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Conserved domains on  [gi|767973831|ref|XP_011536482|]
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anti-Muellerian hormone type-2 receptor isoform X6 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

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

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
97-417 1.22e-165

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


The actual alignment was detected with superfamily member cd14054:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 300  Bit Score: 469.15  E-value: 1.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKdc 176
Cdd:cd14054    1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADGRMEYLLVLEYAPK-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSC 256
Cdd:cd14054   79 -----------------GSLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGSC 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVLPGLTQPpaWTPTQPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMALRRADIYSLALLLWEILSRCPDL 336
Cdd:cd14054  142 VICDFGLAMVLRGSSLV--RGRPGAAENASISEVGTLRYMAPEVLEGAVNLRDCESALKQVDVYALGLVLWEIAMRCSDL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 337 RPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd14054  220 YPGESVPPYQMPYEAELGNHPTFEDMQLLVSREKARPKFPDAWKENSLAVRSLKETIEDCWDQDAEARLTALCVEERLAE 299

                 .
gi 767973831 417 L 417
Cdd:cd14054  300 L 300
 
Name Accession Description Interval E-value
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
97-417 1.22e-165

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 469.15  E-value: 1.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKdc 176
Cdd:cd14054    1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADGRMEYLLVLEYAPK-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSC 256
Cdd:cd14054   79 -----------------GSLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGSC 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVLPGLTQPpaWTPTQPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMALRRADIYSLALLLWEILSRCPDL 336
Cdd:cd14054  142 VICDFGLAMVLRGSSLV--RGRPGAAENASISEVGTLRYMAPEVLEGAVNLRDCESALKQVDVYALGLVLWEIAMRCSDL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 337 RPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd14054  220 YPGESVPPYQMPYEAELGNHPTFEDMQLLVSREKARPKFPDAWKENSLAVRSLKETIEDCWDQDAEARLTALCVEERLAE 299

                 .
gi 767973831 417 L 417
Cdd:cd14054  300 L 300
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
94-420 1.48e-26

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 108.00  E-value: 1.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831    94 ECEQVIREGGHAVVWAGQLQ--GKLVAIKAFPPRS----VAQFQAERALYELpgLQHDHIVRFITAsrggpgrllsgpll 167
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKktGKLVAIKVIKKKKikkdRERILREIKILKK--LKHPNIVRLYDV-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   168 vleLHPKDCVCLCprgraphNSLCPIGSLCHYLTQY---TSDWgsSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLS 244
Cdd:smart00220  66 ---FEDEDKLYLV-------MEYCEGGDLFDLLKKRgrlSEDE--ARFYLRQILSALEYLHSK---------GIVHRDLK 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   245 SQNVLIREDGSCAIGDLGLALVLPGltqppawtptqpqGPAAIMEAGTQRYMAPELLDKtldlQDWGMAlrrADIYSLAL 324
Cdd:smart00220 125 PENILLDEDGHVKLADFGLARQLDP-------------GEKLTTFVGTPEYMAPEVLLG----KGYGKA---VDIWSLGV 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   325 LLWEILSRCpdlrpdsspPPFQlayeaelgntptSDELWALAVQERRRPYIPSTWRCFATDPDgLRELLEDCWDADPEAR 404
Cdd:smart00220 185 ILYELLTGK---------PPFP------------GDDQLLELFKKIGKPKPPFPPPEWDISPE-AKDLIRKLLVKDPEKR 242
                          330
                   ....*....|....*.
gi 767973831   405 LTAEcvqqrlAALAHP 420
Cdd:smart00220 243 LTAE------EALQHP 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
96-420 1.15e-22

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 100.47  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAG--QLQGKLVAIK------AFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGrllsgPLL 167
Cdd:COG0515   12 LRLLGRGGMGVVYLArdLRLGRPVALKvlrpelAADPEARERFRREARA--LARLNHPNIVRVYDVGEEDGR-----PYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 168 VLELHPkdcvclcprGRaphnslcpigSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQ 246
Cdd:COG0515   85 VMEYVE---------GE----------SLADLLRRRGPlPPAEALRILAQLAEALAAAHAA---------GIVHRDIKPA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 247 NVLIREDGSCAIGDLGLALVLPGLTQPPAWTPtqpqgpaaimeAGTQRYMAPE-LLDKTLDlqdwgmalRRADIYSLALL 325
Cdd:COG0515  137 NILLTPDGRVKLIDFGIARALGGATLTQTGTV-----------VGTPGYMAPEqARGEPVD--------PRSDVYSLGVT 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 326 LWEILSRCpdlrpdsspPPFQLAYEAELGNTPTSDELWALAvqeRRRPYIPSTW-----RCFATDPD-------GLRELL 393
Cdd:COG0515  198 LYELLTGR---------PPFDGDSPAELLRAHLREPPPPPS---ELRPDLPPALdaivlRALAKDPEeryqsaaELAAAL 265
                        330       340
                 ....*....|....*....|....*..
gi 767973831 394 EDCWDADPEARLTAECVQQRLAALAHP 420
Cdd:COG0515  266 RAVLRSLAAAAAAAAAAAAAAAAAAAA 292
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
97-414 3.62e-22

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: 95.64  E-value: 3.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   97 QVIREGGHAVVWAGQLQGK------LVAIKAFPP----RSVAQFQAERALyeLPGLQHDHIVRFITA-SRGGPgrllsgP 165
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEgentkiKVAVKTLKEgadeEEREDFLEEASI--MKKLDHPNIVKLLGVcTQGEP------L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  166 LLVLELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDL 243
Cdd:pfam07714  77 YIVTEY-------------------MPGGDLLDFLRKHKRKLTLKdlLSMALQIAKGMEYLESKN---------FVHRDL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  244 SSQNVLIREDGSCAIGDLGLAlvlpgltqppawtPTQPQGPAAIMEAGTQ---RYMAPE-LLDKTLDLQdwgmalrrADI 319
Cdd:pfam07714 129 AARNCLVSENLVVKISDFGLS-------------RDIYDDDYYRKRGGGKlpiKWMAPEsLKDGKFTSK--------SDV 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  320 YSLALLLWEILSRCpdlrpdssPPPFQlayeaelgNTPTSDELWALavQERRRPYIPSTWrcfatdPDGLRELLEDCWDA 399
Cdd:pfam07714 188 WSFGVLLWEIFTLG--------EQPYP--------GMSNEEVLEFL--EDGYRLPQPENC------PDELYDLMKQCWAY 243
                         330
                  ....*....|....*
gi 767973831  400 DPEARLTAECVQQRL 414
Cdd:pfam07714 244 DPEDRPTFSELVEDL 258
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
211-330 2.34e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 50.18  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG--LTQppawTptqpqgpAAIM 288
Cdd:NF033483 110 VEIMIQILSALEHAHRN---------GIVHRDIKPQNILITKDGRVKVTDFGIARALSSttMTQ----T-------NSVL 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767973831 289 eaGTQRYMAPElldktldlQDWG-MALRRADIYSLALLLWEIL 330
Cdd:NF033483 170 --GTVHYLSPE--------QARGgTVDARSDIYSLGIVLYEML 202
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
215-408 3.27e-05

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 45.91  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlPGLTQPPAWTPTQPQGPAAIMEAGTQR 294
Cdd:PTZ00024 126 LQILNGLNVLH---------KWYFMHRDLSPANIFINSKGICKIADFGLA---RRYGYPPYSDTLSKDETMQRREEMTSK 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 295 -----YMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPdLRPDSSPPPfQLAYEAELGNTPTSDElWALAVqe 369
Cdd:PTZ00024 194 vvtlwYRAPELL---MGAEKYHFAV---DMWSVGCIFAELLTGKP-LFPGENEID-QLGRIFELLGTPNEDN-WPQAK-- 262
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767973831 370 rrrpYIPSTWRCFATDPDGLRELL----EDCWD-------ADPEARLTAE 408
Cdd:PTZ00024 263 ----KLPLYTEFTPRKPKDLKTIFpnasDDAIDllqsllkLNPLERISAK 308
 
Name Accession Description Interval E-value
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
97-417 1.22e-165

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 469.15  E-value: 1.22e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHPKdc 176
Cdd:cd14054    1 QLIGQGRYGTVWKGSLDERPVAVKVFPARHRQNFQNEKDIYELPLMEHSNILRFIGADERPTADGRMEYLLVLEYAPK-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSC 256
Cdd:cd14054   79 -----------------GSLCSYLRENTLDWMSSCRMALSLTRGLAYLHTDLRRGDQYKPAIAHRDLNSRNVLVKADGSC 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVLPGLTQPpaWTPTQPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMALRRADIYSLALLLWEILSRCPDL 336
Cdd:cd14054  142 VICDFGLAMVLRGSSLV--RGRPGAAENASISEVGTLRYMAPEVLEGAVNLRDCESALKQVDVYALGLVLWEIAMRCSDL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 337 RPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd14054  220 YPGESVPPYQMPYEAELGNHPTFEDMQLLVSREKARPKFPDAWKENSLAVRSLKETIEDCWDQDAEARLTALCVEERLAE 299

                 .
gi 767973831 417 L 417
Cdd:cd14054  300 L 300
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
97-417 1.99e-90

Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 277.40  E-value: 1.99e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKdc 176
Cdd:cd13998    1 EVIGKGRFGEVWKASLKNEPVAVKIFSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTA-LRTELWLVTAFHPN-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLIREDGSC 256
Cdd:cd13998   78 -----------------GSL*DYLSLHTIDWVSLCRLALSVARGLAHLHSEIPGCTQGKPAIAHRDLKSKNILVKNDGTC 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVL-PGLTQPPAwtptqpqgpAAIMEAGTQRYMAPELLDKTLDLQDWGmALRRADIYSLALLLWEILSRCPD 335
Cdd:cd13998  141 CIADFGLAVRLsPSTGEEDN---------ANNGQVGTKRYMAPEVLEGAINLRDFE-SFKRVDIYAMGLVLWEMASRCTD 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 336 LrpDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWrcfaTDPDGLR---ELLEDCWDADPEARLTAECVQQ 412
Cdd:cd13998  211 L--FGIVEEYKPPFYSEVPNHPSFEDMQEVVVRDKQRPNIPNRW----LSHPGLQslaETIEECWDHDAEARLTAQCIEE 284

                 ....*
gi 767973831 413 RLAAL 417
Cdd:cd13998  285 RLSEF 289
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
107-419 6.24e-85

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 263.03  E-value: 6.24e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 107 VWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKdcvclcprgrap 186
Cdd:cd14053   11 VWKAQYLNRLVAVKIFPLQEKQSWLTEREIYSLPGMKHENILQFIGAEKHGES-LEAEYWLITEFHER------------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 187 hnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEER-WQNGQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLAL 265
Cdd:cd14053   78 -------GSLCDYLKGNVISWNELCKIAESMARGLAYLHEDIpATNGGHKPSIAHRDFKSKNVLLKSDLTACIADFGLAL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 266 VLpgltqppawTPTQPQGPAAiMEAGTQRYMAPELLDKTLDLQ-DwgmALRRADIYSLALLLWEILSRCPDlrPDSSPPP 344
Cdd:cd14053  151 KF---------EPGKSCGDTH-GQVGTRRYMAPEVLEGAINFTrD---AFLRIDMYAMGLVLWELLSRCSV--HDGPVDE 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 345 FQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFAtdpdGLREL---LEDCWDADPEARLTAECVQQRLAALAH 419
Cdd:cd14053  216 YQLPFEEEVGQHPTLEDMQECVVHKKLRPQIRDEWRKHP----GLAQLcetIEECWDHDAEARLSAGCVEERLSQLSR 289
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
97-418 5.14e-70

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 224.95  E-value: 5.14e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQL------QGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrllsgpllvle 170
Cdd:cd14055    1 KLVGKGRFAEVWKAKLkqnasgQYETVAVKIFPYEEYASWKNEKDIFTDASLKHENILQFLTAEERGVG----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 171 lHPKDcVCLCprgraphNSLCPIGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNGQYKPGIAHRDLSSQNVLI 250
Cdd:cd14055   70 -LDRQ-YWLI-------TAYHENGSLQDYLTRHILSWEDLCKMAGSLARGLAHLHSDRTPCGRPKIPIAHRDLKSSNILV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 REDGSCAIGDLGLALVL-PGLTqppawtptqPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMaLRRADIYSLALLLWEI 329
Cdd:cd14055  141 KNDGTCVLADFGLALRLdPSLS---------VDELANSGQVGTARYMAPEALESRVNLEDLES-FKQIDVYSMALVLWEM 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 330 LSRCPDLrpdSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWR-----CFatdpdgLRELLEDCWDADPEAR 404
Cdd:cd14055  211 ASRCEAS---GEVKPYELPFGSKVRERPCVESMKDLVLRDRGRPEIPDSWLthqgmCV------LCDTITECWDHDPEAR 281
                        330
                 ....*....|....
gi 767973831 405 LTAECVQQRLAALA 418
Cdd:cd14055  282 LTASCVAERFNELK 295
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
107-417 2.56e-64

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 209.82  E-value: 2.56e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 107 VWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPG---RLLsgplLVLELHPKdcvclcprg 183
Cdd:cd14056   11 VWLGKYRGEKVAVKIFSSRDEDSWFRETEIYQTVMLRHENILGFIAADIKSTGswtQLW----LITEYHEH--------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 184 raphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAIGDLGL 263
Cdd:cd14056   78 ----------GSLYDYLQRNTLDTEEALRLAYSAASGLAHLHTEIVGT-QGKPAIAHRDLKSKNILVKRDGTCCIADLGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 264 ALVLPGLTQPPAwTPTQPQgpaaimeAGTQRYMAPELLDKTLDLQDWGmALRRADIYSLALLLWEILSRCPDlrpDSSPP 343
Cdd:cd14056  147 AVRYDSDTNTID-IPPNPR-------VGTKRYMAPEVLDDSINPKSFE-SFKMADIYSFGLVLWEIARRCEI---GGIAE 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 344 PFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRcfaTDP--DGLRELLEDCWDADPEARLTAECVQQRLAAL 417
Cdd:cd14056  215 EYQLPYFGMVPSDPSFEEMRKVVCVEKLRPPIPNRWK---SDPvlRSMVKLMQECWSENPHARLTALRVKKTLAKL 287
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
97-417 1.35e-60

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 200.26  E-value: 1.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGpGRLLSGPLLVLELHPKdc 176
Cdd:cd14140    1 EIKARGRFGCVWKAQLMNEYVAVKIFPIQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRG-SNLEMELWLITAFHDK-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEE-RWQNGQ-YKPGIAHRDLSSQNVLIREDG 254
Cdd:cd14140   78 -----------------GSLTDYLKGNIVSWNELCHIAETMARGLSYLHEDvPRCKGEgHKPAIAHRDFKSKNVLLKNDL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 255 SCAIGDLGLALVL-PGltQPPAWTPTQpqgpaaimeAGTQRYMAPELLDKTLDLQDwgMALRRADIYSLALLLWEILSRC 333
Cdd:cd14140  141 TAVLADFGLAVRFePG--KPPGDTHGQ---------VGTRRYMAPEVLEGAINFQR--DSFLRIDMYAMGLVLWELVSRC 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 334 PdlRPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWrcfaTDPDGLREL---LEDCWDADPEARLTAECV 410
Cdd:cd14140  208 K--AADGPVDEYMLPFEEEIGQHPSLEDLQEVVVHKKMRPVFKDHW----LKHPGLAQLcvtIEECWDHDAEARLSAGCV 281

                 ....*..
gi 767973831 411 QQRLAAL 417
Cdd:cd14140  282 EERISQI 288
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
97-418 1.24e-59

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 197.66  E-value: 1.24e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKdc 176
Cdd:cd14143    1 ESIGKGRFGEVWRGRWRGEDVAVKIFSSREERSWFREAEIYQTVMLRHENILGFIAADNKDNG-TWTQLWLVSDYHEH-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEErWQNGQYKPGIAHRDLSSQNVLIREDGSC 256
Cdd:cd14143   78 -----------------GSLFDYLNRYTVTVEGMIKLALSIASGLAHLHME-IVGTQGKPAIAHRDLKSKNILVKKNGTC 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVLPGLTQppawTPTQPQGPaaimEAGTQRYMAPELLDKTLDLQDWGmALRRADIYSLALLLWEILSRCpdl 336
Cdd:cd14143  140 CIADLGLAVRHDSATD----TIDIAPNH----RVGTKRYMAPEVLDDTINMKHFE-SFKRADIYALGLVFWEIARRC--- 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 337 RPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFatdpDGLR---ELLEDCWDADPEARLTAECVQQR 413
Cdd:cd14143  208 SIGGIHEDYQLPYYDLVPSDPSIEEMRKVVCEQKLRPNIPNRWQSC----EALRvmaKIMRECWYANGAARLTALRIKKT 283

                 ....*
gi 767973831 414 LAALA 418
Cdd:cd14143  284 LSQLS 288
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
97-417 9.27e-51

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 174.20  E-value: 9.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLlSGPLLVLELHPkdc 176
Cdd:cd14144    1 RSVGKGRYGEVWKGKWRGEKVAVKIFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSW-TQLYLITDYHE--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpIGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSC 256
Cdd:cd14144   77 ----------------NGSLYDFLRGNTLDTQSMLKLAYSAACGLAHLHTEIFGT-QGKPAIAHRDIKSKNILVKKNGTC 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVLPGLTQPPAWTPTQPQgpaaimeaGTQRYMAPELLDKTLDLQDWGmALRRADIYSLALLLWEILSRCPDl 336
Cdd:cd14144  140 CIADLGLAVKFISETNEVDLPPNTRV--------GTKRYMAPEVLDESLNRNHFD-AYKMADMYSFGLVLWEIARRCIS- 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 337 rpDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTW---RCFATdpdgLRELLEDCWDADPEARLTAECVQQR 413
Cdd:cd14144  210 --GGIVEEYQLPYYDAVPSDPSYEDMRRVVCVERRRPSIPNRWssdEVLRT----MSKLMSECWAHNPAARLTALRVKKT 283

                 ....
gi 767973831 414 LAAL 417
Cdd:cd14144  284 LGKL 287
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
97-417 1.03e-50

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 174.46  E-value: 1.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGrLLSGPLLVLELHPKdc 176
Cdd:cd14141    1 EIKARGRFGCVWKAQLLNEYVAVKIFPIQDKLSWQNEYEIYSLPGMKHENILQFIGAEKRGTN-LDVDLWLITAFHEK-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 vclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEE--RWQNGqYKPGIAHRDLSSQNVLIREDG 254
Cdd:cd14141   78 -----------------GSLTDYLKANVVSWNELCHIAQTMARGLAYLHEDipGLKDG-HKPAIAHRDIKSKNVLLKNNL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 255 SCAIGDLGLALVLPGltqppAWTPTQPQGpaaimEAGTQRYMAPELLDKTLDLQDwgMALRRADIYSLALLLWEILSRCP 334
Cdd:cd14141  140 TACIADFGLALKFEA-----GKSAGDTHG-----QVGTRRYMAPEVLEGAINFQR--DAFLRIDMYAMGLVLWELASRCT 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 335 dlRPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWRCFATDPdGLRELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd14141  208 --ASDGPVDEYMLPFEEEVGQHPSLEDMQEVVVHKKKRPVLRECWQKHAGMA-MLCETIEECWDHDAEARLSAGCVEERI 284

                 ...
gi 767973831 415 AAL 417
Cdd:cd14141  285 IQM 287
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
93-418 4.39e-50

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 173.01  E-value: 4.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  93 TECeqvIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFIT---ASRGGPGRLLsgplLVL 169
Cdd:cd14142   10 VEC---IGKGRYGEVWRGQWQGESVAVKIFSSRDEKSWFRETEIYNTVLLRHENILGFIAsdmTSRNSCTQLW----LIT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 170 ELHPKdcvclcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVL 249
Cdd:cd14142   83 HYHEN-------------------GSLYDYLQRTTLDHQEMLRLALSAASGLVHLHTEIFGT-QGKPAIAHRDLKSKNIL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 250 IREDGSCAIGDLGLALvlpgltqppawTPTQPQG---PAAIMEAGTQRYMAPELLDKTLDLQDWGmALRRADIYSLALLL 326
Cdd:cd14142  143 VKSNGQCCIADLGLAV-----------THSQETNqldVGNNPRVGTKRYMAPEVLDETINTDCFE-SYKRVDIYAFGLVL 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 327 WEILSRCPD--LRPDSSPPPFQLayeaeLGNTPTSDELWALAVQERRRPYIPSTWrcfATDPD--GLRELLEDCWDADPE 402
Cdd:cd14142  211 WEVARRCVSggIVEEYKPPFYDV-----VPSDPSFEDMRKVVCVDQQRPNIPNRW---SSDPTltAMAKLMKECWYQNPS 282
                        330
                 ....*....|....*.
gi 767973831 403 ARLTAECVQQRLAALA 418
Cdd:cd14142  283 ARLTALRIKKTLLKIL 298
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
99-404 6.14e-43

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: 152.31  E-value: 6.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQGKLVAIKAFPPRS-----VAQFQAERALyeLPGLQHDHIVRFITASRGGPgrllsgPL-LVLELh 172
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTDVAIKKLKVEDdndelLKEFRREVSI--LSKLRHPNIVQFIGACLSPP------PLcIVTEY- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 173 pkdcvclcprgraphnslCPIGSLCHYLT--QYTSDWGSSLRMALSLAQGLAFLHEerwqngqykPGIAHRDLSSQNVLI 250
Cdd:cd13999   72 ------------------MPGGSLYDLLHkkKIPLSWSLRLKIALDIARGMNYLHS---------PPIIHRDLKSLNILL 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 REDGSCAIGDLGLALVLpgltqppawtptqpQGPAAIM--EAGTQRYMAPELLDKtldlqdwGMALRRADIYSLALLLWE 328
Cdd:cd13999  125 DENFTVKIADFGLSRIK--------------NSTTEKMtgVVGTPRWMAPEVLRG-------EPYTEKADVYSFGIVLWE 183
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 329 ILSRcpdlrpdssPPPFQlayeaELGNTptsdELWALAVQERRRPYIPSTWrcfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd13999  184 LLTG---------EVPFK-----ELSPI----QIAAAVVQKGLRPPIPPDC------PPELSKLIKRCWNEDPEKR 235
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
99-417 2.60e-42

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 151.73  E-value: 2.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLlSGPLLVLELHPKdcvc 178
Cdd:cd14220    3 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSW-TQLYLITDYHEN---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 179 lcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAI 258
Cdd:cd14220   78 ---------------GSLYDFLKCTTLDTRALLKLAYSAACGLCHLHTEIYGT-QGKPAIAHRDLKSKNILIKKNGTCCI 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 259 GDLGLALVLPGLTQP---PAWTptqpqgpaaimEAGTQRYMAPELLDKTLDLQDWgMALRRADIYSLALLLWEILSRCPd 335
Cdd:cd14220  142 ADLGLAVKFNSDTNEvdvPLNT-----------RVGTKRYMAPEVLDESLNKNHF-QAYIMADIYSFGLIIWEMARRCV- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 336 lrPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWrcfaTDPDGLR---ELLEDCWDADPEARLTAECVQQ 412
Cdd:cd14220  209 --TGGIVEEYQLPYYDMVPSDPSYEDMREVVCVKRLRPTVSNRW----NSDECLRavlKLMSECWAHNPASRLTALRIKK 282

                 ....*
gi 767973831 413 RLAAL 417
Cdd:cd14220  283 TLAKM 287
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
99-422 2.81e-42

