD---DLWSLFYMLVEFAVGQLP 238
Cdd:cd06635    175 ASPAN--SFVGTPYWMAPEVILAMDEGQYDgkvDVWSLGITCIELAERKPP 223
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
2-311 8.13e-06

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: 50.01  E-value: 8.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883    2 QCLAAALKDETNMSGGGEQA----DILPANYVVKDRWKVLKKIGGGGFGE-----------IYeAMDLLTRENVALKVES 66
Cdd:cd05624     38 ECSHSPLRRDKYVSEFLEWAkpftQLVKEMQLHRDDFEIIKVIGRGAFGEvavvkmknterIY-AMKILNKWEMLKRAET 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   67 AqqpkqVLKMEVAVLkkLQGKdhvCRFIG----CGRNEKFNYVVMQ--LQGRNLADLRRSQPRGTFTLSTtLRLGKQILe 140
Cdd:cd05624    117 A-----CFREERNVL--VNGD---CQWITtlhyAFQDENYLYLVMDyyVGGDLLTLLSKFEDKLPEDMAR-FYIGEMVL- 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  141 SIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQyTNTTGDVRPPRNVagfrGTVRYASVNAHKNRE--MGR 218
Cdd:cd05624    185 AIHSIHQLHYVHRDIKPDNV----LLDMNGHIRLADFGSCLK-MNDDGTVQSSVAV----GTPDYISPEILQAMEdgMGK 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  219 HD---DLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKeKYEHRMllkHMPSefhlfldHIASLDYFTKPDYQLIMSVFEN 295
Cdd:cd05624    256 YGpecDWWSLGVCMYEMLYGETPFYAESLVETYGKIM-NHEERF---QFPS-------HVTDVSEEAKDLIQRLICSRER 324
                          330       340
                   ....*....|....*....|..
gi 1034651883  296 SMKERGIAE------NEAFDWE 311
Cdd:cd05624    325 RLGQNGIEDfkkhafFEGLNWE 346
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
34-180 9.33e-06

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 49.37  E-value: 9.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQVlKMEVAVLKKLQGKD----HVCRFIGCGRNEKFNYVVM 107
Cdd:cd14211      1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIlkNHPSYARQG-QIEVSILSRLSQENadefNFVRAYECFQHKNHTCLVF 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  108 QLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPstYRkCYMLDFGLA 180
Cdd:cd14211     80 EMLEQNLYDFLKQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLvdpVRQP--YR-VKVIDFGSA 152
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
34-238 9.88e-06

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: 48.87  E-value: 9.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPK--QVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQG 111
Cdd:cd06646     11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDdfSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGG 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRR-SQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTGDV 190
Cdd:cd06646     91 GSLQDIYHvTGPLSELQIAYVCR---ETLQGLAYLHSKGKMHRDIKGANI----LLTDNGDVKLADFGVAAKITATIAKR 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  191 RpprnvaGFRGTVRYAS---VNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06646    164 K------SFIGTPYWMApevAAVEKNGGYNQLCDIWAVGITAIELAELQPP 208
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
37-255 1.13e-05

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: 48.60  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMdLLTRENVALKV--ESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFnYVVMQL--QGR 112
Cdd:cd05059      9 LKELGSGQFGVVHLGK-WRGKIDVAIKMikEGSMSEDDFIE-EAKVMMKLSHPKLVQLYGVCTKQRPI-FIVTEYmaNGC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLAR-----QYTNTT 187
Cdd:cd05059     86 LLNYLRER--RGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVV----KVSDFGLARyvlddEYTSSV 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  188 GDVRPprnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKY 255
Cdd:cd05059    160 GTKFP----------VKWSPPEVFMYSKFSSKSDVWSFGVLMWEvFSEGKMPYERFSNSEVVEHISQGY 218
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
38-248 1.20e-05

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: 49.23  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEI----------YEAMDLLTRENVALKVESAQQ--PKQVLKME----VAVLK-KLQGKDHVCrfigcgrne 100
Cdd:cd05595      1 KLLGKGTFGKVilvrekatgrYYAMKILRKEVIIAKDEVAHTvtESRVLQNTrhpfLTALKyAFQTHDRLC--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 kfnyVVMQLQGRNLADLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyrkcymlDF 177
Cdd:cd05595     72 ----FVMEYANGGELFFHLSRER-VFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLdkdGHIKIT-------DF 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  178 GLARQYTNTTGDVRPprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKiKDKEQV 248
Cdd:cd05595    140 GLCKEGITDGATMKT------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHERL 203
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
40-242 1.20e-05

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 48.44  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAmdLLTRENVALKVeSAQQPK-------QVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQG- 111
Cdd:cd14148      2 IGVGGFGKVYKG--LWRGEEVAVKA-ARQDPDediavtaENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGg 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 ---RNLADlRRSQPRGTFTLSTTLRLGKQILESiEAIhsVGFLHRDIKPSNFAM------GRLPSTYRKcyMLDFGLARQ 182
Cdd:cd14148     79 alnRALAG-KKVPPHVLVNWAVQIARGMNYLHN-EAI--VPIIHRDLKSSNILIlepienDDLSGKTLK--ITDFGLARE 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  183 YTNTTGdvrpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKI 242
Cdd:cd14148    153 WHKTTK--------MSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREI 204
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
37-181 1.21e-05

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: 48.80  E-value: 1.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQV---LKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQgRN 113
Cdd:cd07870      5 LEKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVpftAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMH-TD 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  114 LADLRRSQPRGTFTLSTTLRLgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd07870     84 LAQYMIQHPGGLHPYNVRLFM-FQLLRGLAYIHGQHILHRDLKPQNL----LISYLGELKLADFGLAR 146
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
30-272 1.28e-05

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 48.30  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMD--LLTRENVALKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVM 107
Cdd:cd14112      1 PTGRFSFGSEIFRGRFSVIVKAVDstTETDAHCAVKIFEVSDEASEAVREFESLRTLQ-HENVQRLIAAFKPSNFAYLVM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QlqgRNLAD-LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLArQYTNT 186
Cdd:cd14112     80 E---KLQEDvFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVK--LVDFGRA-QKVSK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  187 TGDVRPPrnvagfrGTVRYASVNAHKNRE-MGRHDDLWSLFYMLVEFAVGQLPWRKIKDKE---QVGMIKEKYEHRMLLK 262
Cdd:cd14112    154 LGKVPVD-------GDTDWASPEFHNPETpITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEeetKENVIFVKCRPNLIFV 226
                          250
                   ....*....|
gi 1034651883  263 HMPSEFHLFL 272
Cdd:cd14112    227 EATQEALRFA 236
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
130-274 1.31e-05

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: 48.47  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  130 TTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLARQyTNTTgdvrpprnVAGFRGTVRYAsvn 209
Cdd:cd13987     92 RVKRCAAQLASALDFMHSKNLVHRDIKPENVLL--FDKDCRRVKLCDFGLTRR-VGST--------VKRVSGTIPYT--- 157
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  210 AHKNREMGRHD--------DLWS----LFYMLvefaVGQLPWRKIKDKEQVGMIKEKYEHRmLLKHMPSEFHLFLDH 274
Cdd:cd13987    158 APEVCEAKKNEgfvvdpsiDVWAfgvlLFCCL----TGNFPWEKADSDDQFYEEFVRWQKR-KNTAVPSQWRRFTPK 229
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
29-159 1.33e-05

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 49.08  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAMDLLTR-ENVALK-VESAQQPKQVLKMEVAVLKKLQGKDHVCRFiGCGRN-EKFNY- 104
Cdd:cd14213      9 VLRARYEIVDTLGEGAFGKVVECIDHKMGgMHVAVKiVKNVDRYREAARSEIQVLEHLNTTDPNSTF-RCVQMlEWFDHh 87
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  105 ----VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN 159
Cdd:cd14213     88 ghvcIVFELLGLSTYDFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPEN 146
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
30-253 1.33e-05

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 48.85  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKK-IGGGGFGEIY--EAMDLL-TRENVALKVESAQQP----KQVLKMEVAVLKKLQgKDHVCRFIG-CGRNE 100
Cdd:cd05094      2 IKRRDIVLKReLGEGAFGKVFlaECYNLSpTKDKMLVAVKTLKDPtlaaRKDFQREAELLTNLQ-HDHIVKFYGvCGDGD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQLQGRNLADLRRS-----------QPR---GTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlp 166
Cdd:cd05094     81 PLIMVFEYMKHGDLNKFLRAhgpdamilvdgQPRqakGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVG--- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  167 sTYRKCYMLDFGLAR-----QYTNTTGDVRPPrnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWR 240
Cdd:cd05094    158 -ANLLVKIGDFGMSRdvystDYYRVGGHTMLP---------IRWMPPESIMYRKFTTESDVWSFGVILWEiFTYGKQPWF 227
                          250
                   ....*....|...
gi 1034651883  241 KIKDKEQVGMIKE 253
Cdd:cd05094    228 QLSNTEVIECITQ 240
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
38-248 1.34e-05

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 48.52  E-value: 1.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMdllTRENVALKVESAQQPK----QVLKMEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVMQLQGRN 113
Cdd:cd14151     14 QRIGSGSFGTVYKGK---WHGDVAVKMLNVTAPTpqqlQAFKNEVGVLRKTRHVN-ILLFMGYSTKPQLAIVTQWCEGSS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 L-ADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLARQYTNTTGDvrp 192
Cdd:cd14151     90 LyHHLHIIETK--FEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTV----KIGDFGLATVKSRWSGS--- 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  193 pRNVAGFRGTVRYAS---VNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQV 248
Cdd:cd14151    161 -HQFEQLSGSILWMApevIRMQDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQI 218
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
34-186 1.40e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 48.87  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKqvlkMEVAVLKKLQGKD----HVCRFIGCGRNEKFNY 104
Cdd:cd14229      2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKIlknhpSYARQGQ----IEVGILARLSNENadefNFVRAYECFQHRNHTC 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPstYRkCYMLDFGLAR 181
Cdd:cd14229     78 LVFEMLEQNLYDFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpVRQP--YR-VKVIDFGSAS 154

                   ....*
gi 1034651883  182 QYTNT 186
Cdd:cd14229    155 HVSKT 159
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
40-193 1.48e-05

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 48.40  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK--VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGC-GRNEKFNYVVMQLQGRNLAD 116
Cdd:cd14222      1 LGKGFFGQAIKVTHKATGKVMVMKelIRCDEETQKTFLTEVKVMRSLD-HPNVLKFIGVlYKDKRLNLLTEFIEGGTLKD 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  117 LRRSQPrgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNfAMGRLPSTyrkCYMLDFGLARQYTNTTgdVRPP 193
Cdd:cd14222     80 FLRADD--PFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHN-CLIKLDKT---VVVADFGLSRLIVEEK--KKPP 148
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
31-255 1.51e-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: 48.53  E-value: 1.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLK-------KIGGGGFGEIYEAM-DLLTRENVALKVESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCgrNEKF 102
Cdd:cd05071      1 KDAWEIPReslrlevKLGQGCFGEVWMGTwNGTTRVAIKTLKPGTMSPEAFLQ-EAQVMKKLRHEKLVQLYAVV--SEEP 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 NYVVMQLQGR-NLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFGLAR 181
Cdd:cd05071     78 IYIVTEYMSKgSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGE----NLVCKVADFGLAR 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  182 QYTNTTGDVRpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAV-GQLPWRKIKDKEQVGMIKEKY 255
Cdd:cd05071    154 LIEDNEYTAR-----QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGY 223
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
29-248 1.52e-05

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 48.43  E-value: 1.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYE--AMDLLTRE---NVALKV--ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEK 101
Cdd:cd05061      3 VSREKITLLRELGQGSFGMVYEgnARDIIKGEaetRVAVKTvnESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FNYVVMQLQG--------RNL-ADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNfAMGRLPSTYRkc 172
Cdd:cd05061     83 PTLVVMELMAhgdlksylRSLrPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARN-CMVAHDFTVK-- 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  173 yMLDFGLARQYTNTTGDVRpprnvaGFRG--TVRYASVNAHKNREMGRHDDLWSLFYMLVEF-AVGQLPWRKIKDkEQV 248
Cdd:cd05061    160 -IGDFGMTRDIYETDYYRK------GGKGllPVRWMAPESLKDGVFTTSSDMWSFGVVLWEItSLAEQPYQGLSN-EQV 230
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
30-180 1.56e-05