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 152.51  E-value: 2.81e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLlSGPLLVLELHPKdcvc 178
Cdd:cd14219   13 IGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSW-TQLYLITDYHEN---- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 179 lcprgraphnslcpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWQNgQYKPGIAHRDLSSQNVLIREDGSCAI 258
Cdd:cd14219   88 ---------------GSLYDYLKSTTLDTKAMLKLAYSSVSGLCHLHTEIFST-QGKPAIAHRDLKSKNILVKKNGTCCI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 259 GDLGLALVLPGLTQPPAWTPTqpqgpaaiMEAGTQRYMAPELLDKTLD---LQDWGMalrrADIYSLALLLWEILSRCPD 335
Cdd:cd14219  152 ADLGLAVKFISDTNEVDIPPN--------TRVGTKRYMPPEVLDESLNrnhFQSYIM----ADMYSFGLILWEVARRCVS 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 336 lrpDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTWrcfaTDPDGLRE---LLEDCWDADPEARLTAECVQQ 412
Cdd:cd14219  220 ---GGIVEEYQLPYHDLVPSDPSYEDMREIVCIKRLRPSFPNRW----SSDECLRQmgkLMTECWAHNPASRLTALRVKK 292
                        330
                 ....*....|
gi 767973831 413 RLAALAHPQE 422
Cdd:cd14219  293 TLAKMSESQD 302
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
94-419 4.83e-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: 114.99  E-value: 4.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  94 ECEQVIREGGHAVVWAG--QLQGKLVAIKAFPP------RSVAQFQAE-RALYELpglQHDHIVRFITAsrggpGRLLSG 164
Cdd:cd14014    3 RLVRLLGRGGMGEVYRArdTLLGRPVAIKVLRPelaedeEFRERFLREaRALARL---SHPNIVRVYDV-----GEDDGR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 165 PLLVLELhpkdcvclcprgraphnslCPIGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDL 243
Cdd:cd14014   75 PYIVMEY-------------------VEGGSLADLLRERGPlPPREALRILAQIADALAAAHRA---------GIVHRDI 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 244 SSQNVLIREDGSCAIGDLGLALVL--PGLTQPPawtptqpqgpaaiMEAGTQRYMAPE-LLDKTLDlqdwgmalRRADIY 320
Cdd:cd14014  127 KPANILLTEDGRVKLTDFGIARALgdSGLTQTG-------------SVLGTPAYMAPEqARGGPVD--------PRSDIY 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 321 SLALLLWEILSRCpdlrpdsspPPFQLAYEAELgntptsdelwaLAVQERRRPYIPSTWRCFAtdPDGLRELLEDCWDAD 400
Cdd:cd14014  186 SLGVVLYELLTGR---------PPFDGDSPAAV-----------LAKHLQEAPPPPSPLNPDV--PPALDAIILRALAKD 243
                        330
                 ....*....|....*....
gi 767973831 401 PEARLTAecVQQRLAALAH 419
Cdd:cd14014  244 PEERPQS--AAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
94-420 1.48e-26

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 108.00  E-value: 1.48e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831    94 ECEQVIREGGHAVVWAGQLQ--GKLVAIKAFPPRS----VAQFQAERALYELpgLQHDHIVRFITAsrggpgrllsgpll 167
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKktGKLVAIKVIKKKKikkdRERILREIKILKK--LKHPNIVRLYDV-------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   168 vleLHPKDCVCLCprgraphNSLCPIGSLCHYLTQY---TSDWgsSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLS 244
Cdd:smart00220  66 ---FEDEDKLYLV-------MEYCEGGDLFDLLKKRgrlSEDE--ARFYLRQILSALEYLHSK---------GIVHRDLK 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   245 SQNVLIREDGSCAIGDLGLALVLPGltqppawtptqpqGPAAIMEAGTQRYMAPELLDKtldlQDWGMAlrrADIYSLAL 324
Cdd:smart00220 125 PENILLDEDGHVKLADFGLARQLDP-------------GEKLTTFVGTPEYMAPEVLLG----KGYGKA---VDIWSLGV 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   325 LLWEILSRCpdlrpdsspPPFQlayeaelgntptSDELWALAVQERRRPYIPSTWRCFATDPDgLRELLEDCWDADPEAR 404
Cdd:smart00220 185 ILYELLTGK---------PPFP------------GDDQLLELFKKIGKPKPPFPPPEWDISPE-AKDLIRKLLVKDPEKR 242
                          330
                   ....*....|....*.
gi 767973831   405 LTAEcvqqrlAALAHP 420
Cdd:smart00220 243 LTAE------EALQHP 252
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
96-412 9.30e-25

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: 103.01  E-value: 9.30e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831    96 EQVIREGGHAVVWAGQLQGKL------VAIKAfpPRSVAQFQAERALYE----LPGLQHDHIVRFITASRGGPGrllsgP 165
Cdd:smart00221   4 GKKLGEGAFGEVYKGTLKGKGdgkeveVAVKT--LKEDASEQQIEEFLReariMRKLDHPNIVKLLGVCTEEEP-----L 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   166 LLVLELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHEERwqngqykpgIAHRD 242
Cdd:smart00221  77 MIVMEY-------------------MPGGDLLDYLRKNRPKELSLsdlLSFALQIARGMEYLESKN---------FIHRD 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   243 LSSQNVLIREDGSCAIGDLGLALVLPGLTqppawTPTQPQGPAAImeagtqRYMAPELLD------KTldlqdwgmalrr 316
Cdd:smart00221 129 LAARNCLVGENLVVKISDFGLSRDLYDDD-----YYKVKGGKLPI------RWMAPESLKegkftsKS------------ 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   317 aDIYSLALLLWEILSRCpdlrpdSSPPPfqlayeaELGNtptsDELWALaVQERRRPYIPStwRCfatdPDGLRELLEDC 396
Cdd:smart00221 186 -DVWSFGVLLWEIFTLG------EEPYP-------GMSN----AEVLEY-LKKGYRLPKPP--NC----PPELYKLMLQC 240
                          330
                   ....*....|....*..
gi 767973831   397 WDADPEARLT-AECVQQ 412
Cdd:smart00221 241 WAEDPEDRPTfSELVEI 257
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
96-412 2.06e-24

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 101.84  E-value: 2.06e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831    96 EQVIREGGHAVVWAGQLQGKL------VAIKAfpPRSVAQFQAERALYE----LPGLQHDHIVRFITASRGGPGrllsgP 165
Cdd:smart00219   4 GKKLGEGAFGEVYKGKLKGKGgkkkveVAVKT--LKEDASEQQIEEFLReariMRKLDHPNVVKLLGVCTEEEP-----L 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   166 LLVLELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDL 243
Cdd:smart00219  77 YIVMEY-------------------MEGGDLLSYLRKNRPKLSLSdlLSFALQIARGMEYLESKN---------FIHRDL 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   244 SSQNVLIREDGSCAIGDLGLALVLPG---LTQPPAWTPTqpqgpaaimeagtqRYMAPELLD------KTldlqdwgmal 314
Cdd:smart00219 129 AARNCLVGENLVVKISDFGLSRDLYDddyYRKRGGKLPI--------------RWMAPESLKegkftsKS---------- 184
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   315 rraDIYSLALLLWEILSRCpdlrpdsSPPPFQLayeaelgntpTSDELWALaVQERRRPYIPStwRCfatdPDGLRELLE 394
Cdd:smart00219 185 ---DVWSFGVLLWEIFTLG-------EQPYPGM----------SNEEVLEY-LKNGYRLPQPP--NC----PPELYDLML 237
                          330
                   ....*....|....*....
gi 767973831   395 DCWDADPEARLT-AECVQQ 412
Cdd:smart00219 238 QCWAEDPEDRPTfSELVEI 256
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
99-339 4.11e-23

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 96.96  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQ--GKLVAIKAFPPRSVaQFQAERALYE---LPGLQHDHIVRFITASRGGPGRLLsgpllVLELhp 173
Cdd:cd00180    1 LGKGSFGKVYKARDKetGKKVAVKVIPKEKL-KKLLEELLREieiLKKLNHPNIVKLYDVFETENFLYL-----VMEY-- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 174 kdcvclcprgraphnslCPIGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIR 251
Cdd:cd00180   73 -----------------CEGGSLKDLLKENKGplSEEEALSILRQLLSALEYLHSN---------GIIHRDLKPENILLD 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 252 EDGSCAIGDLGLALVlpgLTQPPAWTPTQPQGPAAimeagtqRYMAPELLDKTLDlqdwgmaLRRADIYSLALLLWEI-- 329
Cdd:cd00180  127 SDGTVKLADFGLAKD---LDSDDSLLKTTGGTTPP-------YYAPPELLGGRYY-------GPKVDIWSLGVILYELee 189
                        250
                 ....*....|....*...
gi 767973831 330 ----LSRC----PDLRPD 339
Cdd:cd00180  190 lkdlIRRMlqydPKKRPS 207
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
90-407 1.06e-22

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: 97.45  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  90 ERTTECEQVIREGGHAVVWAGQLQGKLVAIKAFPPR-----SVAQFQAER-ALYelpgLQHDHIVRFITASRGGPGRllS 163
Cdd:cd13979    2 WEPLRLQEPLGSGGFGSVYKATYKGETVAVKIVRRRrknraSRQSFWAELnAAR----LRHENIVRVLAAETGTDFA--S 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 164 GPLLVLElhpkdcvclCPRGRAPH---NSLCPIGSLCHyltqytsdwgsSLRMALSLAQGLAFLHEErwqngqykpGIAH 240
Cdd:cd13979   76 LGLIIME---------YCGNGTLQqliYEGSEPLPLAH-----------RILISLDIARALRFCHSH---------GIVH 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 241 RDLSSQNVLIREDGSCAIGDLGLALVLPGltqPPAW-TPTQPQGpaaimeaGTQRYMAPELLdKTLDLQDwgmalrRADI 319
Cdd:cd13979  127 LDVKPANILISEQGVCKLCDFGCSVKLGE---GNEVgTPRSHIG-------GTYTYRAPELL-KGERVTP------KADI 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 320 YSLALLLWEILSRcpdlrpdsspppfQLAYEAELGNTptsdeLWALAVQERRrpyiPSTWRCFATDPDG-LRELLEDCWD 398
Cdd:cd13979  190 YSFGITLWQMLTR-------------ELPYAGLRQHV-----LYAVVAKDLR----PDLSGLEDSEFGQrLRSLISRCWS 247

                 ....*....
gi 767973831 399 ADPEARLTA 407
Cdd:cd13979  248 AQPAERPNA 256
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
96-420 1.15e-22

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 100.47  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAG--QLQGKLVAIK------AFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGrllsgPLL 167
Cdd:COG0515   12 LRLLGRGGMGVVYLArdLRLGRPVALKvlrpelAADPEARERFRREARA--LARLNHPNIVRVYDVGEEDGR-----PYL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 168 VLELHPkdcvclcprGRaphnslcpigSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQ 246
Cdd:COG0515   85 VMEYVE---------GE----------SLADLLRRRGPlPPAEALRILAQLAEALAAAHAA---------GIVHRDIKPA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 247 NVLIREDGSCAIGDLGLALVLPGLTQPPAWTPtqpqgpaaimeAGTQRYMAPE-LLDKTLDlqdwgmalRRADIYSLALL 325
Cdd:COG0515  137 NILLTPDGRVKLIDFGIARALGGATLTQTGTV-----------VGTPGYMAPEqARGEPVD--------PRSDVYSLGVT 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 326 LWEILSRCpdlrpdsspPPFQLAYEAELGNTPTSDELWALAvqeRRRPYIPSTW-----RCFATDPD-------GLRELL 393
Cdd:COG0515  198 LYELLTGR---------PPFDGDSPAELLRAHLREPPPPPS---ELRPDLPPALdaivlRALAKDPEeryqsaaELAAAL 265
                        330       340
                 ....*....|....*....|....*..
gi 767973831 394 EDCWDADPEARLTAECVQQRLAALAHP 420
Cdd:COG0515  266 RAVLRSLAAAAAAAAAAAAAAAAAAAA 292
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
97-414 3.62e-22

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: 95.64  E-value: 3.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   97 QVIREGGHAVVWAGQLQGK------LVAIKAFPP----RSVAQFQAERALyeLPGLQHDHIVRFITA-SRGGPgrllsgP 165
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEgentkiKVAVKTLKEgadeEEREDFLEEASI--MKKLDHPNIVKLLGVcTQGEP------L 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  166 LLVLELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDL 243
Cdd:pfam07714  77 YIVTEY-------------------MPGGDLLDFLRKHKRKLTLKdlLSMALQIAKGMEYLESKN---------FVHRDL 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  244 SSQNVLIREDGSCAIGDLGLAlvlpgltqppawtPTQPQGPAAIMEAGTQ---RYMAPE-LLDKTLDLQdwgmalrrADI 319
Cdd:pfam07714 129 AARNCLVSENLVVKISDFGLS-------------RDIYDDDYYRKRGGGKlpiKWMAPEsLKDGKFTSK--------SDV 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  320 YSLALLLWEILSRCpdlrpdssPPPFQlayeaelgNTPTSDELWALavQERRRPYIPSTWrcfatdPDGLRELLEDCWDA 399
Cdd:pfam07714 188 WSFGVLLWEIFTLG--------EQPYP--------GMSNEEVLEFL--EDGYRLPQPENC------PDELYDLMKQCWAY 243
                         330
                  ....*....|....*
gi 767973831  400 DPEARLTAECVQQRL 414
Cdd:pfam07714 244 DPEDRPTFSELVEDL 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
192-406 9.78e-22

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: 94.44  E-value: 9.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 192 PIGSLCHYLTQYTSD--WGSSLRMALSLAQGLAFLHEERwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpg 269
Cdd:cd13978   75 ENGSLKSLLEREIQDvpWSLRFRIIHEIALGMNFLHNMD-------PPLLHHDLKPENILLDNHFHVKISDFGLSKLG-- 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 270 ltqppAWTPTQPQGPAAIMEAGTQRYMAPELLDKTLDLQDwgmalRRADIYSLALLLWEILSRC---PDLRpdsspPPFQ 346
Cdd:cd13978  146 -----MKSISANRRRGTENLGGTPIYMAPEAFDDFNKKPT-----SKSDVYSFAIVIWAVLTRKepfENAI-----NPLL 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 347 LAYEAELGNTPTSDELWALAVQERRRPYIpstwrcfatdpdglrELLEDCWDADPEARLT 406
Cdd:cd13978  211 IMQIVSKGDRPSLDDIGRLKQIENVQELI---------------SLMIRCWDGNPDARPT 255
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
106-412 3.42e-21

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: 92.99  E-value: 3.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 106 VVWAGQLQGK-----LVAIKAfpPRSVAQFQAERALYE----LPGLQHDHIVRFI-TASRGGPgrllsgPLLVLELhpkd 175
Cdd:cd00192   10 EVYKGKLKGGdgktvDVAVKT--LKEDASESERKDFLKearvMKKLGHPNVVRLLgVCTEEEP------LYLVMEY---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 176 cvclcprgraphnslCPIGSLCHYLTQYTSDWGSS----------LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSS 245
Cdd:cd00192   78 ---------------MEGGDLLDFLRKSRPVFPSPepstlslkdlLSFAIQIAKGMEYLASKK---------FVHRDLAA 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 246 QNVLIREDGSCAIGDLGLALVLP----GLTQPPAWTPTqpqgpaaimeagtqRYMAPELLD------KTldlqdwgmalr 315
Cdd:cd00192  134 RNCLVGEDLVVKISDFGLSRDIYdddyYRKKTGGKLPI--------------RWMAPESLKdgiftsKS----------- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 316 raDIYSLALLLWEILSrcpdlrpdsspppfqlayeaeLGNTP----TSDELWAlAVQERRRPYIPStwRCfatdPDGLRE 391
Cdd:cd00192  189 --DVWSFGVLLWEIFT---------------------LGATPypglSNEEVLE-YLRKGYRLPKPE--NC----PDELYE 238
                        330       340
                 ....*....|....*....|..
gi 767973831 392 LLEDCWDADPEARLT-AECVQQ 412
Cdd:cd00192  239 LMLSCWQLDPEDRPTfSELVER 260
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
99-414 5.61e-21

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: 92.34  E-value: 5.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQ-GKLVAIKAFPPRSVA----QFQAEraLYELPGLQHDHIVRFITASRGGpgrllSGPLLVLELHP 173
Cdd:cd14066    1 IGSGGFGTVYKGVLEnGTVVAVKRLNEMNCAaskkEFLTE--LEMLGRLRHPNLVRLLGYCLES-----DEKLLVYEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 174 KdcvclcprgraphnslcpiGSLCHYLTQYTS----DWGSSLRMALSLAQGLAFLHEErwqngqYKPGIAHRDLSSQNVL 249
Cdd:cd14066   74 N-------------------GSLEDRLHCHKGspplPWPQRLKIAKGIARGLEYLHEE------CPPPIIHGDIKSSNIL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 250 IREDGSCAIGDLGLALVLPGLTQppawtpTQPQGPAaimeAGTQRYMAPELLdktldlqdWGM-ALRRADIYSLALLLWE 328
Cdd:cd14066  129 LDEDFEPKLTDFGLARLIPPSES------VSKTSAV----KGTIGYLAPEYI--------RTGrVSTKSDVYSFGVVLLE 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 329 ILSRcpdlrpdssPPPFQLAYEAELGNTpTSDELWALAVQERRRPYIPSTWRCFATDPDGLRELLE---DCWDADPEARL 405
Cdd:cd14066  191 LLTG---------KPAVDENRENASRKD-LVEWVESKGKEELEDILDKRLVDDDGVEEEEVEALLRlalLCTRSDPSLRP 260

                 ....*....
gi 767973831 406 TAECVQQRL 414
Cdd:cd14066  261 SMKEVVQML 269
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
113-418 5.63e-20

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 89.75  E-value: 5.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 113 QGKLVAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRGgPGRLlsGPLLVLELhpkdcvclcprgraphnsl 190
Cdd:cd05038   32 TGEQVAVKSLQPSGEEQHMSdfKREIEILRTLDHEYIVKYKGVCES-PGRR--SLRLIMEY------------------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 268
Cdd:cd05038   90 LPSGSLRDYLqrHRDQIDLKRLLLFASQICKGMEYLGSQR---------YIHRDLAARNILVESEDLVKISDFGLAKVLP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 269 glTQPPAWTPTQP-QGPAaimeagtqRYMAPELLdktldlqdwgmALRR----ADIYSLALLLWEILSRCpdlRPDSSPP 343
Cdd:cd05038  161 --EDKEYYYVKEPgESPI--------FWYAPECL-----------RESRfssaSDVWSFGVTLYELFTYG---DPSQSPP 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 344 PFQLAYEAELGNTPTSDELWALAVQERRRPYIPStwrCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAALA 418
Cdd:cd05038  217 ALFLRMIGIAQGQMIVTRLLELLKSGERLPRPPS---C----PDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
96-420 3.95e-18

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: 83.97  E-value: 3.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVW--AGQLQGKLVAIKafppRSVAQF----QAERALYELPGL----QHDHIVRFITASRGGpGRLlsgp 165
Cdd:cd13997    5 LEQIGSGSFSEVFkvRSKVDGCLYAVK----KSKKPFrgpkERARALREVEAHaalgQHPNIVRYYSSWEEG-GHL---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 166 LLVLELhpkdcvCLCPRGRAPHNSLCPIGSLCHYLTqytsdwgssLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSS 245
Cdd:cd13997   76 YIQMEL------CENGSLQDALEELSPISKLSEAEV---------WDLLLQVALGLAFIHSK---------GIVHLDIKP 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 246 QNVLIREDGSCAIGDLGLALVLPglTQPPawtptqpqgpaaiMEAGTQRYMAPELldktldLQDWGMALRRADIYSLALL 325
Cdd:cd13997  132 DNIFISNKGTCKIGDFGLATRLE--TSGD-------------VEEGDSRYLAPEL------LNENYTHLPKADIFSLGVT 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 326 LWEILSRCPdlrpdsspppfqlayeaelgnTPTSDELWaLAVQERRRPYIPSTWRcfatdPDGLRELLEDCWDADPEARL 405
Cdd:cd13997  191 VYEAATGEP---------------------LPRNGQQW-QQLRQGKLPLPPGLVL-----SQELTRLLKVMLDPDPTRRP 243
                        330
                 ....*....|....*
gi 767973831 406 TAEcvqqrlAALAHP 420
Cdd:cd13997  244 TAD------QLLAHD 252
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
102-417 1.36e-17

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: 82.10  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 102 GGHAVVWAGQLQGKLVAIKAFPPRSVaQFQAERALYELPGLQHDHIVRFITASRGGpgrllSGPLLVLELhpKDCVCLcp 181
Cdd:cd14058    4 GSFGVVCKARWRNQIVAVKIIESESE-KKAFEVEVRQLSRVDHPNIIKLYGACSNQ-----KPVCLVMEY--AEGGSL-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 182 rgrapHNSLCPIGSLCHYLTQYTSDWgsslrmALSLAQGLAFLHeerwqNGQYKPgIAHRDLSSQNVLIREDGS-CAIGD 260
Cdd:cd14058   74 -----YNVLHGKEPKPIYTAAHAMSW------ALQCAKGVAYLH-----SMKPKA-LIHRDLKPPNLLLTNGGTvLKICD 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 261 LGLALVLPglTQppawtPTQPQGPAAimeagtqrYMAPELLDKTLDLQdwgmalrRADIYSLALLLWEILSRcpdlrpds 340
Cdd:cd14058  137 FGTACDIS--TH-----MTNNKGSAA--------WMAPEVFEGSKYSE-------KCDVFSWGIILWEVITR-------- 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973831 341 sPPPFQlayeaELGNTPTSdelWALAVQERRRPyiPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAAL 417
Cdd:cd14058  187 -RKPFD-----HIGGPAFR---IMWAVHNGERP--PLIKNC----PKPIESLMTRCWSKDPEKRPSMKEIVKIMSHL 248
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
102-420 4.40e-17

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: 80.73  E-value: 4.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 102 GGHAVVWAG--QLQGKLVAIKAF-----PPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGpgRLLSgplLVLELhpk 174
Cdd:cd06627   11 GAFGSVYKGlnLNTGEFVAIKQIslekiPKSDLKSVMGEIDL--LKKLNHPNIVKYIGSVKTK--DSLY---IILEY--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 175 dcvclcprgraphnslCPIGSLCHYLTQYtSDWGSSLrMALSLAQ---GLAFLHEErwqngqykpGIAHRDLSSQNVLIR 251
Cdd:cd06627   81 ----------------VENGSLASIIKKF-GKFPESL-VAVYIYQvleGLAYLHEQ---------GVIHRDIKGANILTT 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 252 EDGSCAIGDLGLALVLPGLTQPPAwtptqpqGPaaimeAGTQRYMAPElldkTLDLQDWGMAlrrADIYSLALLLWEILs 331
Cdd:cd06627  134 KDGLVKLADFGVATKLNEVEKDEN-------SV-----VGTPYWMAPE----VIEMSGVTTA---SDIWSVGCTVIELL- 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 332 rcpdlrpDSSPPPFQLAyeaelgntPTSdelwAL-AVQERRRPYIPStwrcfaTDPDGLRELLEDCWDADPEARLTAEcv 410
Cdd:cd06627  194 -------TGNPPYYDLQ--------PMA----ALfRIVQDDHPPLPE------NISPELRDFLLQCFQKDPTLRPSAK-- 246
                        330
                 ....*....|
gi 767973831 411 qqrlAALAHP 420
Cdd:cd06627  247 ----ELLKHP 252
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
97-420 5.44e-17

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: 80.64  E-value: 5.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQ--LQGKLVAIK-----AFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLsgpllVL 169
Cdd:cd06606    6 ELLGKGSFGSVYLALnlDTGELMAVKevelsGDSEEELEALEREIRI--LSSLKHPNIVRYLGTERTENTLNI-----FL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 170 ELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNV 248
Cdd:cd06606   79 EY-------------------VPGGSLASLLKKFGKLPEPVVRKyTRQILEGLEYLHSN---------GIVHRDIKGANI 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 249 LIREDGSCAIGDLGLALVLpgltqppAWTPTQPQGPAAimeAGTQRYMAPELLDKTLDlqdwGmalRRADIYSLALLLWE 328
Cdd:cd06606  131 LVDSDGVVKLADFGCAKRL-------AEIATGEGTKSL---RGTPYWMAPEVIRGEGY----G---RAADIWSLGCTVIE 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 329 ILSRCpdlrpdsspPPFqlayeAELGNTPTSdeLWALAVQErRRPYIPSTWrcfatdPDGLRELLEDCWDADPEARLTAE 408
Cdd:cd06606  194 MATGK---------PPW-----SELGNPVAA--LFKIGSSG-EPPPIPEHL------SEEAKDFLRKCLQRDPKKRPTAD 250
                        330
                 ....*....|..
gi 767973831 409 cvqqRLaaLAHP 420
Cdd:cd06606  251 ----EL--LQHP 256
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
98-420 1.92e-16

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: 78.82  E-value: 1.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQ--LQGKLVAIKAFPPRSVAQFQAER---ALYEL-PGLQHDHIVR---FITASRGGpgrllsGPLLV 168
Cdd:cd05118    6 KIGEGAFGTVWLARdkVTGEKVAIKKIKNDFRHPKAALReikLLKHLnDVEGHPNIVKlldVFEHRGGN------HLCLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 169 LELHPKDCvclcpRGRAPHNSLCpigsLCHYLTQYtsdwgsslrMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNV 248
Cdd:cd05118   80 FELMGMNL-----YELIKDYPRG----LPLDLIKS---------YLYQLLQALDFLHSN---------GIIHRDLKPENI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 249 LIREDGS-CAIGDLGLALVlpgLTQPPAWTPTQPQGpaaimeagtqrYMAPELLdktLDLQDWGMALrraDIYSLALLLW 327
Cdd:cd05118  133 LINLELGqLKLADFGLARS---FTSPPYTPYVATRW-----------YRAPEVL---LGAKPYGSSI---DIWSLGCILA 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 328 EILSRCPdLRPDSSPPPfQLAYEAE-LGntptsdelwalavqerrrpyipstwrcfatdPDGLRELLEDCWDADPEARLT 406
Cdd:cd05118  193 ELLTGRP-LFPGDSEVD-QLAKIVRlLG-------------------------------TPEALDLLSKMLKYDPAKRIT 239
                        330
                 ....*....|....
gi 767973831 407 AEcvqqrlAALAHP 420
Cdd:cd05118  240 AS------QALAHP 247
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
98-417 2.37e-15

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: 75.79  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQLQGKLVAIKAF---PPRSVA----QFQAERALYELpgLQHDHIVRFitasrggPGRLLSGPLLVLe 170
Cdd:cd14148    1 IIGVGGFGKVYKGLWRGEEVAVKAArqdPDEDIAvtaeNVRQEARLFWM--LQHPNIIAL-------RGVCLNPPHLCL- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 171 lhpkdcVCLCPRGRAPHNSLCPIGSLCHYLTqytsDWgsslrmALSLAQGLAFLHeerwqNGQYKPgIAHRDLSSQNVLI 250
Cdd:cd14148   71 ------VMEYARGGALNRALAGKKVPPHVLV----NW------AVQIARGMNYLH-----NEAIVP-IIHRDLKSSNILI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 RE--------DGSCAIGDLGLAlvlpgltqpPAWTPTqpqgpAAIMEAGTQRYMAPELLDKTLdlqdwgmALRRADIYSL 322
Cdd:cd14148  129 LEpienddlsGKTLKITDFGLA---------REWHKT-----TKMSAAGTYAWMAPEVIRLSL-------FSKSSDVWSF 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 323 ALLLWEILSrcpdlrpdsspppfqlayeaelGNTPTSdELWALAV-----QERRRPYIPSTwrCfatdPDGLRELLEDCW 397
Cdd:cd14148  188 GVLLWELLT----------------------GEVPYR-EIDALAVaygvaMNKLTLPIPST--C----PEPFARLLEECW 238
                        330       340
                 ....*....|....*....|
gi 767973831 398 DADPEARLTAECVQQRLAAL 417
Cdd:cd14148  239 DPDPHGRPDFGSILKRLEDI 258
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
99-331 2.84e-15

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 75.99  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQL-QGKLVAIKAFPPRSVA----QFQAEraLYELPGLQHDHIVRFitasRGgpgrLLSGP---LLVLE 170
Cdd:cd14664    1 IGRGGAGTVYKGVMpNGTLVAVKRLKGEGTQggdhGFQAE--IQTLGMIRHRNIVRL----RG----YCSNPttnLLVYE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 171 LHPKDCVCLCPRGRAPHNslcpiGSLchyltqytsDWGSSLRMALSLAQGLAFLHEErwqngqYKPGIAHRDLSSQNVLI 250
Cdd:cd14664   71 YMPNGSLGELLHSRPESQ-----PPL---------DWETRQRIALGSARGLAYLHHD------CSPLIIHRDVKSNNILL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 REDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeAGTQRYMAPELLDKtldlqdwGMALRRADIYSLALLLWEIL 330
Cdd:cd14664  131 DEEFEAHVADFGLAKLM---------DDKDSHVMSSV--AGSYGYIAPEYAYT-------GKVSEKSDVYSYGVVLLELI 192

                 .
gi 767973831 331 S 331
Cdd:cd14664  193 T 193
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
101-436 6.87e-15

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: 75.30  E-value: 6.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 101 EGGHAVVWAGQ--LQGKLVAIKAFP--PRSVAQ----FQAERALYELPGLQHDHIVRFITASrgGPGRLLSgplLVLELH 172
Cdd:cd07841   10 EGTYAVVYKARdkETGRIVAIKKIKlgERKEAKdginFTALREIKLLQELKHPNIIGLLDVF--GHKSNIN---LVFEFM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 173 PKDCVCLcprgraphnslcpIGSLCHYLTQytSDWGSSLRMALslaQGLAFLHEeRWqngqykpgIAHRDLSSQNVLIRE 252
Cdd:cd07841   85 ETDLEKV-------------IKDKSIVLTP--ADIKSYMLMTL---RGLEYLHS-NW--------ILHRDLKPNNLLIAS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 253 DGSCAIGDLGLALVLPgltqppawTPTQPQGPAAImeagTQRYMAPELLdktLDLQDWGMAlrrADIYSLALLLWEILSR 332
Cdd:cd07841  138 DGVLKLADFGLARSFG--------SPNRKMTHQVV----TRWYRAPELL---FGARHYGVG---VDMWSVGCIFAELLLR 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 333 CPDLRPDSspPPFQLA--YEAeLGnTPTSDElWA------LAVQERRRPYIPsTWRCFATDPDGLRELLEDCWDADPEAR 404
Cdd:cd07841  200 VPFLPGDS--DIDQLGkiFEA-LG-TPTEEN-WPgvtslpDYVEFKPFPPTP-LKQIFPAASDDALDLLQRLLTLNPNKR 273
                        330       340       350
                 ....*....|....*....|....*....|..
gi 767973831 405 LTAecvQQRLaalahpqeSHPFPESCPRGCPP 436
Cdd:cd07841  274 ITA---RQAL--------EHPYFSNDPAPTPP 294
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
97-417 1.43e-14

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 73.54  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVA--QFQAERALyeLPGLQHDHIVRFITASrggpgrLLSGPL-LVLELHP 173
Cdd:cd05039   12 ELIGKGEFGDVMLGDYRGQKVAVKCLKDDSTAaqAFLAEASV--MTTLRHPNLVQLLGVV------LEGNGLyIVTEYMA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 174 KDCVC--LCPRGRAPHNSLCPIGslchyltqytsdwgsslrMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIR 251
Cdd:cd05039   84 KGSLVdyLRSRGRAVITRKDQLG------------------FALDVCEGMEYLESKK---------FVHRDLAARNVLVS 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 252 EDGSCAIGDLGLA----LVLPGLTQPPAWTptqpqgpaaimeagtqrymAPElldktldlqdwgmALR------RADIYS 321
Cdd:cd05039  137 EDNVAKVSDFGLAkeasSNQDGGKLPIKWT-------------------APE-------------ALRekkfstKSDVWS 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 322 LALLLWEILS--RCPDLRpdsspppfqlayeaelgnTPTSDELwalavqerrrPYIPSTWRCFATD--PDGLRELLEDCW 397
Cdd:cd05039  185 FGILLWEIYSfgRVPYPR------------------IPLKDVV----------PHVEKGYRMEAPEgcPPEVYKVMKNCW 236
                        330       340
                 ....*....|....*....|
gi 767973831 398 DADPEARLTAECVQQRLAAL 417
Cdd:cd05039  237 ELDPAKRPTFKQLREKLEHI 256
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
113-404 1.48e-14

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 73.07  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 113 QGKLVAIKAFpprsvaqFQAERALYELPGLQHDHIVRFITAsrggpgrllsgpllVLElHPKDCVClcprgraphNSLCP 192
Cdd:cd14060   17 QDKEVAVKKL-------LKIEKEAEILSVLSHRNIIQFYGA--------------ILE-APNYGIV---------TEYAS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 193 IGSLCHYLTQYTS---DWGSSLRMALSLAQGLAFLHEErwqngqyKP-GIAHRDLSSQNVLIREDGSCAIGDLGlalvlp 268
Cdd:cd14060   66 YGSLFDYLNSNESeemDMDQIMTWATDIAKGMHYLHME-------APvKVIHRDLKSRNVVIAADGVLKICDFG------ 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 269 gltqppawtPTQPQGPAAIME-AGTQRYMAPELLdKTLDLQDwgmalrRADIYSLALLLWEILSRcpdLRPDSSPPPFQL 347
Cdd:cd14060  133 ---------ASRFHSHTTHMSlVGTFPWMAPEVI-QSLPVSE------TCDTYSYGVVLWEMLTR---EVPFKGLEGLQV 193
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767973831 348 AYeaelgntptsdelwaLAVQERRRPYIPSTwrCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd14060  194 AW---------------LVVEKNERPTIPSS--C----PRSFAELMRRCWEADVKER 229
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
99-334 1.90e-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: 73.52  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVW-AGQLQ-GKLVAIKAFPPRSVAQFQAERALYELPGLQ----HDHIVRFITASRGGpgrllSGPLLVLELH 172
Cdd:cd07832    8 IGEGAHGIVFkAKDREtGETVALKKVALRKLEGGIPNQALREIKALQacqgHPYVVKLRDVFPHG-----TGFVLVFEYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 173 PKDcvcLCPRGRAPHNSLcPIGSLCHYLtqytsdwgsslRMALslaQGLAFLHEERwqngqykpgIAHRDLSSQNVLIRE 252
Cdd:cd07832   83 LSS---LSEVLRDEERPL-TEAQVKRYM-----------RMLL---KGVAYMHANR---------IMHRDLKPANLLISS 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 253 DGSCAIGDLGLALVlpglTQPPAWTPTQPQgpaaimeAGTQRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSR 332
Cdd:cd07832  136 TGVLKIADFGLARL----FSEEDPRLYSHQ-------VATRWYRAPELL---YGSRKYDEGV---DLWAVGCIFAELLNG 198

                 ..
gi 767973831 333 CP 334
Cdd:cd07832  199 SP 200
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
89-408 2.13e-14

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 73.19  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  89 SERTTECEQVIREGGHavvwagqlQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFItasrggpGRLLSGPLL- 167
Cdd:cd13992    8 SSHTGEPKYVKKVGVY--------GGRTVAIKHITFSRTEKRTILQELNQLKELVHDNLNKFI-------GICINPPNIa 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 168 -VLELHPKdcvclcprgraphnslcpiGSLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykPGIAHRDLS 244
Cdd:cd13992   73 vVTEYCTR-------------------GSLQDVLlnREIKMDWMFKSSFIKDIVKGMNYLHSS--------SIGYHGRLK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIREDGSCAIGDLGLALVLPGltqppaWTPTQPQGPAaimEAGTQRYMAPELLDKTLDlqDWGMALRrADIYSLAL 324
Cdd:cd13992  126 SSNCLVDSRWVVKLTDFGLRNLLEE------QTNHQLDEDA---QHKKLLWTAPELLRGSLL--EVRGTQK-GDVYSFAI 193
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 325 LLWEILSRcpdlrpdsspppfQLAYEAELGNTPTSDELWAlavqeRRRPYIPSTWRCFATDPDGLRELLEDCWDADPEAR 404
Cdd:cd13992  194 ILYEILFR-------------SDPFALEREVAIVEKVISG-----GNKPFRPELAVLLDEFPPRLVLLVKQCWAENPEKR 255

                 ....
gi 767973831 405 LTAE 408
Cdd:cd13992  256 PSFK 259
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
101-334 2.50e-14

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: 73.30  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 101 EGGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYE-----LPGLQHDHIVRFITASRGGPgrllsGPLLVLELHPKd 175
Cdd:cd14158   25 EGGFGVVFKGYINDKNVAVKKLAAMVDISTEDLTKQFEqeiqvMAKCQHENLVELLGYSCDGP-----QLCLVYTYMPN- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 176 cvclcprgraphnslcpiGSL-----CHYLTQYTSdWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI 250
Cdd:cd14158   99 ------------------GSLldrlaCLNDTPPLS-WHMRCKIAQGTANGINYLHEN---------NHIHRDIKSANILL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 REDGSCAIGDLGLAlvlpgltqppawtPTQPQGPAAIME---AGTQRYMAPELLDktldlqdwGMALRRADIYSLALLLW 327
Cdd:cd14158  151 DETFVPKISDFGLA-------------RASEKFSQTIMTeriVGTTAYMAPEALR--------GEITPKSDIFSFGVVLL 209

                 ....*..
gi 767973831 328 EILSRCP 334
Cdd:cd14158  210 EIITGLP 216
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
207-418 3.24e-14

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: 72.54  E-value: 3.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA-LVLPGLTQPPAWTPTQ----- 280
Cdd:cd14154   90 WAQRVRFAKDIASGMAYLHSM---------NIIHRDLNSHNCLVREDKTVVVADFGLArLIVEERLPSGNMSPSEtlrhl 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 281 --PQGPAAIMEAGTQRYMAPELLD-KTLDlqdwgmalRRADIYSLALLLWEILSRC---PDLRPDsspppfqlayeaelg 354
Cdd:cd14154  161 ksPDRKKRYTVVGNPYWMAPEMLNgRSYD--------EKVDIFSFGIVLCEIIGRVeadPDYLPR--------------- 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 355 ntpTSDelWALAVQERRRPYIPStwrCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAALA 418
Cdd:cd14154  218 ---TKD--FGLNVDSFREKFCAG---C----PPPFFKLAFLCCDLDPEKRPPFETLEEWLEALY 269
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
99-408 4.75e-14

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: 71.95  E-value: 4.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVV-----WAgQLQGKLVAIKAFPPR---SVAQFQAERALYE---LPGLQHDHIVRFITasrggpgrllsgplL 167
Cdd:cd13994    1 IGKGATSVVrivtkKN-PRSGVLYAVKEYRRRddeSKRKDYVKRLTSEyiiSSKLHHPNIVKVLD--------------L 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 168 VLELHPKDCVCLcprgraphnSLCPIGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQ 246
Cdd:cd13994   66 CQDLHGKWCLVM---------EYCPGGDLFTLIEKADSlSLEEKDCFFKQILRGVAYLHSH---------GIAHRDLKPE 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 247 NVLIREDGSCAIGDLGLALVLpgltqppawtpTQPQGPAAIMEA---GTQRYMAPELL-DKTLDlqdwgmaLRRADIYSL 322
Cdd:cd13994  128 NILLDEDGVLKLTDFGTAEVF-----------GMPAEKESPMSAglcGSEPYMAPEVFtSGSYD-------GRAVDVWSC 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 323 ALLLWEIlsRCPDLrpdssppPFQLAYeaelgntpTSDELWALAVQERRRPYIPsTWRCFATDPDGLRELLEDCWDADPE 402
Cdd:cd13994  190 GIVLFAL--FTGRF-------PWRSAK--------KSDSAYKAYEKSGDFTNGP-YEPIENLLPSECRRLIYRMLHPDPE 251

                 ....*.
gi 767973831 403 ARLTAE 408
Cdd:cd13994  252 KRITID 257
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
99-404 8.04e-14

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 71.41  E-value: 8.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQGKLVAIK-----AFPPRS-VAQFQAERALyeLPGLQHDHIVRFITASRGGPGRL------LSGPL 166
Cdd:cd14064    1 IGSGSFGKVYKGRCRNKIVAIKryranTYCSKSdVDMFCREVSI--LCRLNHPCVIQFVGACLDDPSQFaivtqyVSGGS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 167 LVLELHPKdcvclcprgraphnslcpigslchyltQYTSDWGSSLRMALSLAQGLAFLHEERwqngqyKPgIAHRDLSSQ 246
Cdd:cd14064   79 LFSLLHEQ---------------------------KRVIDLQSKLIIAVDVAKGMEYLHNLT------QP-IIHRDLNSH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 247 NVLIREDGSCAIGDLGLALVLPGLTQPPawTPTQPqgpaaimeaGTQRYMAPELLDKTldlqdwGMALRRADIYSLALLL 326
Cdd:cd14064  125 NILLYEDGHAVVADFGESRFLQSLDEDN--MTKQP---------GNLRWMAPEVFTQC------TRYSIKADVFSYALCL 187
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 327 WEILsrcpdlrpdSSPPPFqlayeAELGNTPTSDELwalaVQERRRPYIPSTWrcfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd14064  188 WELL---------TGEIPF-----AHLKPAAAAADM----AYHHIRPPIGYSI------PKPISSLLMRGWNAEPESR 241
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
114-419 9.69e-14

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: 71.47  E-value: 9.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRGGPGRLLsgpLLVLELhpkdcvclcprgraphnslC 191
Cdd:cd05080   33 GEMVAVKALKADCGPQHRSgwKQEIDILKTLYHENIVKYKGCCSEQGGKSL---QLIMEY-------------------V 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 192 PIGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLPglt 271
Cdd:cd05080   91 PLGSLRDYLPKHSIGLAQLLLFAQQICEGMAYLHSQHY---------IHRDLAARNVLLDNDRLVKIGDFGLAKAVP--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 272 QPPAWTPTQPQGPAAIMeagtqrYMAPELLDKTldlqDWGMAlrrADIYSLALLLWEILSRCPdlrPDSSPPPfqlAYEA 351
Cdd:cd05080  159 EGHEYYRVREDGDSPVF------WYAPECLKEY----KFYYA---SDVWSFGVTLYELLTHCD---SSQSPPT---KFLE 219
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 352 ELGntPTSDELWALAVQE--RRRPYIPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAALAH 419
Cdd:cd05080  220 MIG--IAQGQMTVVRLIEllERGERLPCPDKC----PQEVYHLMKNCWETEASFRPTFENLIPILKTVHE 283
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
98-417 1.66e-13

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: 70.45  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQLQGKLVAIKAF---PPRSVA----QFQAERALYELpgLQHDHIVRFitasRGgpgrllsgpllvle 170
Cdd:cd14146    1 IIGVGGFGKVYRATWKGQEVAVKAArqdPDEDIKataeSVRQEAKLFSM--LRHPNIIKL----EG-------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 171 lhpkdcVCLcprgRAPHnsLCPI------GSLCHYLTQYTSDWGSS----------LRMALSLAQGLAFLHEErwqngQY 234
Cdd:cd14146   61 ------VCL----EEPN--LCLVmefargGTLNRALAAANAAPGPRrarripphilVNWAVQIARGMLYLHEE-----AV 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 235 KPgIAHRDLSSQNVLIRE----DGSC----AIGDLGLAlvlpgltqpPAWTPTqpqgpAAIMEAGTQRYMAPELLDKTld 306
Cdd:cd14146  124 VP-ILHRDLKSSNILLLEkiehDDICnktlKITDFGLA---------REWHRT-----TKMSAAGTYAWMAPEVIKSS-- 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 307 lqdwgMALRRADIYSLALLLWEILSrcpdlrpdsspppfqlayeaelGNTPTS--DEL---WALAVQERRRPyIPSTwrC 381
Cdd:cd14146  187 -----LFSKGSDIWSYGVLLWELLT----------------------GEVPYRgiDGLavaYGVAVNKLTLP-IPST--C 236
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 767973831 382 fatdPDGLRELLEDCWDADPEARLTAECVQQRLAAL 417
Cdd:cd14146  237 ----PEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
98-414 3.50e-13

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 69.34  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQLQGKLVAIKAF-------PPRSVAQFQAERALYELpgLQHDHIVrfitASRGgpgrllsgpllvle 170
Cdd:cd14061    1 VIGVGGFGKVYRGIWRGEEVAVKAArqdpdedISVTLENVRQEARLFWM--LRHPNII----ALRG-------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 171 lhpkdcVCLCPrgraPHnsLCPI------GSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqyKPGIAHRDLS 244
Cdd:cd14061   61 ------VCLQP----PN--LCLVmeyargGALNRVLAGRKIPPHVLVDWAIQIARGMNYLHNEA------PVPIIHRDLK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIRE--------DGSCAIGDLGLALVLPGLTQPPAwtptqpqgpaaimeAGTQRYMAPELLDKTldlqdwgMALRR 316
Cdd:cd14061  123 SSNILILEaienedleNKTLKITDFGLAREWHKTTRMSA--------------AGTYAWMAPEVIKSS-------TFSKA 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 317 ADIYSLALLLWEILsrcpdlrpdSSPPPFQ------LAYeaelgntptsdelwALAVQERRRPyIPSTwrCfatdPDGLR 390
Cdd:cd14061  182 SDVWSYGVLLWELL---------TGEVPYKgidglaVAY--------------GVAVNKLTLP-IPST--C----PEPFA 231
                        330       340
                 ....*....|....*....|....
gi 767973831 391 ELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd14061  232 QLMKDCWQPDPHDRPSFADILKQL 255
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
192-406 1.11e-12

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 67.91  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 192 PIGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL--VLPG 269
Cdd:cd14027   74 EKGNLMHVLKKVSVPLSVKGRIILEIIEGMAYLHGK---------GVIHKDLKPENILVDNDFHIKIADLGLASfkMWSK 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 270 LTQPPAWTPTQPQGPAAiMEAGTQRYMAPELLdKTLDLQdwgmALRRADIYSLALLLWEILSrcpdlrpDSSPppfqlaY 349
Cdd:cd14027  145 LTKEEHNEQREVDGTAK-KNAGTLYYMAPEHL-NDVNAK----PTEKSDVYSFAIVLWAIFA-------NKEP------Y 205
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 350 EaelgNTPTSDELwALAVQERRRPYIPS-TWRCfatdPDGLRELLEDCWDADPEARLT 406
Cdd:cd14027  206 E----NAINEDQI-IMCIKSGNRPDVDDiTEYC----PREIIDLMKLCWEANPEARPT 254
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
110-417 1.31e-12

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 68.00  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 110 GQLQGKLVAIKAFPPRSVAQFQA-ERALYELPGLQHDHIVRFitasRG---GPGRllSGPLLVLELHPKdcvclcprgra 185
Cdd:cd05081   29 GDNTGALVAVKQLQHSGPDQQRDfQREIQILKALHSDFIVKY----RGvsyGPGR--RSLRLVMEYLPS----------- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 186 phnslcpiGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGL 263
Cdd:cd05081   92 --------GCLRDFLQRHRARLDASrlLLYSSQICKGMEYLGSRRC---------VHRDLAARNILVESEAHVKIADFGL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 264 ALVLPgltQPPAWTPTQPQGPAAIMeagtqrYMAPELLDKTLdlqdwgmALRRADIYSLALLLWEILSRCPDLRpdsSPP 343
Cdd:cd05081  155 AKLLP---LDKDYYVVREPGQSPIF------WYAPESLSDNI-------FSRQSDVWSFGVVLYELFTYCDKSC---SPS 215
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 344 PFQLAYEAELGNTPTSDELWALAVQERRRPYIPSTwrcfatdPDGLRELLEDCWDADPEARLTAECVQQRLAAL 417
Cdd:cd05081  216 AEFLRMMGCERDVPALCRLLELLEEGQRLPAPPAC-------PAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
165-332 1.56e-12

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 67.51  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 165 PLLVLELHPKDCVCLCPRGRAPH----NSLCPIGSLCHYL---TQYTSDWGSSLRMALSLAQGLAFLHeerwqngQYKPG 237
Cdd:cd14057   44 PRLRIFSHPNVLPVLGACNSPPNlvviSQYMPYGSLYNVLhegTGVVVDQSQAVKFALDIARGMAFLH-------TLEPL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 238 IAHRDLSSQNVLIREDGSCAI--GDLGLALVLPGLTQPPAWtptqpqgpaaimeagtqryMAPELLDKTLDLQDWgmalR 315
Cdd:cd14057  117 IPRHHLNSKHVMIDEDMTARInmADVKFSFQEPGKMYNPAW-------------------MAPEALQKKPEDINR----R 173
                        170
                 ....*....|....*..
gi 767973831 316 RADIYSLALLLWEILSR 332
Cdd:cd14057  174 SADMWSFAILLWELVTR 190
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
217-426 1.78e-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: 67.16  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGlTQPPAWTPtqpqgpaaimeAGTQRYM 296
Cdd:cd05123  102 IVLALEYLHSL---------GIIYRDLKPENILLDSDGHIKLTDFGLAKELSS-DGDRTYTF-----------CGTPEYL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLDKtldlQDWGMAlrrADIYSLALLLWEILSRCpdlrpdsspPPFQLAYEAELGNTPTSDELwalavqerrrpYIP 376
Cdd:cd05123  161 APEVLLG----KGYGKA---VDWWSLGVLLYEMLTGK---------PPFYAENRKEIYEKILKSPL-----------KFP 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767973831 377 STWrcfatDPDgLRELLEDCWDADPEARLT---AECVQQrlaalahpqesHPF 426
Cdd:cd05123  214 EYV-----SPE-AKSLISGLLQKDPTKRLGsggAEEIKA-----------HPF 249
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
97-415 2.18e-12