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


Pssm-ID: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 48.93  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQGKD----HVCRFIGCGRNEKFNY 104
Cdd:cd14228     13 MTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKIlKNHPSYARQGQIEVSILSRLSSENadeyNFVRSYECFQHKNHTC 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  105 VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLA 180
Cdd:cd14228     93 LVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSA 168
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
39-238 1.60e-05

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: 48.05  E-value: 1.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   39 KIGGGGFGEIYEAM-DLLTRENVALKVESAQQPKQV----LKMEVAVLKKLQGKdHVCRFIGCGRNEKFNYVVMQL-QGR 112
Cdd:cd14121      2 KLGSGTYATVYKAYrKSGAREVVAVKCVSKSSLNKAstenLLTEIELLKKLKHP-HIVELKDFQWDEEHIYLIMEYcSGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKcyMLDFGLArQYtnttgdVRP 192
Cdd:cd14121     81 DLSRFIRS--RRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLK--LADFGFA-QH------LKP 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034651883  193 PRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd14121    150 NDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAP 195
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
38-269 1.82e-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: 47.82  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKMEVAVLKKLqgkDH--VCRFIGCGRNEKFNYVVMQL-QG 111
Cdd:cd05041      1 EKIGRGNFGDVYRGVLKPDNTEVAVKtcrETLPPDLKRKFLQEARILKQY---DHpnIVKLIGVCVQKQPIMIVMELvPG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLAD-LRRSQPRgtftlsttLRLGKQILESIEAIHSVGFL------HRDIKPSNFAMGRLPSTyrkcYMLDFGLARQ-- 182
Cdd:cd05041     78 GSLLTfLRKKGAR--------LTVKQLLQMCLDAAAGMEYLesknciHRDLAARNCLVGENNVL----KISDFGMSREee 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  183 ---YTNTTGDVRPPrnvagfrgtVRYASVNAhknREMGRHD---DLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKY 255
Cdd:cd05041    146 dgeYTVSDGLKQIP---------IKWTAPEA---LNYGRYTsesDVWSFGILLWEiFSLGATPYPGMSNQQTREQIESGY 213
                          250
                   ....*....|....*
gi 1034651883  256 ehRM-LLKHMPSEFH 269
Cdd:cd05041    214 --RMpAPELCPEAVY 226
PHA03247 PHA03247
large tegument protein UL36; Provisional
1109-1378 1.83e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 1.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1109 DGPAPVSPLEPSPEKVATISPRRHA----MPGSRPRSRIPVLLSEEDTGSEPSGSLSAKERWSKRARPQQDLARlvmekr 1184
Cdd:PHA03247  2550 DPPPPLPPAAPPAAPDRSVPPPRPAprpsEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHA------ 2623
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1185 qgrllLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKS---GRAAATRSRIPRPIGLRMPMPVAAQQPA 1261
Cdd:PHA03247  2624 -----PDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRArrlGRAAQASSPPQRPRRRAARPTVGSLTSL 2698
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1262 SRSHGAAPALDTAITSSRLQLQTPPGSATAADLRPKQP--------------PGRGLGPGRAQAGARPPAPRSPRLPAST 1327
Cdd:PHA03247  2699 ADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPaapappavpagpatPGGPARPARPPTTAGPPAPAPPAAPAAG 2778
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883 1328 SAARNASASPRSQSLSRRESPSPSHQArpGVPPPRGVPPARAQPDGTPSPG 1378
Cdd:PHA03247  2779 PPRRLTRPAVASLSESRESLPSPWDPA--DPPAAVLAPAAALPPAASPAGP 2827
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
37-248 1.87e-05

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 48.54  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEI----------YEAMDLLTRENVALKVESAQQ--PKQVLK-----MEVAVLKKLQGKDHVCrfigcgrn 99
Cdd:cd05593     20 LKLLGKGTFGKVilvrekasgkYYAMKILKKEVIIAKDEVAHTltESRVLKntrhpFLTSLKYSFQTKDRLC-------- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  100 ekfnYVVMQLQGRNLAdLRRSQPRgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyrkcymlD 176
Cdd:cd05593     92 ----FVMEYVNGGELF-FHLSRER-VFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLdkdGHIKIT-------D 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  177 FGLARQYTNTTGDVRPprnvagFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKiKDKEQV 248
Cdd:cd05593    159 FGLCKEGITDAATMKT------FCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYN-QDHEKL 223
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
34-260 1.92e-05

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: 48.02  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQ-VLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ-L 109
Cdd:cd14185      2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIidKSKLKGKEdMIESEILIIKSLS-HPNIVKLFEVYETEKEIYLILEyV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTnttgd 189
Cdd:cd14185     81 RGGDLFDAIIESVK--FTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYVT----- 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  190 vRPPRNVAgfrGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKI-KDKEQVGMIKEKYEHRML 260
Cdd:cd14185    154 -GPIFTVC---GTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPeRDQEELFQIIQLGHYEFL 221
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
35-238 2.15e-05

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 47.96  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ---PKQV--LKMEVAVLKKLqgkDH--VCRFIGCGRNEKFNYVVM 107
Cdd:cd05580      4 EFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiikLKQVehVLNEKRILSEV---RHpfIVNLLGSFQDDRNLYMVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 Q-LQGRNLAD-LRRSqprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTyrkcymlDFGLARQ 182
Cdd:cd05580     81 EyVPGGELFSlLRRS---GRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLlldSDGHIKIT-------DFGFAKR 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  183 YTNTTGDVrpprnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd05580    151 VKDRTYTL---------CGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPP 197
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
40-267 2.15e-05

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 48.10  E-value: 2.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEI-----------YEAMDLLTRENVALKVES-AQQPKQVL-----KMEVAVLKKLQGKDHVCRFIGC--GRNE 100
Cdd:cd05630      8 LGKGGFGEVcacqvratgkmYACKKLEKKRIKKRKGEAmALNEKQILekvnsRFVVSLAYAYETKDALCLVLTLmnGGDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQLQGRNladlrrsQPRGTFtlsttlrLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLA 180
Cdd:cd05630     88 KFHIYHMGQAGFP-------EARAVF-------YAAEICCGLEDLHRERIVYRDLKPENI----LLDDHGHIRISDLGLA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQytnttgdVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR----KIKDKEQVGMIKEKYE 256
Cdd:cd05630    150 VH-------VPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQqrkkKIKREEVERLVKEVPE 222
                          250       260
                   ....*....|....*....|....
gi 1034651883  257 H-------------RMLLKHMPSE 267
Cdd:cd05630    223 EysekfspqarslcSMLLCKDPAE 246
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
37-241 2.29e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 48.13  E-value: 2.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRN 113
Cdd:cd06616     11 LGEIGRGAFGTVNKMLHKPSGTIMAVKrirSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICMELMDIS 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 LADLRR---SQPRGTFTLSTtlrLGKQILESIEAIH----SVGFLHRDIKPSNFAMGRlpstyRKCYML-DFGLARQYTN 185
Cdd:cd06616     91 LDKFYKyvyEVLDSVIPEEI---LGKIAVATVKALNylkeELKIIHRDVKPSNILLDR-----NGNIKLcDFGISGQLVD 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  186 T---TGDV--RP---PRNVAGFRgtvryaSVNAHKNREmgrhdDLWSLFYMLVEFAVGQLPWRK 241
Cdd:cd06616    163 SiakTRDAgcRPymaPERIDPSA------SRDGYDVRS-----DVWSLGITLYEVATGKFPYPK 215
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
34-239 2.52e-05

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 47.68  E-value: 2.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQV----LKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14163      2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIiDKSGGPEEFiqrfLPRELQIVERLDHKNIIHVYEMLESADGKIYLVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrlpsTYRKCYMLDFGLARQYTNTT 187
Cdd:cd14163     82 LaEDGDVFDCVLHG--GPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-----QGFTLKLTDFGFAKQLPKGG 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  188 GDVRpprnvAGFRGTVRYASVNA-----HKNREmgrhDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14163    155 RELS-----QTFCGSTAYAAPEVlqgvpHDSRK----GDIWSMGVVLYVMLCAQLPF 202
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
137-246 2.61e-05

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 48.47  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  137 QILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKcyMLDFGLARQYTNTTG-DVrpprnVAGFRGTVRYASVNAHKNRE 215
Cdd:PTZ00267   177 QIVLALDEVHSRKMMHRDLKSANIFL--MPTGIIK--LGDFGFSKQYSDSVSlDV-----ASSFCGTPYYLAPELWERKR 247
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034651883  216 MGRHDDLWSLFYMLVEFAVGQLPWRKIKDKE 246
Cdd:PTZ00267   248 YSKKADMWSLGVILYELLTLHRPFKGPSQRE 278
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
56-251 2.92e-05

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: 47.60  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   56 TRENVALKV-----------ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGR-NLADLRRSQPr 123
Cdd:cd14182     27 TRQEYAVKIiditgggsfspEEVQELREATLKEIDILRKVSGHPNIIQLKDTYETNTFFFLVFDLMKKgELFDYLTEKV- 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  124 gTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQytnttgdVRPPRNVAGFRGTV 203
Cdd:cd14182    106 -TLSEKETRKIMRALLEVICALHKLNIVHRDLKPENI----LLDDDMNIKLTDFGFSCQ-------LDPGEKLREVCGTP 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  204 RY-------ASVNAHkNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMI 251
Cdd:cd14182    174 GYlapeiieCSMDDN-HPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMI 227
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
38-181 3.31e-05

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 47.42  E-value: 3.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEA--MDLLTRE-NVALKV--ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIG-CgrNEKFNYVVMQLQg 111
Cdd:cd05056     12 RCIGEGQFGDVYQGvyMSPENEKiAVAVKTckNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGvI--TENPVWIVMELA- 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  112 rNLADLRR--SQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd05056     89 -PLGELRSylQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNV----LVSSPDCVKLGDFGLSR 155
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
36-259 3.54e-05

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: 47.09  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   36 VLKKIGGGGFGEIYEAMDLLTREN-----VALKV---ESAQQPKQVLKM--EVAVLKKL------------QGKDH---V 90
Cdd:cd14076      5 LGRTLGEGEFGKVKLGWPLPKANHrsgvqVAIKLirrDTQQENCQTSKImrEINILKGLthpnivrlldvlKTKKYigiV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   91 CRFIGCGrnEKFNYVvmqLQGRNLADlrrsqprgtftlSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYR 170
Cdd:cd14076     85 LEFVSGG--ELFDYI---LARRRLKD------------SVACRLFAQLISGVAYLHKKGVVHRDLKLENL----LLDKNR 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  171 KCYMLDFGLARQYTNTTGDVrpprnVAGFRGTVRYAS---VNAHKNREmGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQ 247
Cdd:cd14076    144 NLVITDFGFANTFDHFNGDL-----MSTSCGSPCYAApelVVSDSMYA-GRKADIWSCGVILYAMLAGYLPFDDDPHNPN 217
                          250
                   ....*....|..
gi 1034651883  248 VGMIKEKYEHRM 259
Cdd:cd14076    218 GDNVPRLYRYIC 229
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
40-270 3.72e-05

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 47.44  E-value: 3.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK-----VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGcgrnekfnyVVMQLQGRN- 113
Cdd:cd13989      1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqeLSPSDKNRERWCLEVQIMKKLN-HPNVVSARD---------VPPELEKLSp 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 -----LA-------DLRR--SQPRGTFTL--STTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPStyRKCYML-D 176
Cdd:cd13989     71 ndlplLAmeycsggDLRKvlNQPENCCGLkeSEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGG--RVIYKLiD 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  177 FGLARqytnttgDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP---------W-RKIKDKE 246
Cdd:cd13989    149 LGYAK-------ELDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPflpnwqpvqWhGKVKQKK 221
                          250       260
                   ....*....|....*....|....*..
gi 1034651883  247 QvGMIKEKYEHR---MLLKHMPSEFHL 270
Cdd:cd13989    222 P-EHICAYEDLTgevKFSSELPSPNHL 247
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
37-233 3.83e-05