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk 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: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 66.82  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQ-FQAERALyeLPGLQHDHIVRFItasrggpGRLL-SGPLLVLELHPK 174
Cdd:cd05083   12 EIIGEGEFGAVLQGEYMGQKVAVKNIKCDVTAQaFLEETAV--MTKLQHKNLVRLL-------GVILhNGLYIVMELMSK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 175 DCVC--LCPRGRAphnsLCPIGSLchyltqytsdwgssLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIRE 252
Cdd:cd05083   83 GNLVnfLRSRGRA----LVPVIQL--------------LQFSLDVAEGMEYLESKK---------LVHRDLAARNILVSE 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 253 DGSCAIGDLGLALVLPGLTQ----PPAWTptqpqgpaaimeagtqrymAPELLDKtldlqdwGMALRRADIYSLALLLWE 328
Cdd:cd05083  136 DGVAKISDFGLAKVGSMGVDnsrlPVKWT-------------------APEALKN-------KKFSSKSDVWSYGVLLWE 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 329 ILS--RCPdlrpdssPPPFQLAYEAElgntptsdelwalAVQERRRPYIPSTwrCfatdPDGLRELLEDCWDADPEARLT 406
Cdd:cd05083  190 VFSygRAP-------YPKMSVKEVKE-------------AVEKGYRMEPPEG--C----PPDVYSIMTSCWEAEPGKRPS 243

                 ....*....
gi 767973831 407 AECVQQRLA 415
Cdd:cd05083  244 FKKLREKLE 252
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
114-330 2.61e-12

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: 66.93  E-value: 2.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFPPRsVAQFQAERALYE---LPGLQHDHIVRFITAsrggpgRLLSGPLLV-LELhpkdcvclcprgraphns 189
Cdd:cd13996   31 GVTYAIKKIRLT-EKSSASEKVLREvkaLAKLNHPNIVRYYTA------WVEEPPLYIqMEL------------------ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 lCPIGSLCHYLTQYTS----DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI-REDGSCAIGDLGLA 264
Cdd:cd13996   86 -CEGGTLRDWIDRRNSssknDRKLALELFKQILKGVSYIHSK---------GIVHRDLKPSNIFLdNDDLQVKIGDFGLA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 265 LVLpGLTQPPAWTPTQPQGPAAIME---AGTQRYMAPELLDKTLDLQdwgmalrRADIYSLALLLWEIL 330
Cdd:cd13996  156 TSI-GNQKRELNNLNNNNNGNTSNNsvgIGTPLYASPEQLDGENYNE-------KADIYSLGIILFEML 216
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
96-420 2.67e-12

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


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 66.56  E-value: 2.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAGQLQ--GKLVAIKafppRSVAQFQAE----RALYELPGL----QHDHIVRFITASRGGpGRLLsgp 165
Cdd:cd14050    6 LSKLGEGSFGEVFKVRSRedGKLYAVK----RSRSRFRGEkdrkRKLEEVERHeklgEHPNCVRFIKAWEEK-GILY--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 166 lLVLELhpkdCVClcprgraphnSLCPIGSLCHYLTQYTSdWGsslrMALSLAQGLAFLHEErwqngqykpGIAHRDLSS 245
Cdd:cd14050   78 -IQTEL----CDT----------SLQQYCEETHSLPESEV-WN----ILLDLLKGLKHLHDH---------GLIHLDIKP 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 246 QNVLIREDGSCAIGDLGLALVLPGltqppawtptqpqgpAAIMEA--GTQRYMAPELLDktldlqdwGMALRRADIYSLA 323
Cdd:cd14050  129 ANIFLSKDGVCKLGDFGLVVELDK---------------EDIHDAqeGDPRYMAPELLQ--------GSFTKAADIFSLG 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 324 LLLWEilsrcpdlrpdsspppfqLAYEAELgntPTSDELWalavQERRRPYIPstWRCFATDPDGLRELLEDCWDADPEA 403
Cdd:cd14050  186 ITILE------------------LACNLEL---PSGGDGW----HQLRQGYLP--EEFTAGLSPELRSIIKLMMDPDPER 238
                        330
                 ....*....|....*..
gi 767973831 404 RLTAEcvqqrlAALAHP 420
Cdd:cd14050  239 RPTAE------DLLALP 249
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
114-404 3.89e-12

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 66.58  E-value: 3.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFPPRSVAQFQA-ERALYELPGLQHDHIVRFITASRGGPGRLLSgplLVLElhpkdcvclcprgraphnsLCP 192
Cdd:cd14205   33 GEVVAVKKLQHSTEEHLRDfEREIEILKSLQHDNIVKYKGVCYSAGRRNLR---LIME-------------------YLP 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 193 IGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLPgl 270
Cdd:cd14205   91 YGSLRDYLQKHKEriDHIKLLQYTSQICKGMEYLGTKRY---------IHRDLATRNILVENENRVKIGDFGLTKVLP-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 271 tQPPAWTPTQPQGPAAIMeagtqrYMAPELLDKTldlqDWGMAlrrADIYSLALLLWEILSRcpdLRPDSSPPPfqlAYE 350
Cdd:cd14205  160 -QDKEYYKVKEPGESPIF------WYAPESLTES----KFSVA---SDVWSFGVVLYELFTY---IEKSKSPPA---EFM 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 351 AELGNTPTSDELWALAVQERRRPY-IPSTWRCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd14205  220 RMIGNDKQGQMIVFHLIELLKNNGrLPRPDGC----PDEIYMIMTECWNNNVNQR 270
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
102-416 4.09e-12

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


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 66.48  E-value: 4.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 102 GGHAVVWAGQLQGKLVAIKAFPPRSVAQFQAERALYELPGLQHDHIVRFITASRGGPGRLLS------GPLLVLELHPKd 175
Cdd:cd14000    5 GGFGSVYRASYKGEPVAVKIFNKHTSSNFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHlhhpsiVYLLGIGIHPL- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 176 CVCLcprgraphnSLCPIGSLCHYLTQYTSDWGSSLRM-----ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI 250
Cdd:cd14000   84 MLVL---------ELAPLGSLDHLLQQDSRSFASLGRTlqqriALQVADGLRYLHSAM---------IIYRDLKSHNVLV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 -----REDGSCAIGDLGLAlvlpgltqppawTPTQPQGpaAIMEAGTQRYMAPELLDKTLDLQDwgmalrRADIYSLALL 325
Cdd:cd14000  146 wtlypNSAIIIKIADYGIS------------RQCCRMG--AKGSEGTPGFRAPEIARGNVIYNE------KVDVFSFGML 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 326 LWEILSrcpDLRPDSSPPPFQLAYEAELGNTPtsdelwalAVQERRRPYipstWRCfatdpdgLRELLEDCWDADPEARL 405
Cdd:cd14000  206 LYEILS---GGAPMVGHLKFPNEFDIHGGLRP--------PLKQYECAP----WPE-------VEVLMKKCWKENPQQRP 263
                        330
                 ....*....|.
gi 767973831 406 TAECVQQRLAA 416
Cdd:cd14000  264 TAVTVVSILNS 274
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
207-349 4.20e-12

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: 65.96  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIR--EDGSCAI-GDLGLAlvlpgltqppAWTPTQPQG 283
Cdd:cd14155   87 WTVRVKLALDIARGLSYLHSK---------GIFHRDLTSKNCLIKrdENGYTAVvGDFGLA----------EKIPDYSDG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 284 PAAIMEAGTQRYMAPELLDKTLDLQdwgmalrRADIYSLALLLWEILSRC---PDLRPDSS----------------PPP 344
Cdd:cd14155  148 KEKLAVVGSPYWMAPEVLRGEPYNE-------KADVFSYGIILCEIIARIqadPDYLPRTEdfgldydafqhmvgdcPPD 220

                 ....*.
gi 767973831 345 F-QLAY 349
Cdd:cd14155  221 FlQLAF 226
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
217-408 6.35e-12

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: 65.56  E-value: 6.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGTQRYM 296
Cdd:cd08215  112 ICLALKYLHSRK---------ILHRDLKTQNIFLTKDGVVKLGDFGISKVL---------ESTTDLAKTVV---GTPYYL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELL-DKTLDlqdwgmalRRADIYSLALLLWEILSrcpdLRpdsspPPFQlayeaelgntptSDELWALAVQERRRPY- 374
Cdd:cd08215  171 SPELCeNKPYN--------YKSDIWALGCVLYELCT----LK-----HPFE------------ANNLPALVYKIVKGQYp 221
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767973831 375 -IPSTWrcfatdPDGLRELLEDCWDADPEARLTAE 408
Cdd:cd08215  222 pIPSQY------SSELRDLVNSMLQKDPEKRPSAN 250
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
207-345 7.05e-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: 65.59  E-value: 7.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDG---SCAIGDLGLALVLPGLtqpPAWTPTQPQG 283
Cdd:cd14065   88 WSQRVSLAKDIASGMAYLHSKN---------IIHRDLNSKNCLVREANrgrNAVVADFGLAREMPDE---KTKKPDRKKR 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 284 PAAImeaGTQRYMAPELLDKTldlqdwgMALRRADIYSLALLLWEILSRCP--------------------DLRPDSSPP 343
Cdd:cd14065  156 LTVV---GSPYWMAPEMLRGE-------SYDEKVDVFSFGIVLCEIIGRVPadpdylprtmdfgldvrafrTLYVPDCPP 225

                 ..
gi 767973831 344 PF 345
Cdd:cd14065  226 SF 227
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
111-329 7.54e-12

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


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 65.91  E-value: 7.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 111 QLQGKLVAIKAFPPRSVAQFQAERALYELPGLQ------HDHIVRFITASRGGpGRLLsgplLVLELhpkdcvclcprgr 184
Cdd:cd14052   23 VPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILReltldgHDNIVQLIDSWEYH-GHLY----IQTEL------------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 185 aphnslCPIGSLCHYLTQYT-----SDWgSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIG 259
Cdd:cd14052   85 ------CENGSLDVFLSELGllgrlDEF-RVWKILVELSLGLRFIHDH---------HFVHLDLKPANVLITFEGTLKIG 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 260 DLGLALVLPgltqppawtptqpqGPAAIMEAGTQRYMAPELLDKtldlqdwGMALRRADIYSLALLLWEI 329
Cdd:cd14052  149 DFGMATVWP--------------LIRGIEREGDREYIAPEILSE-------HMYDKPADIFSLGLILLEA 197
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
102-404 7.90e-12

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


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 65.21  E-value: 7.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 102 GGHAVVWAGQLQGKLVAIKAfpprsvAQFQAERALYELPGLQHDHIVRFitasRGgpgrllsgpllVLELHPKDCVCLcp 181
Cdd:cd14059    4 GAQGAVFLGKFRGEEVAVKK------VRDEKETDIKHLRKLNHPNIIKF----KG-----------VCTQAPCYCILM-- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 182 rgraphnSLCPIGSLCHYLTQ-------YTSDWgsslrmALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDG 254
Cdd:cd14059   61 -------EYCPYGQLYEVLRAgreitpsLLVDW------SKQIASGMNYLHLHK---------IIHRDLKSPNVLVTYND 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 255 SCAIGDLGlalvlpgltqppawTPTQPQGPAAIME-AGTQRYMAPELLDKTldlqdwgMALRRADIYSLALLLWEILSRc 333
Cdd:cd14059  119 VLKISDFG--------------TSKELSEKSTKMSfAGTVAWMAPEVIRNE-------PCSEKVDIWSFGVVLWELLTG- 176
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973831 334 pdlrpdsspppfQLAYEaelgNTPTSDELWALAVQERRRPyIPSTwrCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd14059  177 ------------EIPYK----DVDSSAIIWGVGSNSLQLP-VPST--C----PDGFKLLMKQCWNSKPRNR 224
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
107-414 9.41e-12

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: 65.00  E-value: 9.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 107 VWAGQLQGKL-VAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVR-FITASRGGPgrllsgPLLVLELHPKdcvclcpr 182
Cdd:cd05034   11 VWMGVWNGTTkVAVKTLKPgtMSPEAFLQEAQI--MKKLRHDKLVQlYAVCSDEEP------IYIVTELMSK-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 183 graphnslcpiGSLCHYLTqytSDWGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSC 256
Cdd:cd05034   75 -----------GSLLDYLR---TGEGRALRlpqlidMAAQIASGMAYLESRNY---------IHRDLAARNILVGENNVC 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVLP--------GLTQPPAWTptqpqgpaaimeagtqrymAPE-LLDKTLDLqdwgmalrRADIYSLALLLW 327
Cdd:cd05034  132 KVADFGLARLIEddeytareGAKFPIKWT-------------------APEaALYGRFTI--------KSDVWSFGILLY 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 328 EILS--RCPdlrpdsspppfqlaYEAeLGNTPTSDELwalavqER--RRPYIPStwrCfatdPDGLRELLEDCWDADPEA 403
Cdd:cd05034  185 EIVTygRVP--------------YPG-MTNREVLEQV------ERgyRMPKPPG---C----PDELYDIMLQCWKKEPEE 236
                        330
                 ....*....|.
gi 767973831 404 RLTAECVQQRL 414
Cdd:cd05034  237 RPTFEYLQSFL 247
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
103-328 1.44e-11

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: 65.08  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 103 GHAVVWAGQLQGKLVAIKAFPPRSvAQFQAERALYE---LPGLQHDHIVRFITAsrggpgRLLSGPLLV-LELhpkdcvc 178
Cdd:cd14046   20 GQVVKVRNKLDGRYYAIKKIKLRS-ESKNNSRILREvmlLSRLNHQHVVRYYQA------WIERANLYIqMEY------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 179 lcprgraphnslCPIGSLCH----YLTQYTSD-WgsslRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIRED 253
Cdd:cd14046   86 ------------CEKSTLRDlidsGLFQDTDRlW----RLFRQILEGLAYIHSQ---------GIIHRDLKPVNIFLDSN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 254 GSCAIGDLGLA----LVLPGLTQPPAWTPTQPQGPAAIM--EAGTQRYMAPELLDKTldlqdWGMALRRADIYSLALLLW 327
Cdd:cd14046  141 GNVKIGDFGLAtsnkLNVELATQDINKSTSAALGSSGDLtgNVGTALYVAPEVQSGT-----KSTYNEKVDMYSLGIIFF 215

                 .
gi 767973831 328 E 328
Cdd:cd14046  216 E 216
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
114-412 1.57e-11

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: 64.63  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIK--AFPPRSVAQFQA-ERALYELPGLQHDHIVRFitasrggpgrllsgplLVLELHpKDCVCLcprgrapHNSL 190
Cdd:cd06626   25 GELMAMKeiRFQDNDPKTIKEiADEMKVLEGLDHPNLVRY----------------YGVEVH-REEVYI-------FMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYLtqytsDWGSSL------RMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 264
Cdd:cd06626   81 CQEGTLEELL-----RHGRILdeavirVYTLQLLEGLAYLHEN---------GIVHRDIKPANIFLDSNGLIKLGDFGSA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 LVLPGLTQPPawtptqPQGPAAIMeAGTQRYMAPELLDKTlDLQDWGmalRRADIYSLALLlweILSRCPDLRP----DS 340
Cdd:cd06626  147 VKLKNNTTTM------APGEVNSL-VGTPAYMAPEVITGN-KGEGHG---RAADIWSLGCV---VLEMATGKRPwselDN 212
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 341 sppPFQLAYEAELGNT---PTSDELwalavqerrrpyipstwrcfatDPDGlRELLEDCWDADPEARLTAECVQQ 412
Cdd:cd06626  213 ---EWAIMYHVGMGHKppiPDSLQL----------------------SPEG-KDFLSRCLESDPKKRPTASELLD 261
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
194-414 1.88e-11

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: 64.35  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLtqytSDWGSSLR------MALSLAQGLAFLHEerwQNgqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 267
Cdd:cd05068   88 GSLLEYL----QGKGRSLQlpqlidMAAQVASGMAYLES---QN------YIHRDLAARNVLVGENNICKVADFGLARVI 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 268 ---------PGLTQPPAWTptqpqGPAAIMeagTQRYMApelldktldlqdwgmalrRADIYSLALLLWEILSrcpdlrp 338
Cdd:cd05068  155 kvedeyearEGAKFPIKWT-----APEAAN---YNRFSI------------------KSDVWSFGILLTEIVT------- 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973831 339 dsspppfqlayeaeLGNTPTSDELWALAVQERRRPY-IPstwrCFATDPDGLRELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd05068  202 --------------YGRIPYPGMTNAEVLQQVERGYrMP----CPPNCPPQLYDIMLECWKADPMERPTFETLQWKL 260
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
219-420 1.98e-11

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: 64.15  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtpTQPQGPAAIMeAGTQRYMAP 298
Cdd:cd06614  108 QGLEYLH---------SQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL-----------TKEKSKRNSV-VGTPYWMAP 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLDKtldlQDWGMalrRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTSDELWALavqerrrpyipst 378
Cdd:cd06614  167 EVIKR----KDYGP---KVDIWSLGIMCIEMAEGEP---PYLEEPPLRALFLITTKGIPPLKNPEKW------------- 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767973831 379 wrcfatDPDgLRELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd06614  224 ------SPE-FKDFLNKCLVKDPEKRPSAE------ELLQHP 252
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
207-338 1.99e-11

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: 64.21  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPT--QPQGP 284
Cdd:cd14221   90 WSQRVSFAKDIASGMAYLHSMN---------IIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSlkKPDRK 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 285 AAIMEAGTQRYMAPELLD-KTLDlqdwgmalRRADIYSLALLLWEILSRC---PDLRP 338
Cdd:cd14221  161 KRYTVVGNPYWMAPEMINgRSYD--------EKVDVFSFGIVLCEIIGRVnadPDYLP 210
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
98-426 2.33e-11

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: 63.76  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQ--LQGKLVAIKAFPPRSVAQFQ---AERALyeLPGLQHDHIVRFITASrggpgrLLSGPL-LVLEL 171
Cdd:cd05122    7 KIGKGGFGVVYKARhkKTGQIVAIKKINLESKEKKEsilNEIAI--LKKCKHPNIVKYYGSY------LKKDELwIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 172 hpkdcvclCPRG------RAPHNSLCP--IGSLCHyltqytsdwgsslrmalSLAQGLAFLHEErwqngqykpGIAHRDL 243
Cdd:cd05122   79 --------CSGGslkdllKNTNKTLTEqqIAYVCK-----------------EVLKGLEYLHSH---------GIIHRDI 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 244 SSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQ-GPAAIMEAGTQRYMAPE-LLDKTLDLQdwgmalrrADIYS 321
Cdd:cd05122  125 KAANILLTSDGEVKLIDFGLS--------------AQLSdGKTRNTFVGTPYWMAPEvIQGKPYGFK--------ADIWS 182
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 322 LALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTSDElwalavqerrrpyiPSTWrcfatdPDGLRELLEDCWDADP 401
Cdd:cd05122  183 LGITAIEMAEGKP---PYSELPPMKALFLIATNGPPGLRN--------------PKKW------SKEFKDFLKKCLQKDP 239
                        330       340
                 ....*....|....*....|....*
gi 767973831 402 EARLTAEcvqQRLAalahpqesHPF 426
Cdd:cd05122  240 EKRPTAE---QLLK--------HPF 253
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
101-416 2.48e-11

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: 63.99  E-value: 2.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 101 EGGHAVVWAGQLQGKL-VAIKAFPPRSVA---QFQAEraLYELPGLQHDHIVR-FITASRGGPgrllsgPLLVLELHPKd 175
Cdd:cd05148   16 SGYFGEVWEGLWKNRVrVAIKILKSDDLLkqqDFQKE--VQALKRLRHKHLISlFAVCSVGEP------VYIITELMEK- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 176 cvclcprgraphnslcpiGSLCHYLTqytSDWGSSLR------MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVL 249
Cdd:cd05148   87 ------------------GSLLAFLR---SPEGQVLPvaslidMACQVAEGMAYLEEQN---------SIHRDLAARNIL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 250 IREDGSCAIGDLGLALVLpgltQPPAWTPTQPQGPAaimeagtqRYMAPELLdktldlqDWGMALRRADIYSLALLLWEI 329
Cdd:cd05148  137 VGEDLVCKVADFGLARLI----KEDVYLSSDKKIPY--------KWTAPEAA-------SHGTFSTKSDVWSFGILLYEM 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 330 LSRCpdlrpdsspppfQLAYEAElgntpTSDELWALAVQERRrpyIPSTWRCfatdPDGLRELLEDCWDADPEARLTAEC 409
Cdd:cd05148  198 FTYG------------QVPYPGM-----NNHEVYDQITAGYR---MPCPAKC----PQEIYKIMLECWAAEPEDRPSFKA 253

                 ....*..
gi 767973831 410 VQQRLAA 416
Cdd:cd05148  254 LREELDN 260
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
146-406 2.77e-11

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: 63.90  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 146 HIVRFI-TASRGGPgrllsgPLLVLELHPKDCVCLCPRGRAPHNSLCPIGSLCHYltqytsdwGSSLRMALSLAQGLAFL 224
Cdd:cd05032   70 HVVRLLgVVSTGQP------TLVVMELMAKGDLKSYLRSRRPEAENNPGLGPPTL--------QKFIQMAAEIADGMAYL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 225 HEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppAWTPTQPQGPAAIMEAgtqRYMAPElldkt 304
Cdd:cd05032  136 AAKK---------FVHRDLAARNCMVAEDLTVKIGDFGMTRDI-------YETDYYRKGGKGLLPV---RWMAPE----- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 305 lDLQDwGMALRRADIYSLALLLWEIlsrcpdlrpdsspppfqlayeAELGNTP----TSDELWALAVQerrRPYIPSTWR 380
Cdd:cd05032  192 -SLKD-GVFTTKSDVWSFGVVLWEM---------------------ATLAEQPyqglSNEEVLKFVID---GGHLDLPEN 245
                        250       260
                 ....*....|....*....|....*.
gi 767973831 381 CfatdPDGLRELLEDCWDADPEARLT 406
Cdd:cd05032  246 C----PDKLLELMRMCWQYNPKMRPT 267
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
207-414 3.76e-11

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 63.28  E-value: 3.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALvlpgltqppawtptqpqgPAA 286
Cdd:cd13975  101 LEERLQIALDVVEGIRFLHSQ---------GLVHRDIKLKNVLLDKKNRAKITDLGFCK------------------PEA 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 287 IMEA---GTQRYMAPELLDKTLDlqdwgmalRRADIYSLALLLWEILS---RCPDlrpdsspppfqlAYEaelgNTPTSD 360
Cdd:cd13975  154 MMSGsivGTPIHMAPELFSGKYD--------NSVDVYAFGILFWYLCAghvKLPE------------AFE----QCASKD 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 361 ELW---ALAVQERRRP-YIPSTWRcfatdpdglreLLEDCWDADPEARLTAECVQQRL 414
Cdd:cd13975  210 HLWnnvRKGVRPERLPvFDEECWN-----------LMEACWSGDPSQRPLLGIVQPKL 256
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
96-414 4.05e-11

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 63.46  E-value: 4.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAGQLQGKLVAIKAFPPRSVAQ-FQAERALyeLPGLQHDHIVRFITASRGGPGRLLsgplLVLELHPK 174
Cdd:cd05082   11 LQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQaFLAEASV--MTQLRHSNLVQLLGVIVEEKGGLY----IVTEYMAK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 175 DCVC--LCPRGRAPhnslcpIGSLChyltqytsdwgsSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIRE 252
Cdd:cd05082   85 GSLVdyLRSRGRSV------LGGDC------------LLKFSLDVCEAMEYLEGNNF---------VHRDLAARNVLVSE 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 253 DGSCAIGDLGLALVLPGlTQPPAWTPTQPQGPAAIMEagtQRYMApelldktldlqdwgmalrRADIYSLALLLWEILS- 331
Cdd:cd05082  138 DNVAKVSDFGLTKEASS-TQDTGKLPVKWTAPEALRE---KKFST------------------KSDVWSFGILLWEIYSf 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 332 -RCPDLRpdsspppfqlayeaelgntptsdelwaLAVQErrrpYIPSTWRCFATD-PDG----LRELLEDCWDADPEARL 405
Cdd:cd05082  196 gRVPYPR---------------------------IPLKD----VVPRVEKGYKMDaPDGcppaVYDVMKNCWHLDAAMRP 244

                 ....*....
gi 767973831 406 TAECVQQRL 414
Cdd:cd05082  245 SFLQLREQL 253
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
96-419 6.78e-11

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: 62.74  E-value: 6.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAGQLQ--GKLVAIKA---FPPRSVAQFQAERALY-ELPglQHDHIVRFI-TASRGGPGRllSGPLLV 168
Cdd:cd13985    5 TKQLGEGGFSYVYLAHDVntGRRYALKRmyfNDEEQLRVAIKEIEIMkRLC--GHPNIVQYYdSAILSSEGR--KEVLLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 169 LELhpkdcvclcprgraphnslCPiGSLCHYL-----TQYTSDwgSSLRMALSLAQGLAFLHeerwqngQYKPGIAHRDL 243
Cdd:cd13985   81 MEY-------------------CP-GSLVDILeksppSPLSEE--EVLRIFYQICQAVGHLH-------SQSPPIIHRDI 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 244 SSQNVLIREDGSCAIGDLGLAlvlpgLTQPPAWTPTQpqgPAAIMEAGTQRYM-----APELldktLDLQDWGMALRRAD 318
Cdd:cd13985  132 KIENILFSNTGRFKLCDFGSA-----TTEHYPLERAE---EVNIIEEEIQKNTtpmyrAPEM----IDLYSKKPIGEKAD 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 319 IYSLALLLWEILSRcpdlrpdssPPPFqlayeaelgntptsDELWALAVQERRRPyIPSTWRCfatdPDGLRELLEDCWD 398
Cdd:cd13985  200 IWALGCLLYKLCFF---------KLPF--------------DESSKLAIVAGKYS-IPEQPRY----SPELHDLIRHMLT 251
                        330       340
                 ....*....|....*....|.
gi 767973831 399 ADPEARLTAECVQQRLAALAH 419
Cdd:cd13985  252 PDPAERPDIFQVINIITKDTK 272
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
99-330 7.85e-11