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: 47.34  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKV------ESAQQPKQVLKmEVAVLKKLQGKDHVcRFIGCGRNEKFNYVVMQLQ 110
Cdd:cd06633     26 LHEIGHGSFGAVYFATNSHTNEVVAIKKmsysgkQTNEKWQDIIK-EVKFLQQLKHPNTI-EYKGCYLKDHTAWLVMEYC 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADLRR--SQPRGTFTLSTtlrLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRkcyMLDFGLArqytnttg 188
Cdd:cd06633    104 LGSASDLLEvhKKPLQEVEIAA---ITHGALQGLAYLHSHNMIHRDIKAGNILLTE-PGQVK---LADFGSA-------- 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1034651883  189 DVRPPRNvaGFRGTVRYASVNAHKNREMGRHD---DLWSLFYMLVEFA 233
Cdd:cd06633    169 SIASPAN--SFVGTPYWMAPEVILAMDEGQYDgkvDIWSLGITCIELA 214
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
35-240 3.97e-05

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


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 47.37  E-value: 3.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALK----VESAQQPKQVLkMEVAVLKKlqgkDHVCRFI----GCGRNEKFNYVV 106
Cdd:cd06618     18 ENLGEIGSGTCGQVYKMRHKKTGHVMAVKqmrrSGNKEENKRIL-MDLDVVLK----SHDCPYIvkcyGYFITDSDVFIC 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLADL--RRSQPRGTFTLsttlrlGKQILESIEAIHSV----GFLHRDIKPSNFAMGRLpSTYRKCymlDFGLA 180
Cdd:cd06618     93 MELMSTCLDKLlkRIQGPIPEDIL------GKMTVSIVKALHYLkekhGVIHRDVKPSNILLDES-GNVKLC---DFGIS 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQYTNTTGDVRPprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR 240
Cdd:cd06618    163 GRLVDSKAKTRS----AGCAAYMAPERIDPPDNPKYDIRADVWSLGISLVELATGQFPYR 218
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
134-238 3.99e-05

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 47.51  E-value: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  134 LGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARqYTNTTGDvrpPRNVAgfRGTVRYAS---VNA 210
Cdd:PLN00034   173 VARQILSGIAYLHRRHIVHRDIKPSNL----LINSAKNVKIADFGVSR-ILAQTMD---PCNSS--VGTIAYMSperINT 242
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1034651883  211 HKNRemGRHD----DLWSLFYMLVEFAVGQLP 238
Cdd:PLN00034   243 DLNH--GAYDgyagDIWSLGVSILEFYLGRFP 272
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
56-182 3.99e-05

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: 46.96  E-value: 3.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   56 TRENVALKV-------ESAQQPKQVL---KMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQL-QGRNLADLRRSqprg 124
Cdd:cd14093     27 TGQEFAVKIiditgekSSENEAEELReatRREIEILRQVSGHPNIIELHDVFESPTFIFLVFELcRKGELFDYLTE---- 102
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  125 TFTLS--TTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQ 182
Cdd:cd14093    103 VVTLSekKTRRIMRQLFEAVEFLHSLNIVHRDLKPENI----LLDDNLNVKISDFGFATR 158
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
40-242 4.14e-05

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: 46.96  E-value: 4.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAmdLLTRENVALKV------ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGrn 113
Cdd:cd14145     14 IGIGGFGKVYRA--IWIGDEVAVKAarhdpdEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARG-- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 lADLRRSQPRGTFTLSTTLRLGKQILESIEAIHS---VGFLHRDIKPSNFAM------GRLPSTYRKcyMLDFGLARQYT 184
Cdd:cd14145     90 -GPLNRVLSGKRIPPDILVNWAVQIARGMNYLHCeaiVPVIHRDLKSSNILIlekvenGDLSNKILK--ITDFGLAREWH 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  185 NTTGdvrpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKI 242
Cdd:cd14145    167 RTTK--------MSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGI 216
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
29-279 4.19e-05

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 46.95  E-value: 4.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYE--AMDLLTRE---NVALKV----ESAQQPKQVLkMEVAVLKKLQgKDHVCRFIGCGRN 99
Cdd:cd05032      3 LPREKITLIRELGQGSFGMVYEglAKGVVKGEpetRVAIKTvnenASMRERIEFL-NEASVMKEFN-CHHVVRLLGVVST 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  100 EKFNYVVMQLQGR-NLADLRRSQ--------PRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYR 170
Cdd:cd05032     81 GQPTLVVMELMAKgDLKSYLRSRrpeaennpGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNC----MVAEDL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  171 KCYMLDFGLAR-----QYTNTTGDVRPPrnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVEFA-VGQLPWrKIKD 244
Cdd:cd05032    157 TVKIGDFGMTRdiyetDYYRKGGKGLLP---------VRWMAPESLKDGVFTTKSDVWSFGVVLWEMAtLAEQPY-QGLS 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034651883  245 KEQV------GMIKEKYEH---------RMLLKHMPSEFHLFLDHIASLD 279
Cdd:cd05032    227 NEEVlkfvidGGHLDLPENcpdkllelmRMCWQYNPKMRPTFLEIVSSLK 276
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
35-179 4.67e-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: 47.22  E-value: 4.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGEIYEAMDLLTRENVALKVesaqqpkqVLKMEVavLKKLQgKDHV-------------------CRFig 95
Cdd:cd05599      4 EPLKVIGRGAFGEVRLVRKKDTGHVYAMKK--------LRKSEM--LEKEQ-VAHVraerdilaeadnpwvvklyYSF-- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   96 cgRNEKFNYVVMQ-LQGRNLADL--RRSqprgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLPSTy 169
Cdd:cd05599     71 --QDEENLYLIMEfLPGGDMMTLlmKKD----TLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLlldARGHIKLS- 143
                          170
                   ....*....|
gi 1034651883  170 rkcymlDFGL 179
Cdd:cd05599    144 ------DFGL 147
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
32-255 4.95e-05

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 47.15  E-value: 4.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-------ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNY 104
Cdd:cd14094      3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIvdvakftSSPGLSTEDLKREASICHMLK-HPHIVELLETYSSDGMLY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQ-LQGRNLA--DLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLpSTYRKCYMLDFGLAR 181
Cdd:cd14094     82 MVFEfMDGADLCfeIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASK-ENSAPVKLGGFGVAI 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  182 QYTNTTgdvrpprNVAGFR-GTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKY 255
Cdd:cd14094    161 QLGESG-------LVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKY 228
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
77-267 5.11e-05

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: 46.58  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   77 EVAVLKKLqgkDH--VCRFIGC--GRNEKFNYVVMQLQgrNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLH 152
Cdd:cd14118     64 EIAILKKL---DHpnVVKLVEVldDPNEDNLYMVFELV--DKGAVMEVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIH 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  153 RDIKPSNFAM---GRLPstyrkcyMLDFGLARQY-------TNTTGD--VRPPRNVAGFRGTVRyasvnahknremGRHD 220
Cdd:cd14118    139 RDIKPSNLLLgddGHVK-------IADFGVSNEFegddallSSTAGTpaFMAPEALSESRKKFS------------GKAL 199
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  221 DLWSLFYMLVEFAVGQLPW---------RKIKDKEQV----GMIKEKYEH---RMLLKHmPSE 267
Cdd:cd14118    200 DIWAMGVTLYCFVFGRCPFeddhilglhEKIKTDPVVfpddPVVSEQLKDlilRMLDKN-PSE 261
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
31-233 5.18e-05

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: 46.94  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQV--LKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd06643      4 EDFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELedYMVEIDILASCD-HPNIVKLLDAFYYENNLWILIE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTg 188
Cdd:cd06643     83 FCAGGAVDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNI----LFTLDGDIKLADFGVSAKNTRTL- 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034651883  189 dvrppRNVAGFRGTVRYAS-----VNAHKNREMGRHDDLWSLFYMLVEFA 233
Cdd:cd06643    158 -----QRRDSFIGTPYWMApevvmCETSKDRPYDYKADVWSLGVTLIEMA 202
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
34-251 5.33e-05

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 46.70  E-value: 5.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQ 110
Cdd:cd07836      2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEihlDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMD 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GrnlaDLRR----SQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPstyrkcyMLDFGLARQY 183
Cdd:cd07836     82 K----DLKKymdtHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLInkrGELK-------LADFGLARAF 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  184 ---TNT-TGDV-----RPPRNVAGFRgtVRYASVnahknremgrhdDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMI 251
Cdd:cd07836    151 gipVNTfSNEVvtlwyRAPDVLLGSR--TYSTSI------------DIWSVGCIMAEMITGRPLFPGTNNEDQLLKI 213
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
38-159 5.42e-05

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: 47.05  E-value: 5.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAmdlltrenvALKVESAQQPKQ--VLK-------MEVAVLKKLQ--GKDHVCRFIGC---GRNEKFN 103
Cdd:cd14013      1 KKLGEGGFGTVYKG---------SLLQKDPGGEKRrvVLKkakeygeVEIWMNERVRraCPSSCAEFVGAfldTTSKKFT 71
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  104 ----YVVMQLQG-RNLADL-----------------RRSQPRGTFTLSTTLR-LGKQILESIEAIHSVGFLHRDIKPSN 159
Cdd:cd14013     72 kpslWLVWKYEGdATLADLmqgkefpynlepiifgrVLIPPRGPKRENVIIKsIMRQILVALRKLHSTGIVHRDVKPQN 150
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
40-159 5.83e-05

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 46.56  E-value: 5.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIG-CGRNEKFNYVVMQLQGRNLad 116
Cdd:cd14174     10 LGEGAYAKVQGCVSLQNGKEYAVKIieKNAGHSRSRVFREVETLYQCQGNKNILELIEfFEDDTRFYLVFEKLRGGSI-- 87
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1034651883  117 LRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSN 159
Cdd:cd14174     88 LAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPEN 130
BREX_PglW NF033442
BREX system serine/threonine kinase PglW; Members of this family are PglW, a predicted serine ...
32-205 6.54e-05

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


Pssm-ID: 468028 [Multi-domain]  Cd Length: 1387  Bit Score: 47.64  E-value: 6.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGfgeiyEAMDLLTRENVA------LKVESAQQPKQVLKMEVAVLKKLQGkDHVCRFIGcGRNEKFNYV 105
Cdd:NF033442   510 GGFEVRRRLGTGS-----TSRALLVRDRDAdgeervLKVALDDEHAARLRAEAEVLGRLRH-PRIVALVE-GPLEIGGRT 582
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQ---GRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQ 182
Cdd:NF033442   583 ALLLEyagEQTLAERLRKE--GRLSLDLLERFGDDLLSAVVHLEGQGVWHRDIKPDNIGIRPRPSRTLHLVLFDFSLAGA 660
                          170       180
                   ....*....|....*....|...
gi 1034651883  183 ytnttgdvrPPRNVAGfrGTVRY 205
Cdd:NF033442   661 ---------PADNIEA--GTPGY 672
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
34-246 6.59e-05

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 46.10  E-value: 6.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQ-------VLKMEVAVLKKL-QGKDHVCRFIGCGRNEKFNYV 105
Cdd:cd14102      2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEwgtlngvMVPLEIVLLKKVgSGFRGVIKLLDWYERPDGFLI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQLQ--GRNLADLrrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRkcyMLDFGLARQY 183
Cdd:cd14102     82 VMERPepVKDLFDF--ITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGELK---LIDFGSGALL 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  184 TNTTgdvrpprnVAGFRGTVRYAS---VNAHknREMGRHDDLWSLFYMLVEFAVGQLPWRkiKDKE 246
Cdd:cd14102    157 KDTV--------YTDFDGTRVYSPpewIRYH--RYHGRSATVWSLGVLLYDMVCGDIPFE--QDEE 210
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
38-179 6.74e-05

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


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 46.11  E-value: 6.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQvLKM------EVAVLKKLQgKDHVCR----------------FIG 95
Cdd:cd14079      8 KTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKS-LDMeekirrEIQILKLFR-HPHIIRlyevietptdifmvmeYVS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   96 CGrnEKFNYVVmqLQGRnladLRRSQPRgtftlsttlRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYML 175
Cdd:cd14079     86 GG--ELFDYIV--QKGR----LSEDEAR---------RFFQQIISGVEYCHRHMVVHRDLKPENLLLDS----NMNVKIA 144

                   ....
gi 1034651883  176 DFGL 179
Cdd:cd14079    145 DFGL 148
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
35-241 7.10e-05

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


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 46.10  E-value: 7.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   35 KVLKKIGGGGFGE--IYEAMDllTRENVALKVESAQqpKQVLKMEVA-VLKK---LQGKDH--VCRFIGCGRNEKFNYVV 106
Cdd:cd05578      3 QILRVIGKGSFGKvcIVQKKD--TKKMFAMKYMNKQ--KCIEKDSVRnVLNEleiLQELEHpfLVNLWYSFQDEEDMYMV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRnlADLR-RSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQytn 185
Cdd:cd05578     79 VDLLLG--GDLRyHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNI----LLDEQGHVHITDFNIATK--- 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  186 ttgdVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSL---FYmlvEFAVGQLPWRK 241
Cdd:cd05578    150 ----LTDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLgvtAY---EMLRGKRPYEI 201
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
145-238 7.60e-05

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 46.27  E-value: 7.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  145 IHSVgfLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTGDvrpprnvaGFRGTVRYASvnahKNREMGRH----D 220
Cdd:cd06615    118 KHKI--MHRDVKPSNI----LVNSRGEIKLCDFGVSGQLIDSMAN--------SFVGTRSYMS----PERLQGTHytvqS 179
                           90
                   ....*....|....*...
gi 1034651883  221 DLWSLFYMLVEFAVGQLP 238
Cdd:cd06615    180 DIWSLGLSLVEMAIGRYP 197
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
37-238 7.74e-05

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: 46.55  E-value: 7.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALKV------ESAQQPKQVLKmEVAVLKKLQGKDHVcRFIGCGRNEKFNYVVMQLQ 110
Cdd:cd06634     20 LREIGHGSFGAVYFARDVRNNEVVAIKKmsysgkQSNEKWQDIIK-EVKFLQKLRHPNTI-EYRGCYLREHTAWLVMEYC 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 GRNLADLRRSQPRGTFTLSTTlRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRkcyMLDFGLArqytnttgDV 190
Cdd:cd06634     98 LGSASDLLEVHKKPLQEVEIA-AITHGALQGLAYLHSHNMIHRDVKAGNILLTE-PGLVK---LGDFGSA--------SI 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  191 RPPRNvaGFRGTVRYASVNAHKNREMGRHD---DLWSLFYMLVEFAVGQLP 238
Cdd:cd06634    165 MAPAN--SFVGTPYWMAPEVILAMDEGQYDgkvDVWSLGITCIELAERKPP 213
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
40-164 7.78e-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: 45.88  E-value: 7.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK---VES-AQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ-LQGRNL 114
Cdd:cd08220      8 VGRGAYGTVYLCRRKDDNKLVIIKqipVEQmTKEERQAALNEVKVLSMLH-HPNIIEYYESFLEDKALMIVMEyAPGGTL 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGR 164
Cdd:cd08220     87 FEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNK 136
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
30-180 8.63e-05

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 46.62  E-value: 8.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQGKD----HVCRFIGCGRNEKFNY 104
Cdd:cd14227     13 MTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKIlKNHPSYARQGQIEVSILARLSTESaddyNFVRAYECFQHKNHTC 92
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  105 VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLA 180
Cdd:cd14227     93 LVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSA 168
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
32-239 8.77e-05

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 45.79  E-value: 8.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK---VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14088      1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKkflKRDGRKVRKAAKNEINILKMVK-HPNILQLVDVFETRKEYFIFLE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L-QGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFA-MGRLPSTyrKCYMLDFGLARQytnT 186
Cdd:cd14088     80 LaTGREVFDWILDQ--GYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyYNRLKNS--KIVISDFHLAKL---E 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  187 TGDVRPPrnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14088    153 NGLIKEP------CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPF 199
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
30-184 9.44e-05

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 45.75  E-value: 9.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGF-GEIYEAMDLLTRENVALKVeSAQQPKQvlKMEVAVLKKLQGKDHVCRFIGCGRN----EKFNY 104
Cdd:cd14172      1 VTDDYKLSKQVLGLGVnGKVLECFHRRTGQKCALKL-LYDSPKA--RREVEHHWRASGGPHIVHILDVYENmhhgKRCLL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQ-LQGRNLadLRRSQPRG--TFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYML---DFG 178
Cdd:cd14172     78 IIMEcMEGGEL--FSRIQERGdqAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENL----LYTSKEKDAVLkltDFG 151

                   ....*.
gi 1034651883  179 LARQYT 184
Cdd:cd14172    152 FAKETT 157
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
40-268 9.73e-05

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 45.98  E-value: 9.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGC-----GRNEKFNYVVMQLQGRNL 114
Cdd:cd05577      1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSlayafETKDKLCLVLTLMNGGDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARqytnttgDVRPPR 194
Cdd:cd05577     81 KYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENI----LLDDHGHVRISDLGLAV-------EFKGGK 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  195 NVAGFRGTVRYASVNAHKNREMGRHD-DLWSLFYMLVEFAVGQLPWRKIKDKeqvgmiKEKYEHRMLLKHMPSEF 268
Cdd:cd05577    150 KIKGRVGTHGYMAPEVLQKEVAYDFSvDWFALGCMLYEMIAGRSPFRQRKEK------VDKEELKRRTLEMAVEY 218
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
40-270 9.98e-05

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: 45.93  E-value: 9.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQV----LKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLqGRNL 114
Cdd:cd14165      9 LGEGSYAKVKSAYSERLKCNVAIKiIDKKKAPDDFvekfLPRELEILARLNHKSIIKTYEIFETSDGKVYIVMEL-GVQG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQY-TNTTGDVRPP 193
Cdd:cd14165     88 DLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENL----LLDKDFNIKLTDFGFSKRClRDENGRIVLS 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  194 RNvagFRGTVRYAS--VNAHKNREMGRHdDLWSLFYMLVEFAVGQLPWRKIKDKEqvgMIKEKYEHRMllkHMPSEFHL 270
Cdd:cd14165    164 KT---FCGSAAYAApeVLQGIPYDPRIY-DIWSLGVILYIMVCGSMPYDDSNVKK---MLKIQKEHRV---RFPRSKNL 232
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
32-267 1.20e-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: 45.84  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQ----PKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFNyVVM 107
Cdd:cd07869      5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEeegtPFTAIR-EASLLKGLKHANIVLLHDIIHTKETLT-LVF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQGRNLADLRRSQPRGTFTLSTTLRLgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR------ 181
Cdd:cd07869     83 EYVHTDLCQYMDKHPGGLHPENVKLFL-FQLLRGLSYIHQRYILHRDLKPQNL----LISDTGELKLADFGLARaksvps 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  182 -QYTNTTGDV--RPPRNVAgfrGTVRYASVNahknremgrhdDLWSLFYMLVEFAVGQLPWRKIKDkeqvgmIKEKYEHR 258
Cdd:cd07869    158 hTYSNEVVTLwyRPPDVLL---GSTEYSTCL-----------DMWGVGCIFVEMIQGVAAFPGMKD------IQDQLERI 217

                   ....*....
gi 1034651883  259 MLLKHMPSE 267
Cdd:cd07869    218 FLVLGTPNE 226
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
40-239 1.22e-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: 45.45  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAmdLLTRENVALKVESAQQPK----QVLKMEVAVLKkLQgKDHVCRFIG---CGRNEKFNYVVMQLQG- 111
Cdd:cd13979     11 LGSGGFGSVYKA--TYKGETVAVKIVRRRRKNrasrQSFWAELNAAR-LR-HENIVRVLAaetGTDFASLGLIIMEYCGn 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLrrsqprgTFTLSTTLRLGKQILESIEAI------HSVGFLHRDIKPSNFAMgrlpSTYRKCYMLDFGlARQYTN 185
Cdd:cd13979     87 GTLQQL-------IYEGSEPLPLAHRILISLDIAralrfcHSHGIVHLDVKPANILI----SEQGVCKLCDFG-CSVKLG 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  186 TTGDVRPPRNvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd13979    155 EGNEVGTPRS--HIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPY 206
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
40-193 1.25e-04

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 45.48  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKV---ESAQQPKQVLKmEVAVLKKLQGKDHVCRFIG-CGRNEKFNYVVMQLQGRNLa 115
Cdd:cd14090     10 LGEGAYASVQTCINLYTGKEYAVKIiekHPGHSRSRVFR-EVETLHQCQGHPNILQLIEyFEDDERFYLVFEKMRGGPL- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  116 dLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNF---AMGRLpSTYRKCymlDFGLARQYTNTTGDVRP 192
Cdd:cd14090     88 -LSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENIlceSMDKV-SPVKIC---DFDLGSGIKLSSTSMTP 162

                   .
gi 1034651883  193 P 193
Cdd:cd14090    163 V 163
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
38-257 1.27e-04

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


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 45.71  E-value: 1.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEI----------YEAMDLLTRENVALK--VESAQQPKQVLKM--EVAVLKKL----QGKDHVcrfigcgrn 99
Cdd:cd05620      1 KVLGKGSFGKVllaelkgkgeYFAVKALKKDVVLIDddVECTMVEKRVLALawENPFLTHLyctfQTKEHL--------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  100 ekfnYVVMQ-LQGRNLadLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFG 178
Cdd:cd05620     72 ----FFVMEfLNGGDL--MFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDR----DGHIKIADFG 141
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  179 LARQytNTTGDVRpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEH 257
Cdd:cd05620    142 MCKE--NVFGDNR----ASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPH 214
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
30-253 1.31e-04

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 45.53  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKK-IGGGGFGEIY--EAMDLLTREN---VALKV---ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIG-CGRN 99
Cdd:cd05049      2 IKRDTIVLKReLGEGAFGKVFlgECYNLEPEQDkmlVAVKTlkdASSPDARKDFEREAELLTNLQ-HENIVKFYGvCTEG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  100 EKFNYVVMQLQGRNLADLRRS------------QPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlps 167
Cdd:cd05049     81 DPLLMVFEYMEHGDLNKFLRShgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVG---- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  168 tyrkCYML----DFGLARQ-YTNTTgdvrppRNVAGFRG-TVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWR 240
Cdd:cd05049    157 ----TNLVvkigDFGMSRDiYSTDY------YRVGGHTMlPIRWMPPESILYRKFTTESDVWSFGVVLWEiFTYGKQPWF 226
                          250
                   ....*....|...
gi 1034651883  241 KIKDKEQVGMIKE 253
Cdd:cd05049    227 QLSNTEVIECITQ 239
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
39-256 1.40e-04

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: 45.57  E-value: 1.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   39 KIGGGGFGEIYEAMdlLTRENVALK------VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRN-EKFNYVVMQLQG 111
Cdd:cd14158     22 KLGEGGFGVVFKGY--INDKNVAVKklaamvDISTEDLTKQFEQEIQVMAKCQ-HENLVELLGYSCDgPQLCLVYTYMPN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADlRRSQPRGTFTLSTTLR--LGKQILESIEAIHSVGFLHRDIKPSNFAM--GRLPStyrkcyMLDFGLARQYTNTT 187
Cdd:cd14158     99 GSLLD-RLACLNDTPPLSWHMRckIAQGTANGINYLHENNHIHRDIKSANILLdeTFVPK------ISDFGLARASEKFS 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  188 GDVRPPRNVagfrGTVRYASVNAHKNrEMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYE 256
Cdd:cd14158    172 QTIMTERIV----GTTAYMAPEALRG-EITPKSDIFSFGVVLLEIITGLPPVDENRDPQLLLDIKEEIE 235
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
27-238 1.57e-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: 45.36  E-value: 1.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   27 NYVVKDrwkvlkKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKqvLKMEVAVLKKLQGKDhVCRFIGCGRNEKFNYV 105
Cdd:cd14010      1 NYVLYD------EIGRGKHSVVYKGRRKGTIEFVAIKcVDKSKRPE--VLNEVRLTHELKHPN-VLKFYEWYETSNHLWL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQL-QGRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLpstyRKCymlDFGLAR 181
Cdd:cd14010     72 VVEYcTGGDLETLLRQD--GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLdgnGTL----KLS---DFGLAR 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  182 ----------QYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd14010    143 regeilkelfGQFSDEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPP 209
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
37-238 1.65e-04