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: 62.24  E-value: 7.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAG--QLQGKLVAIKAFP-----PRSVAQFQAERALyeLPGLQHDHIVRFITASRGgPGRLLsgplLVLEL 171
Cdd:cd14009    1 IGRGSFATVWKGrhKQTGEVVAIKEISrkklnKKLQENLESEIAI--LKSIKHPNIVRLYDVQKT-EDFIY----LVLEY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 172 hpkdcvclcprgraphnslCPIGSLCHYLTQY---TSDwgSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNV 248
Cdd:cd14009   74 -------------------CAGGDLSQYIRKRgrlPEA--VARHFMQQLASGLKFLRSK---------NIIHRDLKPQNL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 249 LIREDGSCA---IGDLGLALVLpgltqppawtptQPQGPAAIMeAGTQRYMAPELldktLDLQDWGMalrRADIYSLALL 325
Cdd:cd14009  124 LLSTSGDDPvlkIADFGFARSL------------QPASMAETL-CGSPLYMAPEI----LQFQKYDA---KADLWSVGAI 183

                 ....*
gi 767973831 326 LWEIL 330
Cdd:cd14009  184 LFEML 188
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
96-404 9.51e-11

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: 62.37  E-value: 9.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAGQLQGKLVAIKAF---PPRSVAQ----FQAERALYELpgLQHDHIVRF-------------ITASR 155
Cdd:cd14145   11 EEIIGIGGFGKVYRAIWIGDEVAVKAArhdPDEDISQtienVRQEAKLFAM--LKHPNIIALrgvclkepnlclvMEFAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 156 GGP-GRLLSGPllvlelhpkdcvclcprgRAPHNSLCpigslchyltqytsDWgsslrmALSLAQGLAFLHEErwqngQY 234
Cdd:cd14145   89 GGPlNRVLSGK------------------RIPPDILV--------------NW------AVQIARGMNYLHCE-----AI 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 235 KPgIAHRDLSSQNVLIR---EDGSCA-----IGDLGLAlvlpgltqpPAWTPTqpqgpAAIMEAGTQRYMAPELLDKTld 306
Cdd:cd14145  126 VP-VIHRDLKSSNILILekvENGDLSnkilkITDFGLA---------REWHRT-----TKMSAAGTYAWMAPEVIRSS-- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 307 lqdwgMALRRADIYSLALLLWEILsrcpdlrpdSSPPPFQ------LAYeaelgntptsdelwALAVQERRRPyIPSTwr 380
Cdd:cd14145  189 -----MFSKGSDVWSYGVLLWELL---------TGEVPFRgidglaVAY--------------GVAMNKLSLP-IPST-- 237
                        330       340
                 ....*....|....*....|....
gi 767973831 381 CfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd14145  238 C----PEPFARLMEDCWNPDPHSR 257
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
191-413 9.91e-11

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: 62.37  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYLT---QYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIRED-GSCAIGDLGLALv 266
Cdd:cd13993   87 CPNGDLFEAITenrIYVGKTELIKNVFLQLIDAVKHCHSL---------GIYHRDIKPENILLSQDeGTVKLCDFGLAT- 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 267 lpgltqppawtpTQPQGPAAimEAGTQRYMAPELLDKTLDLQDwGMALRRADIYSLALLLWEILS-RCPDLRPDSSPPPF 345
Cdd:cd13993  157 ------------TEKISMDF--GVGSEFYMAPECFDEVGRSLK-GYPCAAGDIWSLGIILLNLTFgRNPWKIASESDPIF 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 346 QLAYEAElgntptsdelwalavqerrrpyiPSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQR 413
Cdd:cd13993  222 YDYYLNS-----------------------PNLFDVILPMSDDFYNLLRQIFTVNPNNRILLPELQLL 266
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
210-352 1.14e-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: 62.12  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 210 SLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIME 289
Cdd:cd14047  119 ALEIFEQITKGVEYIHSK---------KLIHRDLKPSNIFLVDTGKVKIGDFGLV--------------TSLKNDGKRTK 175
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 290 A-GTQRYMAPElldkTLDLQDWGmalRRADIYSLALLLWEILSRC----------PDLRPDSSPPPFQLAYEAE 352
Cdd:cd14047  176 SkGTLSYMSPE----QISSQDYG---KEVDIYALGLILFELLHVCdsafekskfwTDLRNGILPDIFDKRYKIE 242
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
217-408 1.15e-10

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: 62.17  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERWQNGQykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQppawtptqpqgpAAIMEAGTQRYM 296
Cdd:cd08217  114 LLLALYECHNRSVGGGK----ILHRDLKPANIFLDSDNNVKLGDFGLARVLSHDSS------------FAKTYVGTPYYM 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELL-DKTLDlqdwgmalRRADIYSLALLLWEILSrcpdLRpdsspPPFQLAYEAELgntptsdelwALAVQERRRPYI 375
Cdd:cd08217  178 SPELLnEQSYD--------EKSDIWSLGCLIYELCA----LH-----PPFQAANQLEL----------AKKIKEGKFPRI 230
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767973831 376 PSTWRcfatdpDGLRELLEDCWDADPEARLTAE 408
Cdd:cd08217  231 PSRYS------SELNEVIKSMLNVDPDKRPSVE 257
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
98-407 1.17e-10

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: 62.04  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQ-LQGKL-VAIKAFPPRSVAQFQA---ERALYElpGLQHDHIVRFITA-SRGG---------PGRLL 162
Cdd:cd06624   15 VLGKGTFGVVYAARdLSTQVrIAIKEIPERDSREVQPlheEIALHS--RLSHKNIVQYLGSvSEDGffkifmeqvPGGSL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 163 S-------GPLLVLElhpkdcvclcprgraphnslcpiGSLCHYLTQytsdwgsslrmalsLAQGLAFLHEERwqngqyk 235
Cdd:cd06624   93 SallrskwGPLKDNE-----------------------NTIGYYTKQ--------------ILEGLKYLHDNK------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 236 pgIAHRDLSSQNVLIRE-DGSCAIGDLGLALVLPGLTqppawtptqpqgPAAIMEAGTQRYMAPELLDKtlDLQDWGMAl 314
Cdd:cd06624  129 --IVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGIN------------PCTETFTGTLQYMAPEVIDK--GQRGYGPP- 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 315 rrADIYSLALLLWEILSrcpdlrpdSSPPPFqlayeaELGNtPTSdelwalAVQE----RRRPYIPSTWRcfatdpDGLR 390
Cdd:cd06624  192 --ADIWSLGCTIIEMAT--------GKPPFI------ELGE-PQA------AMFKvgmfKIHPEIPESLS------EEAK 242
                        330
                 ....*....|....*..
gi 767973831 391 ELLEDCWDADPEARLTA 407
Cdd:cd06624  243 SFILRCFEPDPDKRATA 259
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
211-407 1.19e-10

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK 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: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 62.42  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEERWqngqykpgIAHRDLSSQNVLIRED-GSCAIGDLGLALVLPGLTQppawTPTQPQGpaaiME 289
Cdd:cd14001  113 LKVALSIARALEYLHNEKK--------ILHGDIKSGNVLIKGDfESVKLCDFGVSLPLTENLE----VDSDPKA----QY 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 290 AGTQRYMAPELLDKTLDLQDwgmalrRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAElgnTPTSDELWALAVQE 369
Cdd:cd14001  177 VGTEPWKAKEALEEGGVITD------KADIFAYGLVLWEMMTLSV---PHLNLLDIEDDDEDE---SFDEDEEDEEAYYG 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767973831 370 RR--RPYIPSTWRCFATDPdgLRELLEDCWDADPEARLTA 407
Cdd:cd14001  245 TLgtRPALNLGELDDSYQK--VIELFYACTQEDPKDRPSA 282
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
110-406 1.19e-10

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 62.25  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 110 GQLQGKLVAIKAFPPRSVAQFQAE--RALYELPGLQHDHIVRF--ITASRGGpgrllSGPLLVLELHPKdcvclcprgra 185
Cdd:cd05079   29 GDNTGEQVAVKSLKPESGGNHIADlkKEIEILRNLYHENIVKYkgICTEDGG-----NGIKLIMEFLPS----------- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 186 phnslcpiGSLCHYLTQYTS--DWGSSLRMALSLAQGLAFLHEErwqngQYkpgiAHRDLSSQNVLIREDGSCAIGDLGL 263
Cdd:cd05079   93 --------GSLKEYLPRNKNkiNLKQQLKYAVQICKGMDYLGSR-----QY----VHRDLAARNVLVESEHQVKIGDFGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 264 A----------LVLPGLTQPPAWtptqpqgpaaimeagtqryMAPELLDKTldlqdwgMALRRADIYSLALLLWEILSRC 333
Cdd:cd05079  156 TkaietdkeyyTVKDDLDSPVFW-------------------YAPECLIQS-------KFYIASDVWSFGVTLYELLTYC 209
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973831 334 pdlRPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPYIPStwrCfatdPDGLRELLEDCWDADPEARLT 406
Cdd:cd05079  210 ---DSESSPMTLFLKMIGPTHGQMTVTRLVRVLEEGKRLPRPPN---C----PEEVYQLMRKCWEFQPSKRTT 272
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
107-414 1.50e-10

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: 61.98  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 107 VWAGQLQGKL-VAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVR-FITASRGGPgrllsgPLLVLELHPKdcvclcpr 182
Cdd:cd05072   23 VWMGYYNNSTkVAVKTLKPgtMSVQAFLEEANL--MKTLQHDKLVRlYAVVTKEEP------IYIITEYMAK-------- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 183 graphnslcpiGSLCHYLTqytSDWGSSLRM------ALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSC 256
Cdd:cd05072   87 -----------GSLLDFLK---SDEGGKVLLpklidfSAQIAEGMAYIERKNY---------IHRDLRAANVLVSESLMC 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 257 AIGDLGLALVL--------PGLTQPPAWTptqpqgpaaimeagtqrymAPELLdktldlqDWGMALRRADIYSLALLLWE 328
Cdd:cd05072  144 KIADFGLARVIedneytarEGAKFPIKWT-------------------APEAI-------NFGSFTIKSDVWSFGILLYE 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 329 ILSRCPDLRPDSSpppfqlayeaelgntpTSDELWALavqerRRPY-IPSTWRCfatdPDGLRELLEDCWDADPEARLTA 407
Cdd:cd05072  198 IVTYGKIPYPGMS----------------NSDVMSAL-----QRGYrMPRMENC----PDELYDIMKTCWKEKAEERPTF 252

                 ....*..
gi 767973831 408 ECVQQRL 414
Cdd:cd05072  253 DYLQSVL 259
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
91-417 1.59e-10

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


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 61.58  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  91 RTTECEQVIREGGHAVVWAGQLQGKLVAIKAF---PPRSVA----QFQAERALYELpgLQHDHIVRFitasrggPGRLLS 163
Cdd:cd14147    3 QELRLEEVIGIGGFGKVYRGSWRGELVAVKAArqdPDEDISvtaeSVRQEARLFAM--LAHPNIIAL-------KAVCLE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 164 GPLLVLELhpkDCVCLCPRGRAPHNSLCPIgslcHYLTQYtsdwgsslrmALSLAQGLAFLHEErwqngQYKPGIaHRDL 243
Cdd:cd14147   74 EPNLCLVM---EYAAGGPLSRALAGRRVPP----HVLVNW----------AVQIARGMHYLHCE-----ALVPVI-HRDL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 244 SSQNVLI--------REDGSCAIGDLGLAlvlpgltqpPAWTPTqpqgpAAIMEAGTQRYMAPELLDKTldlqDWGMAlr 315
Cdd:cd14147  131 KSNNILLlqpienddMEHKTLKITDFGLA---------REWHKT-----TQMSAAGTYAWMAPEVIKAS----TFSKG-- 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 316 rADIYSLALLLWEILSrcpDLRPDSSPPPFQLAYeaelgntptsdelwALAVQERRRPyIPSTwrCfatdPDGLRELLED 395
Cdd:cd14147  191 -SDVWSFGVLLWELLT---GEVPYRGIDCLAVAY--------------GVAVNKLTLP-IPST--C----PEPFAQLMAD 245
                        330       340
                 ....*....|....*....|..
gi 767973831 396 CWDADPEARLTAECVQQRLAAL 417
Cdd:cd14147  246 CWAQDPHRRPDFASILQQLEAL 267
Pkinase pfam00069
Protein kinase domain;
96-420 1.62e-10

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 60.72  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831   96 EQVIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITAsrggpgrllsgpllvle 170
Cdd:pfam00069   4 LRKLGSGSFGTVYKAKHRdtGKIVAIKKIKKEKIKKKKDKNILREikiLKKLNHPNIVRLYDA----------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  171 LHPKDCVCLCprgraphNSLCPIGSLCHYLTQYTSdwgsslrmalslaqglaflheerwqngqykpgIAHRDLSSqnvLI 250
Cdd:pfam00069  67 FEDKDNLYLV-------LEYVEGGSLFDLLSEKGA--------------------------------FSEREAKF---IM 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  251 REdgscaigdlglalVLPGL-TQPPAWTPTqpqgpaaimeaGTQRYMAPELLDKTldlqdwgMALRRADIYSLALLLWEI 329
Cdd:pfam00069 105 KQ-------------ILEGLeSGSSLTTFV-----------GTPWYMAPEVLGGN-------PYGPKVDVWSLGCILYEL 153
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  330 LSRCPdlrpdssppPFQlayeaelgNTPTSDELWALAVQERRRPYIPSTWrcfatdPDGLRELLEDCWDADPEARLTAEc 409
Cdd:pfam00069 154 LTGKP---------PFP--------GINGNEIYELIIDQPYAFPELPSNL------SEEAKDLLKKLLKKDPSKRLTAT- 209
                         330
                  ....*....|.
gi 767973831  410 vqqrlAALAHP 420
Cdd:pfam00069 210 -----QALQHP 215
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
114-375 1.65e-10

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 61.25  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRGGpgrllsgpllvlelhpkdcvclcprgraphNSL 190
Cdd:cd08530   25 NQVYALKEVNLGSLSQKEREDSVNEirlLASVNHPNIIRYKEAFLDG------------------------------NRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 C------PIGSLCHYLTQYTSD---------WgsslRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGS 255
Cdd:cd08530   75 CivmeyaPFGDLSKLISKRKKKrrlfpeddiW----RIFIQMLRGLKALHDQ---------KILHRDLKSANILLSAGDL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 256 CAIGDLGLALVLPGltqppAWTPTQpqgpaaimeAGTQRYMAPELL-DKTLDLqdwgmalrRADIYSLALLLWEILSrcp 334
Cdd:cd08530  142 VKIGDLGISKVLKK-----NLAKTQ---------IGTPLYAAPEVWkGRPYDY--------KSDIWSLGCLLYEMAT--- 196
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767973831 335 dLRpdsspPPFQ------LAYEAELGNTPT-----SDEL-----WALAVQERRRPYI 375
Cdd:cd08530  197 -FR-----PPFEartmqeLRYKVCRGKFPPippvySQDLqqiirSLLQVNPKKRPSC 247
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
212-420 1.75e-10

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 61.42  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTptqpqgpaaimeAG 291
Cdd:cd14008  112 KYFRDLVLGLEYLHEN---------GIVHRDIKPENLLLTADGTVKISDFGVSEMFEDGNDTLQKT------------AG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 292 TQRYMAPELLDKTLDLQDwGMAlrrADIYSLALLLWEILSRCpdlrpdsspPPFqlayeaelgNTPTSDELwALAVQERR 371
Cdd:cd14008  171 TPAFLAPELCDGDSKTYS-GKA---ADIWALGVTLYCLVFGR---------LPF---------NGDNILEL-YEAIQNQN 227
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767973831 372 RPYIPStwrcfATDPDGLRELLEDCWDADPEARLTAECVQQrlaalaHP 420
Cdd:cd14008  228 DEFPIP-----PELSPELKDLLRRMLEKDPEKRITLKEIKE------HP 265
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
97-414 1.77e-10

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: 61.31  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQGK--LVAIKA----FPPRSVAQF-QAERALyelpgLQHDH--IVRFITASrggpgrLLSGPLL 167
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDntEVAVKTcretLPPDLKRKFlQEARIL-----KQYDHpnIVKLIGVC------VQKQPIM 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 168 -VLELHPKdcvclcprgraphnslcpiGSLCHYLTQYTSDW--GSSLRMALSLAQGLAFLhEERwqngqykpGIAHRDLS 244
Cdd:cd05041   70 iVMELVPG-------------------GSLLTFLRKKGARLtvKQLLQMCLDAAAGMEYL-ESK--------NCIHRDLA 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIREDGSCAIGDLGLA--------LVLPGLTQ-PPAWTptqpqgpaaimeagtqrymAPELLdktldlqDWGMALR 315
Cdd:cd05041  122 ARNCLVGENNVLKISDFGMSreeedgeyTVSDGLKQiPIKWT-------------------APEAL-------NYGRYTS 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 316 RADIYSLALLLWEILSrcpdlrpdsspppfqlayeaeLGNTPTSDelwalAVQERRRPYIPSTWRCFATD--PDGLRELL 393
Cdd:cd05041  176 ESDVWSFGILLWEIFS---------------------LGATPYPG-----MSNQQTREQIESGYRMPAPElcPEAVYRLM 229
                        330       340
                 ....*....|....*....|.
gi 767973831 394 EDCWDADPEARLTAECVQQRL 414
Cdd:cd05041  230 LQCWAYDPENRPSFSEIYNEL 250
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
100-334 1.82e-10

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 61.47  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 100 REGGHAVVWaGQLQgklvaIKAFPPRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLsgpLLVLELhpkdcvcl 179
Cdd:cd13983   23 TEEGIEVAW-NEIK-----LRKLPKAERQRFKQEIEI--LKSLKHPNIIKFYDSWESKSKKEV---IFITEL-------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 180 cprgraphnslCPIGSLCHYLTQYT-------SDWGsslRMALslaQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR- 251
Cdd:cd13983   84 -----------MTSGTLKQYLKRFKrlklkviKSWC---RQIL---EGLNYLHTR-------DPPIIHRDLKCDNIFINg 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 252 EDGSCAIGDLGLAlvlpgltqppawTPTQPQGPAAIMeaGTQRYMAPELLDKTLDlqdwgmalRRADIYSLALLLWEIL- 330
Cdd:cd13983  140 NTGEVKIGDLGLA------------TLLRQSFAKSVI--GTPEFMAPEMYEEHYD--------EKVDIYAFGMCLLEMAt 197

                 ....
gi 767973831 331 SRCP 334
Cdd:cd13983  198 GEYP 201
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
102-331 2.70e-10

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: 61.00  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 102 GGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAER-ALYELPGLQHDHiVRFITAsrggpgrllsgplLVLELHPKDCVC 178
Cdd:cd05577    4 GGFGEVCACQVKatGKMYACKKLDKKRIKKKKGETmALNEKIILEKVS-SPFIVS-------------LAYAFETKDKLC 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 179 LCPrgraphnSLCPIGSLCHYLTQYTSDWGSSLRMALSLAQ---GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGS 255
Cdd:cd05577   70 LVL-------TLMNGGDLKYHIYNVGTRGFSEARAIFYAAEiicGLEHLHNRF---------IVYRDLKPENILLDDHGH 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 256 CAIGDLGLALVLPGLTQPPAwtptqpqgpaaimEAGTQRYMAPELLDKTLDLQdwgmalRRADIYSLALLLWEILS 331
Cdd:cd05577  134 VRISDLGLAVEFKGGKKIKG-------------RVGTHGYMAPEVLQKEVAYD------FSVDWFALGCMLYEMIA 190
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
207-338 5.26e-10

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: 60.34  E-value: 5.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA-LVLPGLTQPPAWTPTQPQGPA 285
Cdd:cd14222   89 WQQKVSFAKGIASGMAYLHSM---------SIIHRDLNSHNCLIKLDKTVVVADFGLSrLIVEEKKKPPPDKPTTKKRTL 159
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 286 AIME-------AGTQRYMAPELLD-KTLDlqdwgmalRRADIYSLALLLWEILSRC---PDLRP 338
Cdd:cd14222  160 RKNDrkkrytvVGNPYWMAPEMLNgKSYD--------EKVDIFSFGIVLCEIIGQVyadPDCLP 215
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
196-404 5.71e-10

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 60.32  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 196 LCHYLTQYTS-DWGSSLRMALSLAQGLAFLHeerwqngQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqpp 274
Cdd:cd14026   87 LLHEKDIYPDvAWPLRLRILYEIALGVNYLH-------NMSPPLLHHDLKTQNILLDGEFHVKIADFGLS---------- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 275 AW---TPTQPQGPAAIMEAGTQRYMAPELLDKTldlqdwgmALRRA----DIYSLALLLWEILSRCPDLrpDSSPPPFQL 347
Cdd:cd14026  150 KWrqlSISQSRSSKSAPEGGTIIYMPPEEYEPS--------QKRRAsvkhDIYSYAIIMWEVLSRKIPF--EEVTNPLQI 219
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 348 AYEAELGNTPTsdelwalaVQERRRPY-IPSTWRcfatdpdgLRELLEDCWDADPEAR 404
Cdd:cd14026  220 MYSVSQGHRPD--------TGEDSLPVdIPHRAT--------LINLIESGWAQNPDER 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
201-420 5.71e-10

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: 59.65  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 201 TQYTSDWGSslRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDG----SCAIGDLGLALVLPGltqpPAW 276
Cdd:cd14095   93 TKFTERDAS--RMVTDLAQALKYLHSL---------SIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKE----PLF 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 277 TPtqpqgpaaimeAGTQRYMAPELLDKTldlqdwGMALrRADIYSLALLLWEILSRCPdlrPDSSPPPFQlayeaelgnt 356
Cdd:cd14095  158 TV-----------CGTPTYVAPEILAET------GYGL-KVDIWAAGVITYILLCGFP---PFRSPDRDQ---------- 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 357 ptsDELWALaVQERRRPYIPSTWrcfatDP--DGLRELLEDCWDADPEARLTAECVqqrlaaLAHP 420
Cdd:cd14095  207 ---EELFDL-ILAGEFEFLSPYW-----DNisDSAKDLISRMLVVDPEKRYSAGQV------LDHP 257
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
217-420 6.40e-10

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: 60.12  E-value: 6.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCA---IGDLGLALVLPGLTQP--PAWTPtQPQGPaaimeAG 291
Cdd:cd14090  109 IASALDFLH---------DKGIAHRDLKPENILCESMDKVSpvkICDFDLGSGIKLSSTSmtPVTTP-ELLTP-----VG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 292 TQRYMAPELLDKTLdlqdwGMAL---RRADIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAELG-----NTPTSDELW 363
Cdd:cd14090  174 SAEYMAPEVVDAFV-----GEALsydKRCDLWSLGVILYIML---------CGYPPFYGRCGEDCGwdrgeACQDCQELL 239
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 364 ALAVQERRRPYIPSTWRCFATDP-DGLRELLEdcwdADPEARLTAECVqqrlaaLAHP 420
Cdd:cd14090  240 FHSIQEGEYEFPEKEWSHISAEAkDLISHLLV----RDASQRYTAEQV------LQHP 287
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
217-405 6.81e-10

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: 59.58  E-value: 6.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQppawtptqpqgpaAIMEAGTQRYM 296
Cdd:cd05578  109 IVLALDYLHSKN---------IIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTL-------------ATSTSGTKPYM 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLDKtldlQDWGMALrraDIYSLALLLWEILSRcpdLRPdsspppfqlaYEAELgNTPTSdelWALAVQERRRPYIP 376
Cdd:cd05578  167 APEVFMR----AGYSFAV---DWWSLGVTAYEMLRG---KRP----------YEIHS-RTSIE---EIRAKFETASVLYP 222
                        170       180
                 ....*....|....*....|....*....
gi 767973831 377 STWrcfatdPDGLRELLEDCWDADPEARL 405
Cdd:cd05578  223 AGW------SEEAIDLINKLLERDPQKRL 245
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
113-404 8.19e-10