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 45.11  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQP---KQVLKmEVAVLKKLQgKDHVCRFIGCGRNEKFN--YVVMQ-L 109
Cdd:cd06621      6 LSSLGEGAGGSVTKCRLRNTKTIFALKtITTDPNPdvqKQILR-ELEINKSCA-SPYIVKYYGAFLDEQDSsiGIAMEyC 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 QGRNL-ADLRRSQPRGTFTLSTTL-RLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRKCymlDFGLARQYTNTt 187
Cdd:cd06621     84 EGGSLdSIYKKVKKKGGRIGEKVLgKIAESVLKGLSYLHSRKIIHRDIKPSNILLTR-KGQVKLC---DFGVSGELVNS- 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  188 gdvrpprnVAG-FRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06621    159 --------LAGtFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFP 202
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
104-185 1.84e-04

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: 43.41  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQ-LQGRNLADLRRSQPRgtftlstTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstyRKCYMLDFGLARQ 182
Cdd:COG3642     32 DLVMEyIEGETLADLLEEGEL-------PPELLRELGRLLARLHRAGIVHGDLTTSNILVDD-----GGVYLIDFGLARY 99

                   ...
gi 1034651883  183 YTN 185
Cdd:COG3642    100 SDP 102
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
32-239 2.05e-04

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


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 45.03  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGF-GEIYEAMDLLTRENVALKVESaQQPKQvlKMEVAVLKKLQGKDHVCRFIGCGRN----EKFNYVV 106
Cdd:cd14170      1 DDYKVTSQVLGLGInGKVLQIFNKRTQEKFALKMLQ-DCPKA--RREVELHWRASQCPHIVRIVDVYENlyagRKCLLIV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQ-LQGRNLadLRRSQPRG--TFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFA-MGRLPSTYRKcyMLDFGLARQ 182
Cdd:cd14170     78 MEcLDGGEL--FSRIQDRGdqAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLyTSKRPNAILK--LTDFGFAKE 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  183 YTNTTGDVRPPRnvagfrgTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14170    154 TTSHNSLTTPCY-------TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPF 203
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
28-181 2.12e-04

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


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 44.76  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   28 YVVKdrWKvlKKIGGGGFGEIYEAMDLLTRENVALKVeSAQQPKQvlKMEVAVLKKLQGKDHVCRFIGCGRNE------- 100
Cdd:cd14171      6 YEVN--WT--QKLGTGISGPVRVCVKKSTGERFALKI-LLDRPKA--RTEVRLHMMCSGHPNIVQIYDVYANSvqfpges 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 ---KFNYVVMQL-QGRNLADlRRSQPRGtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgRLPSTYRKCYMLD 176
Cdd:cd14171     79 sprARLLIVMELmEGGELFD-RISQHRH-FTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLL-KDNSEDAPIKLCD 155

                   ....*
gi 1034651883  177 FGLAR 181
Cdd:cd14171    156 FGFAK 160
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
37-267 2.20e-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: 44.49  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGEI--------YEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGkdhVCRfigcgrNEKFNYVVMQ 108
Cdd:cd05113      9 LKELGTGQFGVVkygkwrgqYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYG---VCT------KQRPIFIITE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 L--QGRNLADLRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkcYMLDFGLAR----- 181
Cdd:cd05113     80 YmaNGCLLNYLREMRKR--FQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVV----KVSDFGLSRyvldd 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  182 QYTNTTGDVRPprnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKyeHRML 260
Cdd:cd05113    154 EYTSSVGSKFP----------VRWSPPEVLMYSKFSSKSDVWAFGVLMWEvYSLGKMPYERFTNSETVEHVSQG--LRLY 221

                   ....*..
gi 1034651883  261 LKHMPSE 267
Cdd:cd05113    222 RPHLASE 228
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
32-254 2.53e-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: 44.70  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEI----------YEAMDLLTREN-VALK-VESAQQPKQVLK-MEVAVLKKLqgkdhVCRFigcgR 98
Cdd:cd14209      1 DDFDRIKTLGTGSFGRVmlvrhketgnYYAMKILDKQKvVKLKqVEHTLNEKRILQaINFPFLVKL-----EYSF----K 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   99 NEKFNYVVMQL--QGRNLADLRR----SQPRGTFtlsttlrLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTy 169
Cdd:cd14209     72 DNSNLYMVMEYvpGGEMFSHLRRigrfSEPHARF-------YAAQIVLAFEYLHSLDLIYRDLKPENLLIdqqGYIKVT- 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  170 rkcymlDFGLARQYTNTTGDVrpprnvagfRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWrkikDKEQVG 249
Cdd:cd14209    144 ------DFGFAKRVKGRTWTL---------CGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPF----FADQPI 204

                   ....*
gi 1034651883  250 MIKEK 254
Cdd:cd14209    205 QIYEK 209
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
39-253 2.54e-04

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 44.55  E-value: 2.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   39 KIGGGGFGEIYEAMDLLTRE--NVALKVESAQQPKQV---LKMEVAVLKKLQGKdHVCRFIGCGRNEKFnYVVMQLQGRN 113
Cdd:cd05115     11 ELGSGNFGCVKKGVYKMRKKqiDVAIKVLKQGNEKAVrdeMMREAQIMHQLDNP-YIVRMIGVCEAEAL-MLVMEMASGG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  114 LADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKcyMLDFGLARQ-------YTNT 186
Cdd:cd05115     89 PLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLL--VNQHYAK--ISDFGLSKAlgaddsyYKAR 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  187 TGDVRPPRNVAGfrgtvryASVNAHKnreMGRHDDLWSL-FYMLVEFAVGQLPWRKIKDKEQVGMIKE 253
Cdd:cd05115    165 SAGKWPLKWYAP-------ECINFRK---FSSRSDVWSYgVTMWEAFSYGQKPYKKMKGPEVMSFIEQ 222
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
32-239 2.74e-04

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 45.01  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKV--ESAQQPKQvlkmEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQL 109
Cdd:cd14176     19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIidKSKRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  110 -QGRNLAD--LRR---SQPRGTFTLSTtlrlgkqILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTYRKCymlDFGLA 180
Cdd:cd14176     95 mKGGELLDkiLRQkffSEREASAVLFT-------ITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRIC---DFGFA 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  181 RQYTNTTGDVRPPRNVAGFrgtvryASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14176    165 KQLRAENGLLMTPCYTANF------VAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF 217
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
38-253 2.75e-04

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 44.65  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIY--EAMDLLTREN---VALKV--ESAQQPKQVLKMEVAVLKKLQgKDHVCRFIG-CGRNEK----FNYV 105
Cdd:cd05093     11 RELGEGAFGKVFlaECYNLCPEQDkilVAVKTlkDASDNARKDFHREAELLTNLQ-HEHIVKFYGvCVEGDPlimvFEYM 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 -------VMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpstYRKCYMLDFG 178
Cdd:cd05093     90 khgdlnkFLRAHGPDAVLMAEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGE----NLLVKIGDFG 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  179 LAR-----QYTNTTGDVRPPrnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIK 252
Cdd:cd05093    166 MSRdvystDYYRVGGHTMLP---------IRWMPPESIMYRKFTTESDVWSLGVVLWEiFTYGKQPWYQLSNNEVIECIT 236

                   .
gi 1034651883  253 E 253
Cdd:cd05093    237 Q 237
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
31-159 3.13e-04

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 45.17  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAM----DLLTRENVALK-------VESAQQ-------PKQVLKMEVAVLKKLQGKDH--- 89
Cdd:PLN03225   131 KDDFVLGKKLGEGAFGVVYKASlvnkQSKKEGKYVLKkateygaVEIWMNervrracPNSCADFVYGFLEPVSSKKEdey 210
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883   90 --VCRFIGCG------RNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRlgkQILESIEAIHSVGFLHRDIKPSN 159
Cdd:PLN03225   211 wlVWRYEGEStladlmQSKEFPYNVEPYLLGKVQDLPKGLERENKIIQTIMR---QILFALDGLHSTGIVHRDVKPQN 285
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
40-238 3.43e-04

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 44.05  E-value: 3.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIG-CGRNEKFNYVVMQLQGRNLADL- 117
Cdd:cd14156      1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKIVREISLLQKLS-HPNIVRYLGiCVKDEKLHPILEYVSGGCLEELl 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  118 -RRSQPrgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNfAMGRLPSTYRKCYMLDFGLARQytntTGDVRP--PR 194
Cdd:cd14156     80 aREELP---LSWREKVELACDISRGMVYLHSKNIYHRDLNSKN-CLIRVTPRGREAVVTDFGLARE----VGEMPAndPE 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034651883  195 NVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFaVGQLP 238
Cdd:cd14156    152 RKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEI-LARIP 194
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
29-252 3.66e-04

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 44.24  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAMD-LLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNY-- 104
Cdd:cd14215      9 WLQERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIiKNVEKYKEAARLEINVLEKINEKDPENKNLCVQMFDWFDYhg 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 ---VVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLAR 181
Cdd:cd14215     89 hmcISFELLGLSTFDFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILF--VNSDYELTYNLEKKRDE 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  182 QYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNR------EMGRHD--DLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIK 252
Cdd:cd14215    167 RSVKSTAIRVVDFGSATFDHEHHSTIVSTRHYRapevilELGWSQpcDVWSIGCIIFEYYVGFTLFQTHDNREHLAMME 245
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
39-239 3.88e-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: 44.21  E-value: 3.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   39 KIGGGGFGEIYEAMDLLTRENVALKVES--AQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFnYVVMQ-LQGRNLA 115
Cdd:cd06659     28 KIGEGSTGVVCIAREKHSGRQVAVKMMDlrKQQRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEEL-WVLMEyLQGGALT 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  116 DLRrSQPRGTFTLSTTLRlgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNttgDVrPPRN 195
Cdd:cd06659    107 DIV-SQTRLNEEQIATVC--EAVLQALAYLHSQGVIHRDIKSDSI----LLTLDGRVKLSDFGFCAQISK---DV-PKRK 175
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1034651883  196 vaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd06659    176 --SLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPY 217
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1222-1381 4.85e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.84  E-value: 4.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1222 ASEPAAAlprkSGRAAATRSRIPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSSrlqlqTPPGSATAADLRPKQPPG 1301
Cdd:PRK07003   357 AFEPAVT----GGGAPGGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAA-----LAPKAAAAAAATRAEAPP 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1302 RglGPGRAQAGARPPAPRSPRLPASTSAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSPGGSK 1381
Cdd:PRK07003   428 A--APAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPA 505
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
133-238 5.05e-04

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 43.89  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  133 RLGKQILE--SIEAIHSVGFL-------HRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTNTTGDvrpprnvaGFRGTV 203
Cdd:cd06650     99 RIPEQILGkvSIAVIKGLTYLrekhkimHRDVKPSNI----LVNSRGEIKLCDFGVSGQLIDSMAN--------SFVGTR 166
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1034651883  204 RYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd06650    167 SYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYP 201
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
38-255 5.69e-04

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: 43.42  E-value: 5.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAM-DLLTRENVA-----LKVESAQQPKQVLKMEVAVLKKLQGKDhVCRFIGCGRNEKFNYVVMQLQG 111
Cdd:cd05063     11 KVIGAGEFGEVFRGIlKMPGRKEVAvaiktLKPGYTEKQRQDFLSEASIMGQFSHHN-IIRLEGVVTKFKPAMIITEYME 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  112 RNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR--------QY 183
Cdd:cd05063     90 NGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNI----LVNSNLECKVSDFGLSRvleddpegTY 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  184 TNTTGDVrpprnvagfrgTVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKY 255
Cdd:cd05063    166 TTSGGKI-----------PIRWTAPEAIAYRKFTSASDVWSFGIVMWEvMSFGERPYWDMSNHEVMKAINDGF 227
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
34-252 5.90e-04

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: 43.31  E-value: 5.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKV-----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd14164      2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIvdrrrASPDFVQKFLPRELSILRRVNHPNIVQMFECIEVANGRLYIVME 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  109 LQGRNLadLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTYRKCYMLDFGLARQYTNttg 188
Cdd:cd14164     82 AAATDL--LQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENIL---LSADDRKIKIADFGFARFVED--- 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  189 dvrPPRNVAGFRGTVRYAS--VNAHKNREMGRHdDLWSLFYMLVEFAVGQLPWrkikDKEQVGMIK 252
Cdd:cd14164    154 ---YPELSTTFCGSRAYTPpeVILGTPYDPKKY-DVWSLGVVLYVMVTGTMPF----DETNVRRLR 211
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
32-239 6.31e-04

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: 43.42  E-value: 6.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEI----------YEAMDLLTRENVALKV---------------ESAQQPKQVLK---MEVAVLKK 83
Cdd:cd14199      2 NQYKLKDEIGKGSYGVVklayneddntYYAMKVLSKKKLMRQAgfprrppprgaraapEGCTQPRGPIErvyQEIAILKK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   84 LqgkDH--VCRFIGC--GRNEKFNYVVMQLQGR-------NLADLRRSQPRGTFtlsttlrlgKQILESIEAIHSVGFLH 152
Cdd:cd14199     82 L---DHpnVVKLVEVldDPSEDHLYMVFELVKQgpvmevpTLKPLSEDQARFYF---------QDLIKGIEYLHYQKIIH 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  153 RDIKPSNFAMGRlpSTYRKcyMLDFGLARQYTNTTGDVrppRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEF 232
Cdd:cd14199    150 RDVKPSNLLVGE--DGHIK--IADFGVSNEFEGSDALL---TNTVGTPAFMAPETLSETRKIFSGKALDVWAMGVTLYCF 222

                   ....*..
gi 1034651883  233 AVGQLPW 239
Cdd:cd14199    223 VFGQCPF 229
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
137-238 6.51e-04

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: 43.45  E-value: 6.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  137 QILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLARQYtNTTGDVRPPRNVagfrGTVRY------ASVNA 210
Cdd:cd05601    110 ELVLAIHSLHSMGYVHRDIKPENILIDR--TGHIK--LADFGSAAKL-SSDKTVTSKMPV----GTPDYiapevlTSMNG 180
                           90       100
                   ....*....|....*....|....*...
gi 1034651883  211 HKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd05601    181 GSKGTYGVECDWWSLGIVAYEMLYGKTP 208
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
37-266 6.90e-04

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: 43.31  E-value: 6.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFGeIYEAMDLLTRENVALKV--ESAQQPKQVLKmEVAVLKKLQGKDHVCRFIGCGRNEKFnYVVMQL--QGR 112
Cdd:cd05114      9 MKELGSGLFG-VVRLGKWRAQYKVAIKAirEGAMSEEDFIE-EAKVMMKLTHPKLVQLYGVCTQQKPI-YIVTEFmeNGC 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  113 NLADLRrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR-----QYTNTT 187
Cdd:cd05114     86 LLNYLR--QRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNC----LVNDTGVVKVSDFGMTRyvlddQYTSSS 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  188 GDVRPprnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKEQVGMIKEKyeHRMLLKHMPS 266
Cdd:cd05114    160 GAKFP----------VKWSPPEVFNYSKFSSKSDVWSFGVLMWEvFTEGKMPFESKSNYEVVEMVSRG--HRLYRPKLAS 227
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
38-246 7.36e-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: 43.20  E-value: 7.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKVES--AQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ-LQGRNL 114
Cdd:cd06648     13 VKIGEGSTGIVCIATDKSTGRQVAVKKMDlrKQQRRELLFNEVVIMRDYQ-HPNIVEMYSSYLVGDELWVVMEfLEGGAL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  115 ADL----RRSQPRgtftLSTTLRlgkQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyrkcymlDFGLARQytnTT 187
Cdd:cd06648     92 TDIvthtRMNEEQ----IATVCR---AVLKALSFLHSQGVIHRDIKSDSILLtsdGRVKLS-------DFGFCAQ---VS 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  188 GDVrPPRNvaGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW---------RKIKDKE 246
Cdd:cd06648    155 KEV-PRRK--SLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYfnepplqamKRIRDNE 219
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
30-266 7.51e-04

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: 43.02  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTREnVALKVESAQQPKQV-----LKMEVAVLKKLQgKDHVCRFIGCGRNEKFNY 104
Cdd:cd14161      1 LKHRYEFLETLGKGTYGRVKKARDSSGRL-VAIKSIRKDRIKDEqdllhIRREIEIMSSLN-HPHIISVYEVFENSSKIV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQLQGR-NLAD-LRRSQPrgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQ 182
Cdd:cd14161     79 IVMEYASRgDLYDyISERQR---LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENI----LLDANGNIKIADFGLSNL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  183 YtnttgdvRPPRNVAGFRGTVRYAS---VNAHKNRemGRHDDLWSLFYMLVEFAVGQLPWrkikdkeqvgmikEKYEHRM 259
Cdd:cd14161    152 Y-------NQDKFLQTYCGSPLYASpeiVNGRPYI--GPEVDSWSLGVLLYILVHGTMPF-------------DGHDYKI 209

                   ....*..
gi 1034651883  260 LLKHMPS 266
Cdd:cd14161    210 LVKQISS 216
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
38-246 7.87e-04

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


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 43.37  E-value: 7.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALK------------VESAQQPKQVLKM--EVAVLKKLqgkdhVCRFigcGRNEKFN 103
Cdd:cd05619     11 KMLGKGSFGKVFLAELKGTNQFFAIKalkkdvvlmdddVECTMVEKRVLSLawEHPFLTHL-----FCTF---QTKENLF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  104 YVVMQLQGRNLadLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQy 183
Cdd:cd05619     83 FVMEYLNGGDL--MFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNI----LLDKDGHIKIADFGMCKE- 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  184 tNTTGDVRpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKE 246
Cdd:cd05619    156 -NMLGDAK----TSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEE 213
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
141-251 9.06e-04

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 43.16  E-value: 9.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  141 SIEAIHSVGFLHRDIKPSNF---AMGRLPSTyrkcymlDFGLARQYTNTTgdvrppRNVAGFRGTVRYASVNAHKNREMG 217
Cdd:cd05582    109 ALDHLHSLGIIYRDLKPENIlldEDGHIKLT-------DFGLSKESIDHE------KKAYSFCGTVEYMAPEVVNRRGHT 175
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1034651883  218 RHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMI 251
Cdd:cd05582    176 QSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMI 209
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1205-1384 9.33e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 43.82  E-value: 9.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1205 RRASETLSGTGSEEDTPASEPAAALPrkSGRAAATRSRIPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSSRLQLQT 1284
Cdd:PRK07764   599 GPPAPASSGPPEEAARPAAPAAPAAP--AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGA 676
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1285 PPGSATAADLRPKQPPGRGLGPGRAQAG--ARPPAPRSPRLPASTSAARNASASPrsQSLSRRESPSPSHQARPGVPPPR 1362
Cdd:PRK07764   677 APAAPPPAPAPAAPAAPAGAAPAQPAPApaATPPAGQADDPAAQPPQAAQGASAP--SPAADDPVPLPPEPDDPPDPAGA 754
                          170       180
                   ....*....|....*....|..
gi 1034651883 1363 GVPPARAQPDGTPSPGGSKKGP 1384
Cdd:PRK07764   755 PAQPPPPPAPAPAAAPAAAPPP 776
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1219-1376 9.50e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 9.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1219 DTPASEPAAALPRKSGRAAATRSRIPRPIGLRMPMPVAAQQPASrshGAAPALDTAITSSRLQLQTPPGSATAADLRPKQ 1298
Cdd:PRK12323   417 RAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAA---AARPAAAGPRPVAAAAAAAPARAAPAAAPAPAD 493
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1299 ---PPGRGLGPGRAQAGARPPAPrSPRLPASTSAARNASASPRSQSLSRRESP--SPSHQARPGVPPPRGVPPARAQPDG 1373
Cdd:PRK12323   494 ddpPPWEELPPEFASPAPAQPDA-APAGWVAESIPDPATADPDDAFETLAPAPaaAPAPRAAAATEPVVAPRPPRASASG 572

                   ...
gi 1034651883 1374 TPS 1376
Cdd:PRK12323   573 LPD 575
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
1227-1378 9.91e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 43.71  E-value: 9.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1227 AALPRKSGRAAATRSRIPRPIGLRMPmPVAAQQPASRSHGAAPALDTAITSSRLQLQTPPGSATAADLRPKQPPGRGLGP 1306
Cdd:PRK12323   362 AFRPGQSGGGAGPATAAAAPVAQPAP-AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQAS 440
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883 1307 GRAQAGARPPAPRSPRLPAStsAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSPG 1378
Cdd:PRK12323   441 ARGPGGAPAPAPAPAAAPAA--AARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA 510
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
32-179 1.02e-03

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 43.12  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEI----------YEAMDLLTRENVALKVESAQqpkqvLKMEVAVLKKLQGKdHVCRFIGCGRNEK 101
Cdd:cd05627      2 DDFESLKVIGRGAFGEVrlvqkkdtghIYAMKILRKADMLEKEQVAH-----IRAERDILVEADGA-WVVKMFYSFQDKR 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  102 FNYVVMQ-LQGRNLADLRrsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGL 179
Cdd:cd05627     76 NLYLIMEfLPGGDMMTLL--MKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNL----LLDAKGHVKLSDFGL 148
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
32-239 1.03e-03

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


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 42.54  E-value: 1.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQ-----VLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd14117      6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKegvehQLRREIEIQSHLR-HPNILRLYNYFHDRKRIYLI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRnlADLRRS-QPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGrlpstYR-KCYMLDFG------ 178
Cdd:cd14117     85 LEYAPR--GELYKElQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMG-----YKgELKIADFGwsvhap 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  179 -LARQYTNTTGDVRPPRNVAGfrgtvryasvNAHKNREmgrhdDLWSLFYMLVEFAVGQLPW 239
Cdd:cd14117    158 sLRRRTMCGTLDYLPPEMIEG----------RTHDEKV-----DLWCIGVLCYELLVGMPPF 204
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
24-225 1.15e-03

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: 42.36  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   24 LPANYVvkdrwKVLKKIGGGGFGEIYEAMDLLT---RENVALK-VESAQQPKQVLKM--EVAVLKKLQgKDHVCRFIGCG 97
Cdd:cd05033      1 IDASYV-----TIEKVIGGGEFGEVCSGSLKLPgkkEIDVAIKtLKSGYSDKQRLDFltEASIMGQFD-HPNVIRLEGVV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   98 RNEKFNYVVMQLQGRNLAD--LRRSqpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYML 175
Cdd:cd05033     75 TKSRPVMIVTEYMENGSLDkfLREN--DGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNI----LVNSDLVCKVS 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1034651883  176 DFGLARQytntTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSL 225
Cdd:cd05033    149 DFGLSRR----LEDSEATYTTKGGKIPIRWTAPEAIAYRKFTSASDVWSF 194
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
40-180 1.17e-03

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: 42.46  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDhVCRFIG-CGRNEKFNYVVMQLQGRNLADLR 118
Cdd:cd14155      1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANMLREVQLMNRLSHPN-ILRFMGvCVHQGQLHALTEYINGGNLEQLL 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  119 RSQPRGTFTLSttLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYrKCYMLDFGLA 180
Cdd:cd14155     80 DSNEPLSWTVR--VKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGY-TAVVGDFGLA 138
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
28-248 1.25e-03

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


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 42.74  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   28 YVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPK----QVLKMEVAVLKKLQGKDHvCRFIGC-----GR 98
Cdd:cd05633      1 HLTMNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmkqgETLALNERIMLSLVSTGD-CPFIVCmtyafHT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   99 NEKFNYVVMQLQGRNLaDLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFG 178
Cdd:cd05633     80 PDKLCFILDLMNGGDL-HYHLSQ-HGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANI----LLDEHGHVRISDLG 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  179 LARQYTNttgdvRPPRNVAGFRGTVryASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR--KIKDKEQV 248
Cdd:cd05633    154 LACDFSK-----KKPHASVGTHGYM--APEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRqhKTKDKHEI 218
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
38-185 1.30e-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: 42.40  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYE--AMDLL------TRENV-ALKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIG-CGRNEKfNYVVM 107
Cdd:cd05044      1 KFLGSGAFGEVFEgtAKDILgdgsgeTKVAVkTLRKGATDQEKAEFLKEAHLMSNFK-HPNILKLLGvCLDNDP-QYIIL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  108 QLQ--GRNLADLRRSQPRGT----FTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKCYML--DFGL 179
Cdd:cd05044     79 ELMegGDLLSYLRAARPTAFtpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSS--KDYRERVVKigDFGL 156