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 59.53  E-value: 8.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 113 QGKLVAIKAFPPRSVAQFQAER-ALYELPGLQHDHIVRFITAsrggpgrllsgpllvlelhpkdcvCLCPrgraPHNSL- 190
Cdd:cd14042   29 KGNLVAIKKVNKKRIDLTREVLkELKHMRDLQHDNLTRFIGA------------------------CVDP----PNICIl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 ---CPIGSLCHYLT--QYTSDW--GSSLRMalSLAQGLAFLHeerwqNGQYKpgiAHRDLSSQNVLIreDGS--CAIGDL 261
Cdd:cd14042   81 teyCPKGSLQDILEneDIKLDWmfRYSLIH--DIVKGMHYLH-----DSEIK---SHGNLKSSNCVV--DSRfvLKITDF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 262 GLAlvlpgltqppawTPTQPQGPAAIMEAGTQR--YMAPELLDKTLDLQdwgMALRRADIYSLALLLWEILSRcpdlrpd 339
Cdd:cd14042  149 GLH------------SFRSGQEPPDDSHAYYAKllWTAPELLRDPNPPP---PGTQKGDVYSFGIILQEIATR------- 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 340 ssPPPFQLaYEAELGntptSDELWALAVQERRRPYI-PSTWRCFAtdPDGLRELLEDCWDADPEAR 404
Cdd:cd14042  207 --QGPFYE-EGPDLS----PKEIIKKKVRNGEKPPFrPSLDELEC--PDEVLSLMQRCWAEDPEER 263
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
102-412 1.04e-09

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 59.21  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 102 GGHAVVWAGQLQGKLVAIKAF------------------------PPRSVAQFQAERALyeLPGLQHDHIVRFITASrgg 157
Cdd:cd14067    5 GSGTVIYRARYQGQPVAVKRFhikkckkrtdgsadtmlkhlraadAMKNFSEFRQEASM--LHSLQHPCIVYLIGIS--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 158 pgrllSGPL-LVLELHPKDCVCLCPRGRAPHNSLCPIGslcHYLTQytsdwgsslRMALSLAQGLAFLHeerwqngqyKP 236
Cdd:cd14067   80 -----IHPLcFALELAPLGSLNTVLEENHKGSSFMPLG---HMLTF---------KIAYQIAAGLAYLH---------KK 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLI-----REDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIMEAGTQRYMAPELLDKTLDLQdwg 311
Cdd:cd14067  134 NIIFCDLKSDNILVwsldvQEHINIKLSDYGIS--------------RQSFHEGALGVEGTPGYQAPEIRPRIVYDE--- 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 312 malrRADIYSLALLLWEILSrcpDLRPDSSPPPFQLAYEAELGNTPTSDElwALAVQERRrpyipstwrcfatdpdgLRE 391
Cdd:cd14067  197 ----KVDMFSYGMVLYELLS---GQRPSLGHHQLQIAKKLSKGIRPVLGQ--PEEVQFFR-----------------LQA 250
                        330       340
                 ....*....|....*....|..
gi 767973831 392 LLEDCWDADPEARLTA-ECVQQ 412
Cdd:cd14067  251 LMMECWDTKPEKRPLAcSVVEQ 272
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
219-426 2.38e-09

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: 58.16  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqpPAWTPTQPQGPAAIMEaGTQRYMAP 298
Cdd:cd06629  119 DGLAYLH---------SKGILHRDLKADNILVDLEGICKISDFGIS---------KKSDDIYGNNGATSMQ-GSVFWMAP 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLDktLDLQDWGMalrRADIYSLALLLWEILSrcpDLRPDSSPPPFQLAYeaELGNtptsdelwalavqERRRPYIPST 378
Cdd:cd06629  180 EVIH--SQGQGYSA---KVDIWSLGCVVLEMLA---GRRPWSDDEAIAAMF--KLGN-------------KRSAPPVPED 236
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767973831 379 wrcFATDPDGLrELLEDCWDADPEARLTAEcvqqRLAalahpqeSHPF 426
Cdd:cd06629  237 ---VNLSPEAL-DFLNACFAIDPRDRPTAA----ELL-------SHPF 269
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
107-414 3.60e-09

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: 57.59  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 107 VWAGQLQG-KLVAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVRFITASRGGPgrllsgPLLVLELHPKdcvclcprg 183
Cdd:cd05067   23 VWMGYYNGhTKVAIKSLKQgsMSPDAFLAEANL--MKQLQHQRLVRLYAVVTQEP------IYIITEYMEN--------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 184 raphnslcpiGSLCHYLTqytSDWGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCA 257
Cdd:cd05067   86 ----------GSLVDFLK---TPSGIKLTinklldMAAQIAEGMAFIEERNY---------IHRDLRAANILVSDTLSCK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 258 IGDLGLALVL--------PGLTQPPAWTptqpqgpaaimeagtqrymAPELLdktldlqDWGMALRRADIYSLALLLWEI 329
Cdd:cd05067  144 IADFGLARLIedneytarEGAKFPIKWT-------------------APEAI-------NYGTFTIKSDVWSFGILLTEI 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 330 LS--RCPdlRPDSSPPPfqlayeaelgntptsdelwalAVQERRRPY-IPSTWRCfatdPDGLRELLEDCWDADPEARLT 406
Cdd:cd05067  198 VThgRIP--YPGMTNPE---------------------VIQNLERGYrMPRPDNC----PEELYQLMRLCWKERPEDRPT 250

                 ....*...
gi 767973831 407 AECVQQRL 414
Cdd:cd05067  251 FEYLRSVL 258
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
189-331 3.61e-09

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: 57.61  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 189 SLCPIGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVL 267
Cdd:cd05581   81 EYAPNGDLLEYIRKYGSlDEKCTRFYTAEIVLALEYLHSK---------GIIHRDLKPENILLDEDMHIKITDFGTAKVL 151
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 268 PGlTQPPAWTPTQPQGPAAIMEA------GTQRYMAPELLDKtldlQDWGMAlrrADIYSLALLLWEILS 331
Cdd:cd05581  152 GP-DSSPESTKGDADSQIAYNQAraasfvGTAEYVSPELLNE----KPAGKS---SDLWALGCIIYQMLT 213
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
212-347 5.09e-09

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: 56.97  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIMEAG 291
Cdd:cd06605  103 KIAVAVVKGLIYLHEKH--------KIIHRDVKPSNILVNSRGQVKLCDFGVS--------------GQLVDSLAKTFVG 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 292 TQRYMAPELLDKTldlqDWGMalrRADIYSLALLLWEI-LSRCPDLRPDSSPP--PFQL 347
Cdd:cd06605  161 TRSYMAPERISGG----KYTV---KSDIWSLGLSLVELaTGRFPYPPPNAKPSmmIFEL 212
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
94-420 6.50e-09

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: 57.11  E-value: 6.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  94 ECEQVIREGGHAVVWAGQ--LQGKLVAIKAFP--------PRSvaqfqaerALYE---LPGLQHDHIVRFITASRGgPGR 160
Cdd:cd07829    2 EKLEKLGEGTYGVVYKAKdkKTGEIVALKKIRldneeegiPST--------ALREislLKELKHPNIVKLLDVIHT-ENK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 161 LLsgplLVLELHPKDcvclcprgraphnslcpigsLCHYLTQYTSdwGSSLRMALSLA----QGLAFLHEERwqngqykp 236
Cdd:cd07829   73 LY----LVFEYCDQD--------------------LKKYLDKRPG--PLPPNLIKSIMyqllRGLAYCHSHR-------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 gIAHRDLSSQNVLIREDGSCAIGDLGLA--LVLPgltqPPAWTPtqpqgpaaimEAGTQRYMAPELLdktLDLQDWGMAL 314
Cdd:cd07829  119 -ILHRDLKPQNLLINRDGVLKLADFGLAraFGIP----LRTYTH----------EVVTLWYRAPEIL---LGSKHYSTAV 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 315 rraDIYSLALLLWEILSRCPDLRPDSspppfqlayEAE--------LGnTPTsDELW----ALAVQERRRPYIPST--WR 380
Cdd:cd07829  181 ---DIWSVGCIFAELITGKPLFPGDS---------EIDqlfkifqiLG-TPT-EESWpgvtKLPDYKPTFPKWPKNdlEK 246
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 767973831 381 CFAT-DPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07829  247 VLPRlDPEGI-DLLSKMLQYNPAKRISAK------EALKHP 280
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
191-331 7.94e-09

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: 56.56  E-value: 7.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVlp 268
Cdd:cd14150   77 CEGSSLYRHLhvTETRFDTMQLIDVARQTAQGMDYLHAK---------NIIHRDLKSNNIFLHEGLTVKIGDFGLATV-- 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 269 gltqPPAWTPTQP-QGPaaimeAGTQRYMAPELldktLDLQDWGMALRRADIYSLALLLWEILS 331
Cdd:cd14150  146 ----KTRWSGSQQvEQP-----SGSILWMAPEV----IRMQDTNPYSFQSDVYAYGVVLYELMS 196
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
97-408 8.47e-09

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: 56.71  E-value: 8.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQ--LQGKLVAIKAF----PPRSVAQFQAERA-LYELPGLQHDHIVRFItasrggpGRLLSGPllvl 169
Cdd:cd06917    7 ELVGRGSYGAVYRGYhvKTGRVVALKVLnldtDDDDVSDIQKEVAlLSQLKLGQPKNIIKYY-------GSYLKGP---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 170 elhpkdcvclcprgraphnSLCPIGSLCHyltqytsdwGSSLRMAL---------------SLAQGLAFLHeerwqngqy 234
Cdd:cd06917   76 -------------------SLWIIMDYCE---------GGSIRTLMragpiaeryiavimrEVLVALKFIH--------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 235 KPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtpTQPQGPAAIMeAGTQRYMAPELL--DKTLDLqdwgm 312
Cdd:cd06917  119 KDGIIHRDIKAANILVTNTGNVKLCDFGVAASL-----------NQNSSKRSTF-VGTPYWMAPEVIteGKYYDT----- 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 313 alrRADIYSLALLLWEILSrcpdlrpdsspppfqlayeaelGNTPTSDELWALAVQ---ERRRPYIPStwRCFATDpdgL 389
Cdd:cd06917  182 ---KADIWSLGITTYEMAT----------------------GNPPYSDVDALRAVMlipKSKPPRLEG--NGYSPL---L 231
                        330
                 ....*....|....*....
gi 767973831 390 RELLEDCWDADPEARLTAE 408
Cdd:cd06917  232 KEFVAACLDEEPKDRLSAD 250
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
218-333 8.58e-09

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: 56.25  E-value: 8.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 218 AQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALV------LPGLTQPpawtptqpqgpaaimeAG 291
Cdd:cd14062   99 AQGMDYLHAK---------NIIHRDLKSNNIFLHEDLTVKIGDFGLATVktrwsgSQQFEQP----------------TG 153
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767973831 292 TQRYMAPELldktLDLQDWGMALRRADIYSLALLLWEILSRC 333
Cdd:cd14062  154 SILWMAPEV----IRMQDENPYSFQSDVYAFGIVLYELLTGQ 191
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
98-420 9.23e-09

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: 56.56  E-value: 9.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRGGpGRLLsgplLVLELh 172
Cdd:cd07833    8 VVGEGAYGVVLKCRNKatGEIVAIKKFKESEDDEDVKKTALREvkvLRQLRHENIVNLKEAFRRK-GRLY----LVFEY- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 173 pkdcvclcprgrAPHNSLcpigslcHYLTQYTSDWGSSL--RMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLI 250
Cdd:cd07833   82 ------------VERTLL-------ELLEASPGGLPPDAvrSYIWQLLQAIAYCH---------SHNIIHRDIKPENILV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 REDGSCAIGDLGLALVLPGLTQPPAWTptqpqgpaaimEAGTQRYMAPELLdktLDLQDWGMAlrrADIYSLALLLWEIL 330
Cdd:cd07833  134 SESGVLKLCDFGFARALTARPASPLTD-----------YVATRWYRAPELL---VGDTNYGKP---VDVWAIGCIMAELL 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 331 SRCPdLRPDSSpppfqlayeaelgntpTSDELWalAVQERRRPYIPSTWRCFATDP--DGLR------------------ 390
Cdd:cd07833  197 DGEP-LFPGDS----------------DIDQLY--LIQKCLGPLPPSHQELFSSNPrfAGVAfpepsqpeslerrypgkv 257
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 767973831 391 -----ELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07833  258 sspalDFLKACLRMDPKERLTCD------ELLQHP 286
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
191-414 9.27e-09

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 56.41  E-value: 9.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLp 268
Cdd:cd14045   84 CPKGSLNDVLlnEDIPLNWGFRFSFATDIARGMAYLHQHK---------IYHGRLKSSNCVIDDRWVCKIADYGLTTYR- 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 269 gltqppawTPTQPQGPAAIMEAGTQRYMAPELLDKTldlqDWGMALrRADIYSLALLLWEILSRcPDLRPDSSPPpfqla 348
Cdd:cd14045  154 --------KEDGSENASGYQQRLMQVYLPPENHSNT----DTEPTQ-ATDVYSYAIILLEIATR-NDPVPEDDYS----- 214
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 349 yeaelgntptSDELWALAVQERRRPYIPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd14045  215 ----------LDEAWCPPLPELISGKTENSCPC----PADYVELIRRCRKNNPAQRPTFEQIKKTL 266
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
97-420 1.01e-08

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: 56.26  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAG--QLQGKLVAIKAFP--------PRSVAQFQAERALyeLPGLQHDHIVRFITASRggpgrlLSGPL 166
Cdd:cd06632    6 QLLGSGSFGSVYEGfnGDTGDFFAVKEVSlvdddkksRESVKQLEQEIAL--LSKLRHPNIVQYYGTER------EEDNL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 167 LV-LELHPkdcvclcprGRAPHNSLCPIGSLCHYLTQ-YTsdwgsslRMALSlaqGLAFLHEERwqngqykpgIAHRDLS 244
Cdd:cd06632   78 YIfLEYVP---------GGSIHKLLQRYGAFEEPVIRlYT-------RQILS---GLAYLHSRN---------TVHRDIK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTptqpqgpaaimeaGTQRYMAPELLDKtldlQDWGMALrRADIYSLAL 324
Cdd:cd06632  130 GANILVDTNGVVKLADFGMAKHVEAFSFAKSFK-------------GSPYWMAPEVIMQ----KNSGYGL-AVDIWSLGC 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 325 LLWEIlsrcpdlrPDSSPPPFQLAYEAELGNTPTSDELwalavqerrrPYIPSTwrcfaTDPDGlRELLEDCWDADPEAR 404
Cdd:cd06632  192 TVLEM--------ATGKPPWSQYEGVAAIFKIGNSGEL----------PPIPDH-----LSPDA-KDFIRLCLQRDPEDR 247
                        330
                 ....*....|....*.
gi 767973831 405 LTAEcvqqrlAALAHP 420
Cdd:cd06632  248 PTAS------QLLEHP 257
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
220-420 1.04e-08

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: 56.76  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPtqpqgpaaimEAGTQRYMAPE 299
Cdd:cd07834  115 GLKYLHSA---------GVIHRDLKPSNILVNSNCDLKICDFGLARGVDPDEDKGFLTE----------YVVTRWYRAPE 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 300 LLdktLDLQDWGMALrraDIYSLALLLWEILSRCPdLRPDSSPPPfQLAYEAELGNTPTSDELWALAVQERR-------- 371
Cdd:cd07834  176 LL---LSSKKYTKAI---DIWSVGCIFAELLTRKP-LFPGRDYID-QLNLIVEVLGTPSEEDLKFISSEKARnylkslpk 247
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767973831 372 RPYIPSTWRCFATDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07834  248 KPKKPLSEVFPGASPEAI-DLLEKMLVFNPKKRITAD------EALAHP 289
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
220-420 1.42e-08

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: 56.13  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgLTQPPAWTPTqpqgpaaimeAGTQRYMAPE 299
Cdd:cd07838  119 GLDFLHSHR---------IVHRDLKPQNILVTSDGQVKLADFGLARI---YSFEMALTSV----------VVTLWYRAPE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 300 LLdktldLQDWGMAlrRADIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTSDElWALAVQERRRPYIPSTW 379
Cdd:cd07838  177 VL-----LQSSYAT--PVDMWSVGCIFAELFNRRPLFRGSSEAD--QLGKIFDVIGLPSEEE-WPRNSALPRSSFPSYTP 246
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767973831 380 RCFAT-----DPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07838  247 RPFKSfvpeiDEEGL-DLLKKMLTFNPHKRISAF------EALQHP 285
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
219-408 1.71e-08

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 55.44  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHeerwQNGQykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppaWTPTQPQGPAAIMEAGTQRYMAP 298
Cdd:cd06610  113 KGLEYLH----SNGQ-----IHRDVKAGNILLGEDGSVKIADFGVSASL--------ATGGDRTRKVRKTFVGTPCWMAP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLDktldlQDWGMALrRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTSDElwalavQERRRPYIPSt 378
Cdd:cd06610  176 EVME-----QVRGYDF-KADIWSFGITAIELATGAA---PYSKYPPMKVLMLTLQNDPPSLET------GADYKKYSKS- 239
                        170       180       190
                 ....*....|....*....|....*....|
gi 767973831 379 wrcfatdpdgLRELLEDCWDADPEARLTAE 408
Cdd:cd06610  240 ----------FRKMISLCLQKDPSKRPTAE 259
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
194-423 1.81e-08

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: 55.89  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqp 273
Cdd:cd06654  102 GSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQ---------VIHRDIKSDNILLGMDGSVKLTDFGFCAQI------ 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 274 pawTPTQPQGPAAImeaGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAEL 353
Cdd:cd06654  167 ---TPEQSKRSTMV---GTPYWMAPEVVTR----KAYG---PKVDIWSLGIMAIEMIEGEP---PYLNENPLRALYLIAT 230
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973831 354 GNTPtsdelwalavqERRRPYIPSTWrcfatdpdgLRELLEDCWDADPEARLTA-ECVQQRLAALAHPQES 423
Cdd:cd06654  231 NGTP-----------ELQNPEKLSAI---------FRDFLNRCLEMDVEKRGSAkELLQHQFLKIAKPLSS 281
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
220-334 1.83e-08

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: 55.66  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTqppaWTPtqpqgpaaimeAGTQRYMAPE 299
Cdd:cd05580  113 ALEYLHSL---------DIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRT----YTL-----------CGTPEYLAPE 168
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767973831 300 LLDKtldlQDWGMAlrrADIYSLALLLWEILSRCP 334
Cdd:cd05580  169 IILS----KGHGKA---VDWWALGILIYEMLAGYP 196
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
94-330 1.97e-08

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: 55.65  E-value: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  94 ECEQVIREGGHAVVWAGQ--LQGKLVAIK--AFPPRSVAQFQAERALYELPGLQHDHIVRFITASrggpgrllsgpllvL 169
Cdd:cd14048    9 EPIQCLGRGGFGVVFEAKnkVDDCNYAVKriRLPNNELAREKVLREVRALAKLDHPGIVRYFNAW--------------L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 170 ELHPK------DCVCLCPRGRaphnsLCPIGSLCHYL----TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIA 239
Cdd:cd14048   75 ERPPEgwqekmDEVYLYIQMQ-----LCRKENLKDWMnrrcTMESRELFVCLNIFKQIASAVEYLHSK---------GLI 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 240 HRDLSSQNVLIREDGSCAIGDLGLALVLPglTQPPAWTPTQPQGPAA--IMEAGTQRYMAPELLDKTldlqdwgMALRRA 317
Cdd:cd14048  141 HRDLKPSNVFFSLDDVVKVGDFGLVTAMD--QGEPEQTVLTPMPAYAkhTGQVGTRLYMSPEQIHGN-------QYSEKV 211
                        250
                 ....*....|...
gi 767973831 318 DIYSLALLLWEIL 330
Cdd:cd14048  212 DIFALGLILFELI 224
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
97-420 2.00e-08

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 55.17  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAG--QLQGKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFI----TasrggPGRLLsgplL 167
Cdd:cd05117    6 KVLGRGSFGVVRLAvhKKTGEEYAVKIIDKKKLKSEDEEMLRREieiLKRLDHPNIVKLYevfeD-----DKNLY----L 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 168 VLELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDwgsSLRMAL----SLAQGLAFLHEErwqngqykpGIAHRDL 243
Cdd:cd05117   77 VMEL-------------------CTGGELFDRIVKKGSF---SEREAAkimkQILSAVAYLHSQ---------GIVHRDL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 244 SSQNVLI---REDGSCAIGDLGLALVLPglTQPPAWTPtqpqgpaaimeAGTQRYMAPELLDKtldlQDWGMAlrrADIY 320
Cdd:cd05117  126 KPENILLaskDPDSPIKIIDFGLAKIFE--EGEKLKTV-----------CGTPYYVAPEVLKG----KGYGKK---CDIW 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 321 SLALLLWEILSRCpdlrpdsspPPFQLAYEAELgntptsdeLWalAVQERRRPYIPSTWRCFAtdpDGLRELLEDCWDAD 400
Cdd:cd05117  186 SLGVILYILLCGY---------PPFYGETEQEL--------FE--KILKGKYSFDSPEWKNVS---EEAKDLIKRLLVVD 243
                        330       340
                 ....*....|....*....|
gi 767973831 401 PEARLTAEcvqqrlAALAHP 420
Cdd:cd05117  244 PKKRLTAA------EALNHP 257
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
213-420 2.39e-08

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 55.40  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGltqppawTPTQPQGPAAIMEAG- 291
Cdd:cd07866  120 YMLQLLEGINYLHENH---------ILHRDIKAANILIDNQGILKIADFGLARPYDG-------PPPNPKGGGGGGTRKy 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 292 -----TQRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTsDELWALA 366
Cdd:cd07866  184 tnlvvTRWYRPPELL---LGERRYTTAV---DIWGIGCVFAEMFTRRPILQGKSDID--QLHLIFKLCGTPT-EETWPGW 254
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973831 367 -------VQERRRPYIPSTWRCFAT-DPDGLReLLEDCWDADPEARLTAecvqqrLAALAHP 420
Cdd:cd07866  255 rslpgceGVHSFTNYPRTLEERFGKlGPEGLD-LLSKLLSLDPYKRLTA------SDALEHP 309
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
99-328 2.71e-08

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: 54.72  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAG--QLQGKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITAsrggpgrLLSGPLL--VLEL 171
Cdd:cd08529    8 LGKGSFGVVYKVvrKVDGRVYALKQIDISRMSRKMREEAIDEarvLSKLNSPYVIKYYDS-------FVDKGKLniVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 172 hpkdcvclcprgraphnslCPIGSLCHYLTQYTsdwGSSL------RMALSLAQGLAFLHEERwqngqykpgIAHRDLSS 245
Cdd:cd08529   81 -------------------AENGDLHSLIKSQR---GRPLpedqiwKFFIQTLLGLSHLHSKK---------ILHRDIKS 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 246 QNVLIREDGSCAIGDLGLALVLpgltqppawtptQPQGPAAIMEAGTQRYMAPELL-DKTLDlqdwgmalRRADIYSLAL 324
Cdd:cd08529  130 MNIFLDKGDNVKIGDLGVAKIL------------SDTTNFAQTIVGTPYYLSPELCeDKPYN--------EKSDVWALGC 189

                 ....
gi 767973831 325 LLWE 328
Cdd:cd08529  190 VLYE 193
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
96-420 3.33e-08

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: 54.82  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAGQLQ--GKLVAIKafpprSVAQ---FQaERALYELPGLQHDHIVR----FITASRGGPGRLLSgpl 166
Cdd:cd14137    9 EKVIGSGSFGVVYQAKLLetGEVVAIK-----KVLQdkrYK-NRELQIMRRLKHPNIVKlkyfFYSSGEKKDEVYLN--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 167 LVLELHPKdcvclcprgraphnslcpigSLCHYLTQYtsdWGSSLRMALS--------LAQGLAFLHeerwqngqyKPGI 238
Cdd:cd14137   80 LVMEYMPE--------------------TLYRVIRHY---SKNKQTIPIIyvklysyqLFRGLAYLH---------SLGI 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 239 AHRDLSSQNVLI-REDGSCAIGDLGLALVLpgltqppawTPTQPQgpaaIMEAGTQRYMAPELLdktLDLQDWGMALrra 317
Cdd:cd14137  128 CHRDIKPQNLLVdPETGVLKLCDFGSAKRL---------VPGEPN----VSYICSRYYRAPELI---FGATDYTTAI--- 188
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 318 DIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAE-LGnTPTSDELWALAV--QERRRPYIPS-TWRCF---ATDPDGLr 390
Cdd:cd14137  189 DIWSAGCVLAELLLGQPLFPGESSVD--QLVEIIKvLG-TPTREQIKAMNPnyTEFKFPQIKPhPWEKVfpkRTPPDAI- 264
                        330       340       350
                 ....*....|....*....|....*....|
gi 767973831 391 ELLEDCWDADPEARLTAecvqqrLAALAHP 420
Cdd:cd14137  265 DLLSKILVYNPSKRLTA------LEALAHP 288
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
213-347 4.84e-08