                   ....*..
gi 1034651883  180 ARQ-YTN 185
Cdd:cd05044    157 ARDiYKN 163
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
129-230 1.66e-03

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 41.83  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  129 STTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLpSTYRKCYMLDFGLARQYTNtTGDVRPprnvagFRGTVRYASV 208
Cdd:cd14198    110 NDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSI-YPLGDIKIVDFGMSRKIGH-ACELRE------IMGTPEYLAP 181
                           90       100
                   ....*....|....*....|....*
gi 1034651883  209 NAHKNREMGRHDDLWS---LFYMLV 230
Cdd:cd14198    182 EILNYDPITTATDMWNigvIAYMLL 206
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1081-1378 1.71e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.85  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1081 EGSALSGAPRETPSEMATNSLPNGPAladgPAPVSPLEPSPEKVATISPRRHAMPGSRPRSRIPVLLSEEDTGSEPSGSL 1160
Cdd:PHA03307    92 LSTLAPASPAREGSPTPPGPSSPDPP----PPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAA 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1161 SAKERwskrARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATR 1240
Cdd:PHA03307   168 SSRQA----ALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1241 SRIPRPIGLRM-PMPVAAQQPA-SRSHGAAPALDTAITSSRLQLQTPPGSATAADLRPKQPPGRGLGPGRAQAGARPPAP 1318
Cdd:PHA03307   244 SSGCGWGPENEcPLPRPAPITLpTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE 323
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1319 RSPRLPASTSAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSPG 1378
Cdd:PHA03307   324 SSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAG 383
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
40-181 1.81e-03

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 41.87  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALK--VESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGC-GRNEKFNYVVMQLQGRNLAD 116
Cdd:cd14221      1 LGKGCFGQAIKVTHRETGEVMVMKelIRFDEETQRTFLKEVKVMRCLE-HPNVLKFIGVlYKDKRLNFITEYIKGGTLRG 79
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  117 LRRSQPrGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd14221     80 IIKSMD-SHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNC----LVRENKSVVVADFGLAR 139
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
32-293 2.01e-03

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 41.64  E-value: 2.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK-----VESAQQpKQVLkMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd06617      1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKriratVNSQEQ-KRLL-MDLDISMRSVDCPYTVTFYGALFREGDVWIC 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNLADL-RRSQPRGTFTLSTTL-RLGKQILESIEAIHS-VGFLHRDIKPSNFAMGRLPstyrKCYMLDFGLARQY 183
Cdd:cd06617     79 MEVMDTSLDKFyKKVYDKGLTIPEDILgKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNG----QVKLCDFGISGYL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  184 TNT---TGD-----------VRPPRNVAGFrgTVRyasvnahknremgrhDDLWSLFYMLVEFAVGQLPWRKIKDK-EQV 248
Cdd:cd06617    155 VDSvakTIDagckpymaperINPELNQKGY--DVK---------------SDVWSLGITMIELATGRFPYDSWKTPfQQL 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1034651883  249 GMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDY-QLIMSVF 293
Cdd:cd06617    218 KQVVEEPSPQLPAEKFSPEFQDFVNKCLKKNYKERPNYpELLQHPF 263
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1229-1380 2.02e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.67  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1229 LPRKSGRAAATRSRIPRP---IGLRMPMPVAAQQPASRSHGAAPALdtaitssrlqlQTPPGSATAADLRPKQPPGRGLG 1305
Cdd:PRK07764   364 LPSASDDERGLLARLERLerrLGVAGGAGAPAAAAPSAAAAAPAAA-----------PAPAAAAPAAAAAPAPAAAPQPA 432
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883 1306 PGRAQAGARPPAPRSPRLPASTSAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSPGGS 1380
Cdd:PRK07764   433 PAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGAD 507
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
30-181 2.04e-03

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 41.73  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   30 VKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQL 109
Cdd:cd14085      1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVRTEIGVLLRLS-HPNIIKLKEIFETPTEISLVLEL 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  110 -QGRNLADlrRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlPSTYRKCYMLDFGLAR 181
Cdd:cd14085     80 vTGGELFD--RIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYAT-PAPDAPLKIADFGLSK 149
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
32-180 2.11e-03

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: 42.14  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   32 DRWKVLKKIGGGGFGEIYEAMDLLTRENVALK--VESAQQPKQVLKMEVAVLKKLQGKDH--VCRFIGCGRNEKFNYVVM 107
Cdd:cd05629      1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKtlLKSEMFKKDQLAHVKAERDVLAESDSpwVVSLYYSFQDAQYLYLIM 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034651883  108 Q-LQGRNLAD-LRRSQprgTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLA 180
Cdd:cd05629     81 EfLPGGDLMTmLIKYD---TFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDR--GGHIK--LSDFGLS 148
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
37-239 2.23e-03

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


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 41.93  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   37 LKKIGGGGFG----------EIYEAMDLLTRENVALKVESaqqpKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd05602     12 LKVIGKGSFGkvllarhksdEKFYAVKVLQKKAILKKKEE----KHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQLQGRNL-ADLRRS----QPRGTFtlsttlrLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd05602     88 DYINGGELfYHLQRErcflEPRARF-------YAAEIASALGYLHSLNIVYRDLKPENI----LLDSQGHIVLTDFGLCK 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  182 QytnttgDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:cd05602    157 E------NIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
137-181 2.27e-03

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 42.04  E-value: 2.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1034651883  137 QILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd07853    111 QILRGLKYLHSAGILHRDIKPGNL----LVNSNCVLKICDFGLAR 151
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
40-239 2.34e-03

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 41.73  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   40 IGGGGFGEIYEAMDLLTRENVALKVESAQQpkqVLKM--------EVAVLKKLqgkDH------VCRFigcgRNEKFNYV 105
Cdd:PTZ00263    26 LGTGSFGRVRIAKHKGTGEYYAIKCLKKRE---ILKMkqvqhvaqEKSILMEL---SHpfivnmMCSF----QDENRVYF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  106 VMQ--LQGRNLADLRRSqprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAM---GRLPSTyrkcymlDFGLA 180
Cdd:PTZ00263    96 LLEfvVGGELFTHLRKA---GRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLdnkGHVKVT-------DFGFA 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034651883  181 RQYTNTTgdvrpprnvAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPW 239
Cdd:PTZ00263   166 KKVPDRT---------FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPF 215
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
136-184 2.56e-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: 41.41  E-value: 2.56e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1034651883  136 KQILESIEAIHSVGFLHRDIKPSNFAMgrLPSTYRKCYMLDFGLARQYT 184
Cdd:cd14107    105 QQVLEGIGYLHGMNILHLDIKPDNILM--VSPTREDIKICDFGFAQEIT 151
PTZ00436 PTZ00436
60S ribosomal protein L19-like protein; Provisional
1163-1383 3.08e-03

60S ribosomal protein L19-like protein; Provisional


Pssm-ID: 185616 [Multi-domain]  Cd Length: 357  Bit Score: 41.47  E-value: 3.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1163 KERWSKRARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATRSR 1242
Cdd:PTZ00436   146 KNEKKKERQLAEQLAAKRLKDEQHRHKARKQELRKREKDRERARREDAAAAAAAKQKAAAKKAAAPSGKKSAKAAAPAKA 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1243 IPRPIGLRMPMPVAAQQPASRShgAAPALDTAitssrlqlqtPPGSATAADLRPKQPPGRGLGPgRAQAGARPPAPRSPR 1322
Cdd:PTZ00436   226 AAAPAKAAAPPAKAAAAPAKAA--AAPAKAAA----------PPAKAAAPPAKAAAPPAKAAAP-PAKAAAPPAKAAAPP 292
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883 1323 LPASTSAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQP-DGTPSPGGSKKG 1383
Cdd:PTZ00436   293 AKAAAAPAKAAAAPAKAAAAPAKAAAPPAKAAAPPAKAATPPAKAAAPPaKAAAAPVGKKAG 354
PHA03247 PHA03247
large tegument protein UL36; Provisional
1081-1350 3.37e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1081 EGSALSGAPReTPSEMATNSLPNGPALADGPAPVSPLEPSPEKVATISPRRHAMPGSRPRSRIPVLLSEEDTGSEPSGSL 1160
Cdd:PHA03247  2746 AGPATPGGPA-RPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1161 SAKERWSKRARPqqdlarlvmekrqgrlllrlasgASSSSSEEQRRASETLSGT----GSEEDTPASEPAAALPRKSGRA 1236
Cdd:PHA03247  2825 AGPLPPPTSAQP-----------------------TAPPPPPGPPPPSLPLGGSvapgGDVRRRPPSRSPAAKPAAPARP 2881
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1237 AATR------SRIPRPIGL------RMPMPVAAQQPASRSHGAAPALDTAI--TSSRLQLQTPPGSATAADLRPK----Q 1298
Cdd:PHA03247  2882 PVRRlarpavSRSTESFALppdqpeRPPQPQAPPPPQPQPQPPPPPQPQPPppPPPRPQPPLAPTTDPAGAGEPSgavpQ 2961
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883 1299 PPGRGLGPGRAQAG-ARPPAPRSPR-LPASTSAARNASASPR----SQSLSRRESPSP 1350
Cdd:PHA03247  2962 PWLGALVPGRVAVPrFRVPQPAPSReAPASSTPPLTGHSLSRvsswASSLALHEETDP 3019
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
38-181 3.51e-03

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 40.79  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAmDLLT----RENVALKVESAQQPKQVLKM-----EVAVLKKLQgKDHVCRFIGCGRNEKFNYVVMQ 108
Cdd:cd05040      1 EKLGDGSFGVVRRG-EWTTpsgkVIQVAVKCLKSDVLSQPNAMddflkEVNAMHSLD-HPNLIRLYGVVLSSPLMMVTEL 78
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  109 LQGRNLAD-LRRSQPRgtFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLAR 181
Cdd:cd05040     79 APLGSLLDrLRKDQGH--FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNI----LLASKDKVKIGDFGLMR 146
PHA03378 PHA03378
EBNA-3B; Provisional
1105-1389 3.64e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 41.98  E-value: 3.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1105 PALADGPAPVSPL-EPSPEKVATISPRRHAMPGSRPRsriPVLLSEEDTGSEPSGSLSAKERWSKRARPQQdLARLVMEK 1183
Cdd:PHA03378   565 PAPGLGPLQIQPLtSPTTSQLASSAPSYAQTPWPVPH---PSQTPEPPTTQSHIPETSAPRQWPMPLRPIP-MRPLRMQP 640
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1184 RQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASePAAALPRKsgrAAATRSRIPRPIGLRMPMPVAAQQPASR 1263
Cdd:PHA03378   641 ITFNVLVFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTG-ANTMLPIQ---WAPGTMQPPPRAPTPMRPPAAPPGRAQR 716
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1264 SHGAAPALdtaitssrlqlqTPPGSATAADLRPKQPPGRGLGPGRAQAGARPPAPRSPRLPASTSAARNASASPRSQSls 1343
Cdd:PHA03378   717 PAAATGRA------------RPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQA-- 782
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1034651883 1344 rreSPSPshqarpgvppprgvppaRAQPDGTPSPGGSKKGPRGKLQ 1389
Cdd:PHA03378   783 ---PPAP-----------------QQRPRGAPTPQPPPQAGPTSMQ 808
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
34-248 3.82e-03