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: 54.13  E-value: 4.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGlTQPPAWTptqpqgpaaimEAGT 292
Cdd:cd06623  104 IARQILKGLDYLHTKR--------HIIHRDIKPSNLLINSKGEVKIADFGISKVLEN-TLDQCNT-----------FVGT 163
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 293 QRYMAPELLDKtldlQDWGMAlrrADIYSLALLLWE-ILSRCPdLRPDSSPPPFQL 347
Cdd:cd06623  164 VTYMSPERIQG----ESYSYA---ADIWSLGLTLLEcALGKFP-FLPPGQPSFFEL 211
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
97-437 5.09e-08

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: 54.68  E-value: 5.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAG--QLQGKLVAIKAFPPRSVAQFQAERALYELPGLQ---HDHIVRFITASRG-GPGRLLSGPLLVLE 170
Cdd:cd07855   11 ETIGSGAYGVVCSAidTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRhfkHDNIIAIRDILRPkVPYADFKDVYVVLD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 171 LHPKDCvclcprgrapHNSLCPIGSL-----CHYLTQytsdwgsslrmalsLAQGLAFLHEerwqngqykPGIAHRDLSS 245
Cdd:cd07855   91 LMESDL----------HHIIHSDQPLtlehiRYFLYQ--------------LLRGLKYIHS---------ANVIHRDLKP 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 246 QNVLIREDGSCAIGDLGLALVLpgltqppawtPTQPQGPAAIME--AGTQRYMAPELLdktLDLQDWGMALrraDIYSLA 323
Cdd:cd07855  138 SNLLVNENCELKIGDFGMARGL----------CTSPEEHKYFMTeyVATRWYRAPELM---LSLPEYTQAI---DMWSVG 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 324 LLLWEILSRCPdLRPDSSpPPFQLAYEAELGNTPTSDELWALAVqERRRPYI-------PSTWRCFATD--PDGLrELLE 394
Cdd:cd07855  202 CIFAEMLGRRQ-LFPGKN-YVHQLQLILTVLGTPSQAVINAIGA-DRVRRYIqnlpnkqPVPWETLYPKadQQAL-DLLS 277
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 767973831 395 DCWDADPEARLTAEcvqqrlAALAHPQ-ESHPFPESCPRGCPPL 437
Cdd:cd07855  278 QMLRFDPSERITVA------EALQHPFlAKYHDPDDEPDCAPPF 315
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
217-420 5.56e-08

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: 54.05  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpGLtqpPAWTPTQpqgpaaimEAGTQRYM 296
Cdd:cd07860  109 LLQGLAFCHSHR---------VLHRDLKPQNLLINTEGAIKLADFGLARAF-GV---PVRTYTH--------EVVTLWYR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTsDELWALAVQ-ERRRPYI 375
Cdd:cd07860  168 APEIL---LGCKYYSTAV---DIWSLGCIFAEMVTRRALFPGDSEID--QLFRIFRTLGTPD-EVVWPGVTSmPDYKPSF 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767973831 376 PStWRC--FAT-----DPDGlRELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07860  239 PK-WARqdFSKvvpplDEDG-RDLLSQMLHYDPNKRISAK------AALAHP 282
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
214-404 6.45e-08

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 54.24  E-value: 6.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlPGLTQPPAWTptqPQGPAAImeagTQ 293
Cdd:cd14207  186 SFQVARGMEFLSSRK---------CIHRDLAARNILLSENNVVKICDFGLA---RDIYKNPDYV---RKGDARL----PL 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 294 RYMAPE-LLDKTLDlqdwgmalRRADIYSLALLLWEILSRcpdlrpDSSP-PPFQLayeaelgntptsDELWALAVQERR 371
Cdd:cd14207  247 KWMAPEsIFDKIYS--------TKSDVWSYGVLLWEIFSL------GASPyPGVQI------------DEDFCSKLKEGI 300
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767973831 372 RPYIPStwrcFATDPdgLRELLEDCWDADPEAR 404
Cdd:cd14207  301 RMRAPE----FATSE--IYQIMLDCWQGDPNER 327
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
190-416 7.27e-08

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 53.47  E-value: 7.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA--- 264
Cdd:cd05085   74 LVPGGDFLSFLRKKKDELKTKqlVKFSLDAAAGMAYLESKN---------CIHRDLAARNCLVGENNALKISDFGMSrqe 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 ----LVLPGLTQ-PPAWTptqpqgpaaimeagtqrymAPELLdktldlqDWGMALRRADIYSLALLLWEILSrcpdlrpd 339
Cdd:cd05085  145 ddgvYSSSGLKQiPIKWT-------------------APEAL-------NYGRYSSESDVWSFGILLWETFS-------- 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 340 sspppfqlayeaeLGNTPTSDELWALAVQERRRPY-IPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd05085  191 -------------LGVCPYPGMTNQQAREQVEKGYrMSAPQRC----PEDIYKIMQRCWDYNPENRPKFSELQKELAA 251
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
190-415 7.52e-08

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 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: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 53.45  E-value: 7.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSL------CHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGL 263
Cdd:cd05087   78 FCPLGDLkgylrsCRAAESMAPDPLTLQRMACEVACGLLHLHRNNF---------VHSDLALRNCLLTADLTVKIGDYGL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 264 ALVLPG----LTQPPAWTPTqpqgpaaimeagtqRYMAPELLDK---TLDLQDwgmALRRADIYSLALLLWEILsrcpdl 336
Cdd:cd05087  149 SHCKYKedyfVTADQLWVPL--------------RWIAPELVDEvhgNLLVVD---QTKQSNVWSLGVTIWELF------ 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 337 rpdsspppfqlayeaELGNTP----TSDELWALAVQERR----RPYIPSTWrcfatdPDGLRELLEDCWdADPEARLTAE 408
Cdd:cd05087  206 ---------------ELGNQPyrhySDRQVLTYTVREQQlklpKPQLKLSL------AERWYEVMQFCW-LQPEQRPTAE 263

                 ....*..
gi 767973831 409 CVQQRLA 415
Cdd:cd05087  264 EVHLLLS 270
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
117-414 8.54e-08

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: 53.49  E-value: 8.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 117 VAIKAFPP--RSVAQFQAERALyeLPGLQHDHIVRFITASRGGPgrllsgPLLVLELHPKdcvclcprgraphnslcpiG 194
Cdd:cd05073   38 VAVKTMKPgsMSVEAFLAEANV--MKTLQHDKLVKLHAVVTKEP------IYIITEFMAK-------------------G 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 195 SLCHYLTqytSDWGSSLRM------ALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVL- 267
Cdd:cd05073   91 SLLDFLK---SDEGSKQPLpklidfSAQIAEGMAFIEQRNY---------IHRDLRAANILVSASLVCKIADFGLARVIe 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 268 -------PGLTQPPAWTptqpqgpaaimeagtqrymAPELLdktldlqDWGMALRRADIYSLALLLWEILSrcpdlrpds 340
Cdd:cd05073  159 dneytarEGAKFPIKWT-------------------APEAI-------NFGSFTIKSDVWSFGILLMEIVT--------- 203
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 341 spppfqlayeaeLGNTPTSDELWALAVQERRRPY-IPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd05073  204 ------------YGRIPYPGMSNPEVIRALERGYrMPRPENC----PEELYNIMMRCWKNRPEERPTFEYIQSVL 262
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
217-420 9.30e-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: 53.45  E-value: 9.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpGLtqpPAWTPTQpqgpaaimEAGTQRYM 296
Cdd:cd07835  108 LLQGIAFCHSHR---------VLHRDLKPQNLLIDTEGALKLADFGLARAF-GV---PVRTYTH--------EVVTLWYR 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPP----FQLayeaeLGnTPTsDELWALAVQ-ERR 371
Cdd:cd07835  167 APEIL---LGSKHYSTPV---DIWSVGCIFAEMVTRRPLFPGDSEIDQlfriFRT-----LG-TPD-EDVWPGVTSlPDY 233
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 372 RPYIPStWR-------CFATDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07835  234 KPTFPK-WArqdlskvVPSLDEDGL-DLLSQMLVYDPAKRISAK------AALQHP 281
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
108-406 9.63e-08

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: 53.12  E-value: 9.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 108 WAGQLQGKLVAIKAFPPRSVAQFQAERALYElpGLQHDHIVRFITAsrggpgrllsgpllvlelhpkdcvCLCPRGRAPH 187
Cdd:cd14063   21 WHGDVAIKLLNIDYLNEEQLEAFKEEVAAYK--NTRHDNLVLFMGA------------------------CMDPPHLAIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 188 NSLCPIGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIrEDGSCAIGDLGLaL 265
Cdd:cd14063   75 TSLCKGRTLYSLIHERKEKFDFNktVQIAQQICQGMGYLH---------AKGIIHKDLKSKNIFL-ENGRVVITDFGL-F 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 266 VLPGLTQPPAWTPTQ--PQGPAAimeagtqrYMAPEL---LDKTLDLQDWGMALRRADIYSLALLLWEILSRcpDLrPDS 340
Cdd:cd14063  144 SLSGLLQPGRREDTLviPNGWLC--------YLAPEIiraLSPDLDFEESLPFTKASDVYAFGTVWYELLAG--RW-PFK 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 341 SPPPFQLAYEAELGNTPTSDELwalavqerrrpyipstwrcfaTDPDGLRELLEDCWDADPEARLT 406
Cdd:cd14063  213 EQPAESIIWQVGCGKKQSLSQL---------------------DIGREVKDILMQCWAYDPEKRPT 257
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
117-406 9.68e-08

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: 53.19  E-value: 9.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 117 VAIKAFPPRSVAQFQAE--RALYELPGLQHDHIVRFItasrggpgrllsgpllvlelhpkdCVCLCPRgRAPHNSLCPIG 194
Cdd:cd05057   39 VAIKVLREETGPKANEEilDEAYVMASVDHPHLVRLL------------------------GICLSSQ-VQLITQLMPLG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 195 SLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPgltq 272
Cdd:cd05057   94 CLLDYVRNHRDNIGSQllLNWCVQIAKGMSYLEEKR---------LVHRDLAARNVLVKTPNHVKITDFGLAKLLD---- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 273 ppawtptqPQGPAAIMEAGTQ--RYMAPELLdktldlqDWGMALRRADIYSLALLLWEILSrcpdlrpdsspppF-QLAY 349
Cdd:cd05057  161 --------VDEKEYHAEGGKVpiKWMALESI-------QYRIYTHKSDVWSYGVTVWELMT-------------FgAKPY 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 350 EaelgNTPTSDELWALAVQER-RRPYIpstwrCFATdpdgLRELLEDCWDADPEARLT 406
Cdd:cd05057  213 E----GIPAVEIPDLLEKGERlPQPPI-----CTID----VYMVLVKCWMIDAESRPT 257
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
217-420 9.84e-08

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: 53.25  E-value: 9.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpGLtqpPAWTPTQpqgpaaimEAGTQRYM 296
Cdd:cd07836  109 LLKGIAFCHENR---------VLHRDLKPQNLLINKRGELKLADFGLARAF-GI---PVNTFSN--------EVVTLWYR 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTsDELWALAVQ--ERRRPY 374
Cdd:cd07836  168 APDVL---LGSRTYSTSI---DIWSVGCIMAEMITGRPLFPGTNNED--QLLKIFRIMGTPT-ESTWPGISQlpEYKPTF 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767973831 375 IPSTWRCFA-----TDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07836  239 PRYPPQDLQqlfphADPLGI-DLLHRLLQLNPELRISAH------DALQHP 282
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
125-314 1.17e-07

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 53.08  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 125 RSVAQFQAERALYE---LPGLQHDHIVRFITASRGgpgrllsgpllvlELHPKDCVCLCprgraphNSLCPIGSLCHYLT 201
Cdd:cd14033   37 RKLSKGERQRFSEEvemLKGLQHPNIVRFYDSWKS-------------TVRGHKCIILV-------TELMTSGTLKTYLK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 202 QYTSDWGSSL-RMALSLAQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLAlvlpgltqppawtpT 279
Cdd:cd14033   97 RFREMKLKLLqRWSRQILKGLHFLHSR-------CPPILHRDLKCDNIFITgPTGSVKIGDLGLA--------------T 155
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767973831 280 QPQGPAAIMEAGTQRYMAPEL----LDKTLDLQDWGMAL 314
Cdd:cd14033  156 LKRASFAKSVIGTPEFMAPEMyeekYDEAVDVYAFGMCI 194
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
101-264 1.19e-07

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


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 53.15  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 101 EGGHAVVWAGQ--LQGKLVAIKA--FPPRSVAQFQAERALYELPGLQHDHIVRF--ITASRggpgRLLSgplLVLELHPK 174
Cdd:cd07844   10 EGSYATVYKGRskLTGQLVALKEirLEHEEGAPFTAIREASLLKDLKHANIVTLhdIIHTK----KTLT---LVFEYLDT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 175 DcvclcprgraphnslcpigslchyLTQYTSDWGSSLRMA------LSLAQGLAFLHEERwqngqykpgIAHRDLSSQNV 248
Cdd:cd07844   83 D------------------------LKQYMDDCGGGLSMHnvrlflFQLLRGLAYCHQRR---------VLHRDLKPQNL 129
                        170
                 ....*....|....*.
gi 767973831 249 LIREDGSCAIGDLGLA 264
Cdd:cd07844  130 LISERGELKLADFGLA 145
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
116-416 1.23e-07

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: 53.05  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 116 LVAIKAFPPRSVA---QFQAERALyeLPGLQHDHIVRFITASRggPGRLLsgpLLVLELHPKDCVCLCPRGRAPHNSLC- 191
Cdd:cd05092   37 LVAVKALKEATESarqDFQREAEL--LTVLQHQHIVRFYGVCT--EGEPL---IMVFEYMRHGDLNRFLRSHGPDAKILd 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 192 -----PIGSLChyLTQYtsdwgssLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA-- 264
Cdd:cd05092  110 ggegqAPGQLT--LGQM-------LQIASQIASGMVYLASLHF---------VHRDLATRNCLVGQGLVVKIGDFGMSrd 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 ------LVLPGLTQPPA-WTPtqpqgPAAIMeagtQRYMAPElldktldlqdwgmalrrADIYSLALLLWEILSRcpdlr 337
Cdd:cd05092  172 iystdyYRVGGRTMLPIrWMP-----PESIL----YRKFTTE-----------------SDIWSFGVVLWEIFTY----- 220
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 338 pdSSPPPFQLAYEAELGNTPTSDELwalavqERRRpyipstwrcfaTDPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd05092  221 --GKQPWYQLSNTEAIECITQGREL------ERPR-----------TCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
101-268 1.39e-07

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: 52.73  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 101 EGGHAVVWAG---QLQGKL--VAIKAFPPRSVAQFQA-ERALYE---LPGLQHDHIVRFItasrggpGRLLSGPL-LVLE 170
Cdd:cd05040    5 DGSFGVVRRGewtTPSGKViqVAVKCLKSDVLSQPNAmDDFLKEvnaMHSLDHPNLIRLY-------GVVLSSPLmMVTE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 171 LHPKDCVCLCPRGRAPHnslCPIGSLCHYLTQytsdwgsslrmalsLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI 250
Cdd:cd05040   78 LAPLGSLLDRLRKDQGH---FLISTLCDYAVQ--------------IANGMAYLESKR---------FIHRDLAARNILL 131
                        170
                 ....*....|....*...
gi 767973831 251 REDGSCAIGDLGLALVLP 268
Cdd:cd05040  132 ASKDKVKIGDFGLMRALP 149
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
212-329 1.77e-07

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: 52.43  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA--LVlpgltqppawtptqpQGPAAIME 289
Cdd:cd06617  107 KIAVSIVKALEYLHS--------KLSVIHRDVKPSNVLINRNGQVKLCDFGISgyLV---------------DSVAKTID 163
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767973831 290 AGTQRYMAPELLDKTLDLQDWGMalrRADIYSLALLLWEI 329
Cdd:cd06617  164 AGCKPYMAPERINPELNQKGYDV---KSDVWSLGITMIEL 200
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
191-332 2.02e-07

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 52.56  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI---REDGSCAIGDLGLALVL 267
Cdd:cd13977  117 CDGGDMNEYLLSRRPDRQTNTSFMLQLSSALAFLHRNQ---------IVHRDLKPDNILIshkRGEPILKVADFGLSKVC 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973831 268 PGLTqppawtpTQPQGPAAIME------AGTQRYMAPELLDktldlqdwGMALRRADIYSLALLLWEILSR 332
Cdd:cd13977  188 SGSG-------LNPEEPANVNKhflssaCGSDFYMAPEVWE--------GHYTAKADIFALGIIIWAMVER 243
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
129-314 2.25e-07

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 52.42  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 129 QFQAERALyeLPGLQHDHIVRFITASRGgpgrLLSGpllvlelhpKDCVCLCprgraphNSLCPIGSLCHYLTQYTSDWG 208
Cdd:cd14031   55 RFKEEAEM--LKGLQHPNIVRFYDSWES----VLKG---------KKCIVLV-------TELMTSGTLKTYLKRFKVMKP 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 209 SSLR-MALSLAQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLALVLpgltqppawtptqpQGPAA 286
Cdd:cd14031  113 KVLRsWCRQILKGLQFLHTR-------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLATLM--------------RTSFA 171
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767973831 287 IMEAGTQRYMAPEL----LDKTLDLQDWGMAL 314
Cdd:cd14031  172 KSVIGTPEFMAPEMyeehYDESVDVYAFGMCM 203
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
191-331 2.30e-07

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: 52.37  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYL--TQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVlp 268
Cdd:cd14151   85 CEGSSLYHHLhiIETKFEMIKLIDIARQTAQGMDYLHAK---------SIIHRDLKSNNIFLHEDLTVKIGDFGLATV-- 153
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973831 269 gltqPPAWTPTQPQGPAaimeAGTQRYMAPELldktLDLQDWGMALRRADIYSLALLLWEILS 331
Cdd:cd14151  154 ----KSRWSGSHQFEQL----SGSILWMAPEV----IRMQDKNPYSFQSDVYAFGIVLYELMT 204
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
212-408 2.31e-07

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: 52.37  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA--LVLPGLTQPPAWTPtqpqgpaaimE 289
Cdd:cd07865  123 KVMKMLLNGLYYIHRNK---------ILHRDMKAANILITKDGVLKLADFGLAraFSLAKNSQPNRYTN----------R 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 290 AGTQRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTSD--------E 361
Cdd:cd07865  184 VVTLWYRPPELL---LGERDYGPPI---DMWGAGCIMAEMWTRSPIMQGNTEQH--QLTLISQLCGSITPEvwpgvdklE 255
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 362 LWALA---------VQERRRPYIpstwrcfaTDPDGLrELLEDCWDADPEARLTAE 408
Cdd:cd07865  256 LFKKMelpqgqkrkVKERLKPYV--------KDPYAL-DLIDKLLVLDPAKRIDAD 302
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
99-393 2.39e-07

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: 51.99  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQGK---LVAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRggpgrLLSGPLLVLELhp 173
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKpdlPVAIKCITKKNLSKSQNllGKEIKILKELSHENVVALLDCQE-----TSSSVYLVMEY-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 174 kdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSSLRMAL-SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIRE 252
Cdd:cd14120   74 -----------------CNGGDLADYLQAKGTLSEDTIRVFLqQIAAAMKALHSK---------GIVHRDLKPQNILLSH 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 253 DGSCA---------IGDLGLALVLPGltqppawtptqpqGPAAIMEAGTQRYMAPELLdktldlqdwgMALR---RADIY 320
Cdd:cd14120  128 NSGRKpspndirlkIADFGFARFLQD-------------GMMAATLCGSPMYMAPEVI----------MSLQydaKADLW 184
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 321 SLALLLWEILsrcpdlrpdSSPPPFQlayeaelGNTPtsDELWALAVQERR-RPYIPSTwrcfaTDPDgLRELL 393
Cdd:cd14120  185 SIGTIVYQCL---------TGKAPFQ-------AQTP--QELKAFYEKNANlRPNIPSG-----TSPA-LKDLL 234
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
114-348 2.39e-07

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: 51.85  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFPPRSVAQ-FQAERALYELP---GLQHDHIVRFITASRGGpgrllSGPLLVLELhpkdcvclCPRgraphNS 189
Cdd:cd14189   26 NKTYAVKVIPHSRVAKpHQREKIVNEIElhrDLHHKHVVKFSHHFEDA-----ENIYIFLEL--------CSR-----KS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSLCHYLTQYTSDWgsSLRMALSlaqGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpg 269
Cdd:cd14189   88 LAHIWKARHTLLEPEVRY--YLKQIIS---GLKYLHLK---------GILHRDLKLGNFFINENMELKVGDFGLAARL-- 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 270 ltQPPAwtptqpQGPAAImeAGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILsrCPDlrpdsspPPFQLA 348
Cdd:cd14189  152 --EPPE------QRKKTI--CGTPNYLAPEVLLR----QGHG---PESDVWSLGCVMYTLL--CGN-------PPFETL 204
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
212-330 2.82e-07

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: 51.48  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA-------LVLPGLTqppawtptqpqgp 284
Cdd:cd14002  103 SIAKQLVSALHYLHSNR---------IIHRDMKPQNILIGKGGVVKLCDFGFAramscntLVLTSIK------------- 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767973831 285 aaimeaGTQRYMAPELL-DKTLDlqdwgmalRRADIYSLALLLWEIL 330
Cdd:cd14002  161 ------GTPLYMAPELVqEQPYD--------HTADLWSLGCILYELF 193
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
110-416 3.14e-07

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 51.94  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 110 GQLQGKLVAIKAFP----PRSVAQFQAERALyeLPGLQHDHIVRFITA-SRGGPGRLLSGPLLVLELHPKDCVclcprgR 184
Cdd:cd05090   30 GMDHAQLVAIKTLKdynnPQQWNEFQQEASL--MTELHHPNIVCLLGVvTQEQPVCMLFEFMNQGDLHEFLIM------R 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 185 APHNSL-CpiGSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGL 263
Cdd:cd05090  102 SPHSDVgC--SSDEDGTVKSSLDHGDFLHIAIQIAAGMEYLSSHFF---------VHKDLAARNILVGEQLHVKISDLGL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 264 ALVLpgltQPPAWTPTQPQGPAAImeagtqRYMAPELLdktldlqDWGMALRRADIYSLALLLWEILSRcpDLRPdsspp 343
Cdd:cd05090  171 SREI----YSSDYYRVQNKSLLPI------RWMPPEAI-------MYGKFSSDSDIWSFGVVLWEIFSF--GLQP----- 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 344 pfqlayeaelgntptsdeLWALAVQE-----RRRPYIPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd05090  227 ------------------YYGFSNQEviemvRKRQLLPCSEDC----PPRMYSLMTECWQEIPSRRPRFKDIHARLRS 282
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
94-412 3.22e-07

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: 51.50  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  94 ECEQVIREGGHAVVWAGQ--LQGKLVAIKafpprSVAQF------QAERALYE---LPGLQHDHIVRFITAsrggpgrLL 162
Cdd:cd08224    3 EIEKKIGKGQFSVVYRARclLDGRLVALK-----KVQIFemmdakARQDCLKEidlLQQLNHPNIIKYLAS-------FI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 163 SGPLL--VLELhpkdcvclCPRG--------RAPHNSLCPIGSLCHYLTQytsdwgsslrmalsLAQGLAFLHEERwqng 232
Cdd:cd08224   71 ENNELniVLEL--------ADAGdlsrlikhFKKQKRLIPERTIWKYFVQ--------------LCSALEHMHSKR---- 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 233 qykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQppawtptqpqgpAAIMEAGTQRYMAPELLDKTldLQDWgm 312
Cdd:cd08224  125 -----IMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTT------------AAHSLVGTPYYMSPERIREQ--GYDF-- 183
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 313 alrRADIYSLALLLWEILSrcpdLRpdsspPPFqlayEAELGNtptsdeLWALAVQERRRPYIPSTWRCFatdPDGLREL 392
Cdd:cd08224  184 ---KSDIWSLGCLLYEMAA----LQ-----SPF----YGEKMN------LYSLCKKIEKCEYPPLPADLY---SQELRDL 238
                        330       340
                 ....*....|....*....|
gi 767973831 393 LEDCWDADPEARLTAECVQQ 412
Cdd:cd08224  239 VAACIQPDPEKRPDISYVLD 258
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
237-301 3.51e-07