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


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 41.19  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPK----QVLKMEVAVLKKLQGKDHvCRFIGC-----GRNEKFNY 104
Cdd:cd14223      2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKmkqgETLALNERIMLSLVSTGD-CPFIVCmsyafHTPDKLSF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQLQGRNLaDLRRSQpRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYT 184
Cdd:cd14223     81 ILDLMNGGDL-HYHLSQ-HGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANI----LLDEFGHVRISDLGLACDFS 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  185 NttgdvRPPRNVAGFRGTVryASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWR--KIKDKEQV 248
Cdd:cd14223    155 K-----KKPHASVGTHGYM--APEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRqhKTKDKHEI 213
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
142-238 3.84e-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: 41.15  E-value: 3.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  142 IEAIHSVGFLHRDIKPSNFAMGRlpSTYRKcyMLDFGLArqytnttgdvrpprnvAGFR--------------GTVRYAS 207
Cdd:cd05598    114 IESVHKMGFIHRDIKPDNILIDR--DGHIK--LTDFGLC----------------TGFRwthdskyylahslvGTPNYIA 173
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1034651883  208 VNAHKNREMGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd05598    174 PEVLLRTGYTQLCDWWSVGVILYEMLVGQPP 204
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
1221-1394 3.89e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 3.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1221 PASEPAAALPRKSGRAAATRSRIPRPIGLRMPMPVAAQQPASRSHGAAPALDTAITSSRLQLQTPPGSATAADLRPKQPP 1300
Cdd:PHA03307   761 PSLVPAKLAEALALLEPAEPQRGAGSSPPVRAEAAFRRPGRLRRSGPAADAASRTASKRKSRSHTPDGGSESSGPARPPG 840
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1301 GRGLGPGRAQAGARPPAPRSPRLPASTSAARNASASPRSQSLSRRESPSPSHQARPGVPPPRGVPPARAQPDGTPSP--- 1377
Cdd:PHA03307   841 AAARPPPARSSESSKSKPAAAGGRARGKNGRRRPRPPEPRARPGAAAPPKAAAAAPPAGAPAPRPRPAPRVKLGPMPpgg 920
                          170       180
                   ....*....|....*....|.
gi 1034651883 1378 ----GGSKKGPRGKLQAQRAT 1394
Cdd:PHA03307   921 pdprGGFRRVPPGDLHTPAPS 941
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
29-246 4.11e-03

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 40.86  E-value: 4.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKD-RWKVLKKIGGGGFGEIYEAMDLLTREN----VALKV---ESAQQPKQVLKMEVAVLKKLqGKDHVCRFIGCGRNE 100
Cdd:cd05057      3 IVKEtELEKGKVLGSGAFGTVYKGVWIPEGEKvkipVAIKVlreETGPKANEEILDEAYVMASV-DHPHLVRLLGICLSS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  101 KFNYVVMQLQGRNLADLRRsQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLA 180
Cdd:cd05057     82 QVQLITQLMPLGCLLDYVR-NHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNV----LVKTPNHVKITDFGLA 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034651883  181 RQYTNTTGDVRpprnVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIKDKE 246
Cdd:cd05057    157 KLLDVDEKEYH----AEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWElMTFGAKPYEGIPAVE 219
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
137-245 4.16e-03

Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 40.80  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  137 QILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQytnttgdVRPPRNVAGFRGTVRYASVNAHKNREM 216
Cdd:cd05605    110 EITCGLEHLHSERIVYRDLKPENI----LLDDHGHVRISDLGLAVE-------IPEGETIRGRVGTVGYMAPEVVKNERY 178
                           90       100
                   ....*....|....*....|....*....
gi 1034651883  217 GRHDDLWSLFYMLVEFAVGQLPWRKIKDK 245
Cdd:cd05605    179 TFSPDWWGLGCLIYEMIEGQAPFRARKEK 207
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
137-185 4.19e-03

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 41.12  E-value: 4.19e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1034651883  137 QILESIEAIHSVGFLHRDIKPSN-FAMGRLPSTYR-KcyMLDFGLARQYTN 185
Cdd:cd07842    116 QILNGIHYLHSNWVLHRDLKPANiLVMGEGPERGVvK--IGDLGLARLFNA 164
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
29-253 4.72e-03

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 40.79  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   29 VVKDRWKVLKKIGGGGFGEIYEAM-------DLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEK 101
Cdd:cd05062      3 VAREKITMSRELGQGSFGMVYEGIakgvvkdEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  102 FNYVVMQLQGRN---------LADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTyrkc 172
Cdd:cd05062     83 PTLVIMELMTRGdlksylrslRPEMENNPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTV---- 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  173 YMLDFGLARQYTNTTGDVRPPRNVAgfrgTVRYASVNAHKNREMGRHDDLWSLFYMLVEFA-VGQLPWRKIKDKEQVGMI 251
Cdd:cd05062    159 KIGDFGMTRDIYETDYYRKGGKGLL----PVRWMSPESLKDGVFTTYSDVWSFGVVLWEIAtLAEQPYQGMSNEQVLRFV 234

                   ..
gi 1034651883  252 KE 253
Cdd:cd05062    235 ME 236
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
33-238 5.15e-03

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: 40.45  E-value: 5.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALK------VESAQQPKQVlKMEVAVLKKLQgKDHVCRFIGCGRNEKFNYVV 106
Cdd:cd14073      2 RYELLETLGKGTYGKVKLAIERATGREVAIKsikkdkIEDEQDMVRI-RREIEIMSSLN-HPHIIRIYEVFENKDKIVIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  107 MQL-QGRNLADLrrSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLARQYTN 185
Cdd:cd14073     80 MEYaSGGELYDY--ISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENI----LLDQNGNAKIADFGLSNLYSK 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034651883  186 TtgdvrppRNVAGFRGTVRYAS---VNAHKNRemGRHDDLWSLFYMLVEFAVGQLP 238
Cdd:cd14073    154 D-------KLLQTFCGSPLYASpeiVNGTPYQ--GPEVDCWSLGVLLYTLVYGTMP 200
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
34-239 5.16e-03

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: 40.45  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   34 WKVLKKIGGGGFGEIYEAMDLLTRENVALK-VESAQQPKQVLKM---EVAVLKKLqgkDH------------------VC 91
Cdd:cd14071      2 YDIERTIGKGNFAVVKLARHRITKTEVAIKiIDKSQLDEENLKKiyrEVQIMKML---NHphiiklyqvmetkdmlylVT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   92 RFIGCGrnEKFNYVVMQlqGRnladLRRSQPRGTFtlsttlrlgKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRK 171
Cdd:cd14071     79 EYASNG--EIFDYLAQH--GR----MSEKEARKKF---------WQILSAVEYCHKRHIVHRDLKAENL----LLDANMN 137
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034651883  172 CYMLDFGLARQYTnttgdvrPPRNVAGFRGTVRYASVNAHKNRE-MGRHDDLWSL---FYMLVefaVGQLPW 239
Cdd:cd14071    138 IKIADFGFSNFFK-------PGELLKTWCGSPPYAAPEVFEGKEyEGPQLDIWSLgvvLYVLV---CGALPF 199
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
31-294 5.40e-03

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 40.55  E-value: 5.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   31 KDRWKVLKKIGGGGFGEIYEAMDL-LTRENVALKV------ESAQ-QPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKF 102
Cdd:cd05055     34 RNNLSFGKTLGAGAFGKVVEATAYgLSKSDAVMKVavkmlkPTAHsSEREALMSELKIMSHLGNHENIVNLLGACTIGGP 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  103 NYVVMQ--LQGrNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGLA 180
Cdd:cd05055    114 ILVITEycCYG-DLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNV----LLTHGKIVKICDFGLA 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  181 RQYTNTT-----GDVRPPrnvagfrgtVRYASVNAHKNREMGRHDDLWSLFYMLVE-FAVGQLPWRKIK-DKEQVGMIKE 253
Cdd:cd05055    189 RDIMNDSnyvvkGNARLP---------VKWMAPESIFNCVYTFESDVWSYGILLWEiFSLGSNPYPGMPvDSKFYKLIKE 259
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1034651883  254 KYehRMLL-KHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFE 294
Cdd:cd05055    260 GY--RMAQpEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIG 299
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
72-279 5.65e-03

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: 40.42  E-value: 5.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   72 QVLKMEVAVLKKLQgKDHVCRFIG--CGRNEKFN----YVVMQ-LQGRNLADLRRSQprGTFTLSTTLRLGKQILESIEA 144
Cdd:cd14012     43 QLLEKELESLKKLR-HPNLVSYLAfsIERRGRSDgwkvYLLTEyAPGGSLSELLDSV--GSVPLDTARRWTLQLLEALEY 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  145 IHSVGFLHRDIKPSNFAMGRLPSTYrKCYMLDFGlarqYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWS 224
Cdd:cd14012    120 LHRNGVVHKSLHAGNVLLDRDAGTG-IVKLTDYS----LGKTLLDMCSRGSLDEFKQTYWLPPELAQGSKSPTRKTDVWD 194
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034651883  225 LFYMLVEFAVGQLPWrkikdkeqvgmikEKYEHRMLLK---HMPSEFHLFLDHIASLD 279
Cdd:cd14012    195 LGLLFLQMLFGLDVL-------------EKYTSPNPVLvslDLSASLQDFLSKCLSLD 239
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
1221-1339 5.97e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.12  E-value: 5.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1221 PASEPAAALPRKSGRAAATRSRIPRPIGLRMPMPVAAQQPAsrshGAAPALDTAITSSRLQLQTPPGSATAADLRPKQPP 1300
Cdd:PRK07764   402 AAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPP----SPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPT 477
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1034651883 1301 GRGlGPGRAQAGARPPAPRSPRlPASTSAARNASASPRS 1339
Cdd:PRK07764   478 AAP-APAPPAAPAPAAAPAAPA-APAAPAGADDAATLRE 514
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
38-191 6.54e-03

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


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 40.03  E-value: 6.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   38 KKIGGGGFGEIYEAMDLLTRENVALKV----ESAQQPKQVLKMEVAVLKKLQGKDHVCRFigcgrNEKF---NYVVMQLQ 110
Cdd:cd14106     14 TPLGRGKFAVVRKCIHKETGKEYAAKFlrkrRRGQDCRNEILHEIAVLELCKDCPRVVNL-----HEVYetrSELILILE 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  111 ---GRNLADLRRSQprGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAmgrLPSTYRKC--YMLDFGLARqYTN 185
Cdd:cd14106     89 laaGGELQTLLDEE--ECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNIL---LTSEFPLGdiKLCDFGISR-VIG 162

                   ....*.
gi 1034651883  186 TTGDVR 191
Cdd:cd14106    163 EGEEIR 168
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
33-162 6.81e-03

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK2 mediates neuronal cell cycle and cell death through regulation of nuclear cyclin D1. It has also been found to promote leukemia cell proliferation by regulating cyclin A1. SRPK2 also plays a role in regulating pre-mRNA splicing and is required for spliceosomal B complex formation. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 40.40  E-value: 6.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883   33 RWKVLKKIGGGGFGEIYEAMDLLTRENVALKV-ESAQQPKQVLKMEVAVLKKLQ-------GKDHVCRFIG----CGRNE 100
Cdd:cd14217     13 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVvKSAQHYTETALDEIKLLRCVResdpedpNKDMVVQLIDdfkiSGMNG 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883  101 KFNYVVMQLQGRNLAD-LRRSQPRGtFTLSTTLRLGKQILESIEAIHS-VGFLHRDIKPSNFAM 162
Cdd:cd14217     93 IHVCMVFEVLGHHLLKwIIKSNYQG-LPIRCVKSIIRQVLQGLDYLHSkCKIIHTDIKPENILM 155
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
105-231 7.02e-03

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 40.62  E-value: 7.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883  105 VVMQLQGRNLADLR-----RSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFamgrLPSTYRKCYMLDFGL 179
Cdd:PTZ00283   114 IALVLDYANAGDLRqeiksRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANI----LLCSNGLVKLGDFGF 189
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1034651883  180 ARQYTNTTGDvrpprNVA-GFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVE 231
Cdd:PTZ00283   190 SKMYAATVSD-----DVGrTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYE 237
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
1105-1338 7.63e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 40.60  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1105 PALADGPAPVSPLEPSPekvatisPRrhAMPGSRPRSRIPVLLSEEDTGSEPSGSLSAkerwskRARPQQDLARlvmekr 1184
Cdd:PRK07003   360 PAVTGGGAPGGGVPARV-------AG--AVPAPGARAAAAVGASAVPAVTAVTGAAGA------ALAPKAAAAA------ 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034651883 1185 qgrlllrlasgasSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKSGRAAATRSriprpiglrmPMPVAAQQPASRS 1264
Cdd:PRK07003   419 -------------AATRAEAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSR----------CDERDAQPPADSG 475
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034651883 1265 HGAAPALDTAiTSSRLQLQTPPGSATAADLRPKQPPGRGLGPGRAQAgarpPAPRSPRLPASTSAARNASASPR 1338
Cdd:PRK07003   476 SASAPASDAP-PDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDA----PAAAAPPAPEARPPTPAAAAPAA 544
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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