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 51.83  E-value: 3.51e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 237 GIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGltqppawtptqpqGPAAIMEAGTQRYMAPELL 301
Cdd:cd05607  124 KIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKE-------------GKPITQRAGTNGYMAPEIL 175
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
211-414 3.64e-07

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 51.47  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA--------LVLPGLTQPPA-WTptqp 281
Cdd:cd05084   98 IRMVENAAAGMEYLESKH---------CIHRDLAARNCLVTEKNVLKISDFGMSreeedgvyAATGGMKQIPVkWT---- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 282 qgpaaimeagtqrymAPELLdktldlqDWGMALRRADIYSLALLLWEILSrcpdlrpdsspppfqlayeaeLGNTPtsde 361
Cdd:cd05084  165 ---------------APEAL-------NYGRYSSESDVWSFGILLWETFS---------------------LGAVP---- 197
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 362 lWALAVQERRRPYIPSTWRCFATD--PDGLRELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd05084  198 -YANLSNQQTREAVEQGVRLPCPEncPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
143-406 3.89e-07

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 51.65  E-value: 3.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 143 QHDHIVRFITASRGGpgrllsGPL-LVLELHPKDCVCLCPRGRAPHNSLC-PIGSLCH--YLTQYtsDWGSslrMALSLA 218
Cdd:cd05053   75 KHKNIINLLGACTQD------GPLyVVVEYASKGNLREFLRARRPPGEEAsPDDPRVPeeQLTQK--DLVS---FAYQVA 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQ---------PPAWtptqpqgpaaime 289
Cdd:cd05053  144 RGMEYLASKK---------CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYyrkttngrlPVKW------------- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 290 agtqryMAPE-LLDKTLDLQdwgmalrrADIYSLALLLWEILSrcpdlrPDSSPPPfqlayeaelgNTPTsDELWALAVQ 368
Cdd:cd05053  202 ------MAPEaLFDRVYTHQ--------SDVWSFGVLLWEIFT------LGGSPYP----------GIPV-EELFKLLKE 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767973831 369 ERR--RPyipstwrcfATDPDGLRELLEDCWDADPEARLT 406
Cdd:cd05053  251 GHRmeKP---------QNCTQELYMLMRDCWHEVPSQRPT 281
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
116-416 4.17e-07

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: 51.31  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 116 LVAIKAFPPRSVAQ----FQAERALyeLPGLQHDHIVRFI-TASRGGPgrllsgPLLVLELHPKDCVCLCPRGRAPH-NS 189
Cdd:cd05049   37 LVAVKTLKDASSPDarkdFEREAEL--LTNLQHENIVKFYgVCTEGDP------LLMVFEYMEHGDLNKFLRSHGPDaAF 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSLCHYLTQytsdwGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA----- 264
Cdd:cd05049  109 LASEDSAPGELTL-----SQLLHIAVQIASGMVYLASQHF---------VHRDLATRNCLVGTNLVVKIGDFGMSrdiys 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 ---LVLPGLTQPPA-WTPtqpqgPAAIMeagtqrymapelldktldlqdWGMALRRADIYSLALLLWEILSRcpdlrpdS 340
Cdd:cd05049  175 tdyYRVGGHTMLPIrWMP-----PESIL---------------------YRKFTTESDVWSFGVVLWEIFTY-------G 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 341 SPPPFQLAyeaelgNTPTSDELWALAVQERRRpyipstwrcfaTDPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd05049  222 KQPWFQLS------NTEVIECITQGRLLQRPR-----------TCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
97-331 4.37e-07

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: 51.56  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  97 QVIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAER-ALYELPGLQHDHiVRFITAsrggpgrllsgplLVLELHP 173
Cdd:cd05630    6 RVLGKGGFGEVCACQVRatGKMYACKKLEKKRIKKRKGEAmALNEKQILEKVN-SRFVVS-------------LAYAYET 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 174 KDCVCLCPrgraphnSLCPIGSL---CHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI 250
Cdd:cd05630   72 KDALCLVL-------TLMNGGDLkfhIYHMGQAGFPEARAVFYAAEICCGLEDLHRER---------IVYRDLKPENILL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 REDGSCAIGDLGLALVLpgltqppawtptqPQGPAAIMEAGTQRYMAPELL--DKTLDLQDWgmalrradiYSLALLLWE 328
Cdd:cd05630  136 DDHGHIRISDLGLAVHV-------------PEGQTIKGRVGTVGYMAPEVVknERYTFSPDW---------WALGCLLYE 193

                 ...
gi 767973831 329 ILS 331
Cdd:cd05630  194 MIA 196
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
234-412 4.80e-07

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: 50.87  E-value: 4.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 234 YKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlVLPGLTQPPAWTPTQpqgpaaimeAGTQRYMAPELLDKTldlqdwGMA 313
Cdd:cd14663  117 HSRGVFHRDLKPENLLLDEDGNLKISDFGLS-ALSEQFRQDGLLHTT---------CGTPNYVAPEVLARR------GYD 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 314 LRRADIYSLALLLWEILSRCpdlrpdsspPPFQlayeaelgntptSDELWALAVQ-ERRRPYIPStWrcFATdpdGLREL 392
Cdd:cd14663  181 GAKADIWSCGVILFVLLAGY---------LPFD------------DENLMALYRKiMKGEFEYPR-W--FSP---GAKSL 233
                        170       180
                 ....*....|....*....|
gi 767973831 393 LEDCWDADPEARLTAECVQQ 412
Cdd:cd14663  234 IKRILDPNPSTRITVEQIMA 253
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
211-428 5.06e-07

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: 51.12  E-value: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLglalvlpGLTQPPAWTPTQPQGPAAIMEA 290
Cdd:cd05061  122 IQMAAEIADGMAYLNAKKF---------VHRDLAARNCMVAHDFTVKIGDF-------GMTRDIYETDYYRKGGKGLLPV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 291 gtqRYMAPElldktlDLQDwGMALRRADIYSLALLLWEILSRcpdlrpdsSPPPFQ-LAYEAELGNTPTSDelwalavqe 369
Cdd:cd05061  186 ---RWMAPE------SLKD-GVFTTSSDMWSFGVVLWEITSL--------AEQPYQgLSNEQVLKFVMDGG--------- 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 370 rrrpYIPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAALAHPQeshpFPE 428
Cdd:cd05061  239 ----YLDQPDNC----PERVTDLMRMCWQFNPKMRPTFLEIVNLLKDDLHPS----FPE 285
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
217-420 5.22e-07

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: 51.52  E-value: 5.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErWqngqykpgIAHRDLSSQNVLI----REDGSCAIGDLGLALvlpgLTQPPAWTPTQPQGPAAimeagT 292
Cdd:cd07842  117 ILNGIHYLHSN-W--------VLHRDLKPANILVmgegPERGVVKIGDLGLAR----LFNAPLKPLADLDPVVV-----T 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 293 QRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSrcpdLRP-------DSSPP-PF---QLAYEAELGNTPTsDE 361
Cdd:cd07842  179 IWYRAPELL---LGARHYTKAI---DIWAIGCIFAELLT----LEPifkgreaKIKKSnPFqrdQLERIFEVLGTPT-EK 247
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 362 LW----------ALAVQERRRPY---IPSTWR--CFATDPDGLReLLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07842  248 DWpdikkmpeydTLKSDTKASTYpnsLLAKWMhkHKKPDSQGFD-LLRKLLEYDPTKRITAE------EALEHP 314
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
214-417 5.42e-07

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 51.52  E-value: 5.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlPGLTQPPAWTptqPQGPAAImeagTQ 293
Cdd:cd05103  185 SFQVAKGMEFLASRK---------CIHRDLAARNILLSENNVVKICDFGLA---RDIYKDPDYV---RKGDARL----PL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 294 RYMAPE-LLDKTLDLQdwgmalrrADIYSLALLLWEILSrcpdlrpdsspppfqlayeaeLGNTPTS----DELWALAVQ 368
Cdd:cd05103  246 KWMAPEtIFDRVYTIQ--------SDVWSFGVLLWEIFS---------------------LGASPYPgvkiDEEFCRRLK 296
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767973831 369 ERRRPYIPSTwrcfaTDPDGLRELLeDCWDADPEARLTAECVQQRLAAL 417
Cdd:cd05103  297 EGTRMRAPDY-----TTPEMYQTML-DCWHGEPSQRPTFSELVEHLGNL 339
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
201-420 5.62e-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: 50.80  E-value: 5.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 201 TQYTSDWGSSlrMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIRE--DG--SCAIGDLGLALVLPGltqpPAW 276
Cdd:cd14184   94 TKYTERDASA--MVYNLASALKYLH---------GLCIVHRDIKPENLLVCEypDGtkSLKLGDFGLATVVEG----PLY 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 277 TPtqpqgpaaimeAGTQRYMAPELLDKTldlqdwGMALrRADIYSLALLLWEILSRCPDLRPDSSpppfqlaYEAELGNT 356
Cdd:cd14184  159 TV-----------CGTPTYVAPEIIAET------GYGL-KVDIWAAGVITYILLCGFPPFRSENN-------LQEDLFDQ 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 357 PTSDELwalavqERRRPYipstWRCFAtdpDGLRELLEDCWDADPEARLTAECVqqrlaaLAHP 420
Cdd:cd14184  214 ILLGKL------EFPSPY----WDNIT---DSAKELISHMLQVNVEARYTAEQI------LSHP 258
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
191-414 6.47e-07

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk 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: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 50.66  E-value: 6.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYL------TQYTSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA 264
Cdd:cd05042   77 CDLGDLKAYLrserehERGDSDTRTLQRMACEVAAGLAHLHKLNF---------VHSDLALRNCLLTSDLTVKIGDYGLA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 LVLPG----LTQPPAWTPTqpqgpaaimeagtqRYMAPELLDktlDLQDWGMAL---RRADIYSLALLLWEILsrcpdlr 337
Cdd:cd05042  148 HSRYKedyiETDDKLWFPL--------------RWTAPELVT---EFHDRLLVVdqtKYSNIWSLGVTLWELF------- 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 338 pdsspppfqlayeaELGNTP----TSDELWALAVQERR----RPYIPSTWrcfatdPDGLRELLEDCWdADPEARLTAEC 409
Cdd:cd05042  204 --------------ENGAQPysnlSDLDVLAQVVREQDtklpKPQLELPY------SDRWYEVLQFCW-LSPEQRPAAED 262

                 ....*
gi 767973831 410 VQQRL 414
Cdd:cd05042  263 VHLLL 267
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
213-412 6.60e-07

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: 50.72  E-value: 6.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIR--EDGSCA--IGDLGLALVLPGltqpPAWTPtqpqgpaaim 288
Cdd:cd14185  103 MIIDLCEALVYIHSKH---------IVHRDLKPENLLVQhnPDKSTTlkLADFGLAKYVTG----PIFTV---------- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 289 eAGTQRYMAPELLDKTldlqdwGMALrRADIYSLALLLWEILSRCPDLRpdsSPPPFQlayeaelgntptsDELWALaVQ 368
Cdd:cd14185  160 -CGTPTYVAPEILSEK------GYGL-EVDMWAAGVILYILLCGFPPFR---SPERDQ-------------EELFQI-IQ 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767973831 369 ERRRPYIPSTWRCFAtdpDGLRELLEDCWDADPEARLTAECVQQ 412
Cdd:cd14185  215 LGHYEFLPPYWDNIS---EAAKDLISRLLVVDPEKRYTAKQVLQ 255
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
215-408 6.91e-07

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 50.78  E-value: 6.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAQGLAFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPA----WTPTQPQGPAAIMEa 290
Cdd:cd14011  121 LQISEALSFLHNDV--------KLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPyfreYDPNLPPLAQPNLN- 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 291 gtqrYMAPEL-LDKTLDLqdwgmalrRADIYSLALLLWEILSRCpdlrpdssPPPFQlayeaeLGNTPTSDElwALAVQE 369
Cdd:cd14011  192 ----YLAPEYiLSKTCDP--------ASDMFSLGVLIYAIYNKG--------KPLFD------CVNNLLSYK--KNSNQL 243
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767973831 370 RRRpyipsTWRCFATDPDGLRELLEDCWDADPEARLTAE 408
Cdd:cd14011  244 RQL-----SLSLLEKVPEELRDHVKTLLNVTPEVRPDAE 277
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
101-303 7.02e-07

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: 50.63  E-value: 7.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 101 EGGHAVVWAGQLQ--GKLVAIKAFP------PRSVAQFQAERALYElpGLQHDHIVRFITAsrggpgrllsgpllvleLH 172
Cdd:cd14099   11 KGGFAKCYEVTDMstGKVYAGKVVPkssltkPKQREKLKSEIKIHR--SLKHPNIVKFHDC-----------------FE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 173 PKDCVC----LCPRGraphnslcpigSLCHYLTQytsdwgsslRMALS----------LAQGLAFLHEERwqngqykpgI 238
Cdd:cd14099   72 DEENVYilleLCSNG-----------SLMELLKR---------RKALTepevryfmrqILSGVKYLHSNR---------I 122
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 239 AHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptQPQGPAAIMEAGTQRYMAPELLDK 303
Cdd:cd14099  123 IHRDLKLGNLFLDENMNVKIGDFGLAARL------------EYDGERKKTLCGTPNYIAPEVLEK 175
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
217-429 7.99e-07

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 50.82  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEerwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppAWTPTQPQGPAAimeagTQRYM 296
Cdd:cd07878  127 LLRGLKYIHS---------AGIIHRDLKPSNVAVNEDCELRILDFGLA----------RQADDEMTGYVA-----TRWYR 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELldktldLQDWGMALRRADIYSLALLLWEILsRCPDLRPDSSPPPfQLAYEAELGNTPTSDELWALAVQERRR---- 372
Cdd:cd07878  183 APEI------MLNWMHYNQTVDIWSVGCIMAELL-KGKALFPGNDYID-QLKRIMEVVGTPSPEVLKKISSEHARKyiqs 254
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 373 -PYIP-----STWRcfATDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP-----------QESHPFPES 429
Cdd:cd07878  255 lPHMPqqdlkKIFR--GANPLAI-DLLEKMLVLDSDKRISAS------EALAHPyfsqyhdpedePEAEPYDES 319
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
219-331 8.07e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 50.65  E-value: 8.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLP-GLTQPPAWtptqpqgpaaimeAGTQRYMA 297
Cdd:cd05608  116 SGLEHLHQRR---------IIYRDLKPENVLLDDDGNVRISDLGLAVELKdGQTKTKGY-------------AGTPGFMA 173
                         90       100       110
                 ....*....|....*....|....*....|....
gi 767973831 298 PELLDKtldlQDWGMALrraDIYSLALLLWEILS 331
Cdd:cd05608  174 PELLLG----EEYDYSV---DYFTLGVTLYEMIA 200
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
98-331 8.24e-07

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: 50.23  E-value: 8.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAG--QLQGKLVAIKA--FPPRSVAQFQAERALYE--------LPGLQHDHIVRFITASrggpgrlLSGP 165
Cdd:cd06628    7 LIGSGSFGSVYLGmnASSGELMAVKQveLPSVSAENKDRKKSMLDalqreialLRELQHENIVQYLGSS-------SDAN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 166 LLVLELHpkdcvclcprgraphnsLCPIGSLCHYLTQYTSDWGSSLR-MALSLAQGLAFLHEErwqngqykpGIAHRDLS 244
Cdd:cd06628   80 HLNIFLE-----------------YVPGGSVATLLNNYGAFEESLVRnFVRQILKGLNYLHNR---------GIIHRDIK 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIREDGSCAIGDLGLAlvlPGLTQPPAWTPTQPQGPAAimeAGTQRYMAPELLDKTldlqdwgMALRRADIYSLAL 324
Cdd:cd06628  134 GANILVDNKGGIKISDFGIS---KKLEANSLSTKNNGARPSL---QGSVFWMAPEVVKQT-------SYTRKADIWSLGC 200

                 ....*..
gi 767973831 325 LLWEILS 331
Cdd:cd06628  201 LVVEMLT 207
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
190-420 8.36e-07

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: 50.43  E-value: 8.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSLCHYLTQ-YTSDWGSSLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 268
Cdd:cd14093   90 LCRKGELFDYLTEvVTLSEKKTRRIMRQLFEAVEFLH---------SLNIVHRDLKPENILLDDNLNVKISDFGFATRLD 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 269 gltqppawtptqpQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMALrRADIYSLALLLWEILSRCpdlrpdsspPPF--- 345
Cdd:cd14093  161 -------------EGEKLRELCGTPGYLAPEVLKCSMYDNAPGYGK-EVDMWACGVIMYTLLAGC---------PPFwhr 217
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 346 -QLayeaelgntptsdeLWALAVQERRRPYIPSTWRCFATDPdglRELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14093  218 kQM--------------VMLRNIMEGKYEFGSPEWDDISDTA---KDLISKLLVVDPKKRLTAE------EALEHP 270
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
194-420 8.46e-07

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


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 50.35  E-value: 8.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSSLR-MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltq 272
Cdd:cd14181  101 GELFDYLTEKVTLSEKETRsIMRSLLEAVSYLHANN---------IVHRDLKPENILLDDQLHIKLSDFGFSCHL----- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 273 ppawtptqpqGPAAIME--AGTQRYMAPELLDKTLDLQDWGMAlRRADIYSLALLLWEILsrcpdlrpdSSPPPFQlaYE 350
Cdd:cd14181  167 ----------EPGEKLRelCGTPGYLAPEILKCSMDETHPGYG-KEVDLWACGVILFTLL---------AGSPPFW--HR 224
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 351 AELgntptsdeLWALAVQERRRPYIPSTWRcfaTDPDGLRELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14181  225 RQM--------LMLRMIMEGRYQFSSPEWD---DRSSTVKDLISRLLVVDPEIRLTAE------QALQHP 277
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
191-404 9.16e-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: 50.19  E-value: 9.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYLTQ----YTSD--WGSSLRMALSLAqglaFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA 264
Cdd:cd08528   94 APLGEHFSSLKEknehFTEDriWNIFVQMVLALR----YLHKEK--------QIVHRDLKPNNIMLGEDDKVTITDFGLA 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 lvlpgltqppawTPTQPQGPAAIMEAGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEIlsrCpdlrpdSSPPP 344
Cdd:cd08528  162 ------------KQKGPESSKMTSVVGTILYSCPEIVQN----EPYG---EKADIWALGCILYQM---C------TLQPP 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 345 FQlayeaelgntptSDELWALAVQERRRPYIPSTWRCFAtdpDGLRELLEDCWDADPEAR 404
Cdd:cd08528  214 FY------------STNMLTLATKIVEAEYEPLPEGMYS---DDITFVIRSCLTPDPEAR 258
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
234-408 1.21e-06

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 49.74  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 234 YKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGltqppawtptqpQGPAAIMEAGTQRYMAPELLD-KTLDLqdwgm 312
Cdd:cd08221  118 HKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDS------------ESSMAESIVGTPYYMSPELVQgVKYNF----- 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 313 alrRADIYSLALLLWEILSRCpdlRPDSSPPPFQLAYEAELGNTPTSDELWAlavqerrrpyipstwrcfatdpDGLREL 392
Cdd:cd08221  181 ---KSDIWAVGCVLYELLTLK---RTFDATNPLRLAVKIVQGEYEDIDEQYS----------------------EEIIQL 232
                        170
                 ....*....|....*.
gi 767973831 393 LEDCWDADPEARLTAE 408
Cdd:cd08221  233 VHDCLHQDPEDRPTAE 248
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
115-412 1.28e-06

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: 49.64  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 115 KLVAIKAFPPRSVAQFQAERALYELpgLQHDHIVRFITASRGGPGRLLsgpllVLELhpkdcvclCPRGR-----APHNS 189
Cdd:cd14069   32 KFVDMKRAPGDCPENIKKEVCIQKM--LSHKNVVRFYGHRREGEFQYL-----FLEY--------ASGGElfdkiEPDVG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LcPIGSLCHYLTQytsdwgsslrmalsLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALV--- 266
Cdd:cd14069   97 M-PEDVAQFYFQQ--------------LMAGLKYLHSC---------GITHRDIKPENLLLDENDNLKISDFGLATVfry 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 267 ---LPGLTQPpawtptqpqgpaaimeAGTQRYMAPELLDKTldlqdwGMALRRADIYSLALLLWEILsrcpdlrpdsspp 343
Cdd:cd14069  153 kgkERLLNKM----------------CGTLPYVAPELLAKK------KYRAEPVDVWSCGIVLFAML------------- 197
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 344 pfqlayeaeLGNTP-----TSDELWALAVQERRRPYIPstWRCFATDPDG-LRELLEDcwdaDPEARLTAECVQQ 412
Cdd:cd14069  198 ---------AGELPwdqpsDSCQEYSDWKENKKTYLTP--WKKIDTAALSlLRKILTE----NPNKRITIEDIKK 257
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
117-416 1.34e-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: 49.66  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 117 VAIKAFPPRSVAQFQAE--RALYELPGLQHDHIVRFITASRGGPgrllsgPLLVLELhpkdcvclcprgraphnslCPIG 194
Cdd:cd05060   26 VAVKTLKQEHEKAGKKEflREASVMAQLDHPCIVRLIGVCKGEP------LMLVMEL-------------------APLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 195 SLCHYLTQYTSDWGSSLR-MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVL-PGLTQ 272
Cdd:cd05060   81 PLLKYLKKRREIPVSDLKeLAHQVAMGMAYLESKHF---------VHRDLAARNVLLVNRHQAKISDFGMSRALgAGSDY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 273 PPAWTptqpqgpaaimeAGTQ--RYMAPELLdktldlqDWGMALRRADIYSLALLLWEILSRcpdlrpdsSPPPFQlaye 350
Cdd:cd05060  152 YRATT------------AGRWplKWYAPECI-------NYGKFSSKSDVWSYGVTLWEAFSY--------GAKPYG---- 200
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 351 aELgntpTSDELWALAVQERRrpyIPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAA 416
Cdd:cd05060  201 -EM----KGPEVIAMLESGER---LPRPEEC----PQEIYSIMLSCWKYRPEDRPTFSELESTFRR 254
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
194-423 1.35e-06

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 50.11  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqp 273
Cdd:cd06656  101 GSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQ---------VIHRDIKSDNILLGMDGSVKLTDFGFCAQI------ 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 274 pawTPTQPQGPAAImeaGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAEL 353
Cdd:cd06656  166 ---TPEQSKRSTMV---GTPYWMAPEVVTR----KAYG---PKVDIWSLGIMAIEMVEGEP---PYLNENPLRALYLIAT 229
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973831 354 GNTPtsdelwalavqERRRPYipstwRCFATdpdgLRELLEDCWDADPEARLTA-ECVQQRLAALAHPQES 423
Cdd:cd06656  230 NGTP-----------ELQNPE-----RLSAV----FRDFLNRCLEMDVDRRGSAkELLQHPFLKLAKPLSS 280
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
194-417 1.35e-06

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: 49.68  E-value: 1.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSD--WGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPglT 271
Cdd:cd05033   90 GSLDKFLRENDGKftVTQLVGMLRGIASGMKYLSEM---------NYVHRDLAARNILVNSDLVCKVSDFGLSRRLE--D 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 272 QPPAWTPTQPQGPAaimeagtqRYMAPElldkTLDLQDWGMAlrrADIYSLALLLWEILSrcpdlrpdsspppfqlaY-E 350
Cdd:cd05033  159 SEATYTTKGGKIPI--------RWTAPE----AIAYRKFTSA---SDVWSFGIVMWEVMS-----------------YgE 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973831 351 AELGNTPTSDELWALAVQERrrpyIPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRLAAL 417
Cdd:cd05033  207 RPYWDMSNQDVIKAVEDGYR----LPPPMDC----PSALYQLMLDCWQKDRNERPTFSQIVSTLDKM 265
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
194-423 1.43e-06

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: 50.11  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqp 273
Cdd:cd06655  101 GSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQ---------VIHRDIKSDNVLLGMDGSVKLTDFGFCAQI------ 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 274 pawTPTQPQGPAAImeaGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAEL 353
Cdd:cd06655  166 ---TPEQSKRSTMV---GTPYWMAPEVVTR----KAYG---PKVDIWSLGIMAIEMVEGEP---PYLNENPLRALYLIAT 229
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973831 354 GNTPtsdelwALAVQERRRPYipstwrcfatdpdgLRELLEDCWDADPEARLTA-ECVQQRLAALAHPQES 423
Cdd:cd06655  230 NGTP------ELQNPEKLSPI--------------FRDFLNRCLEMDVEKRGSAkELLQHPFLKLAKPLSS 280
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
125-314 1.48e-06

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 49.69  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 125 RSVAQFQAERALYE---LPGLQHDHIVRFI----TASRGgpgrllsgpllvlelhpKDCVCLCprgraphNSLCPIGSLC 197
Cdd:cd14032   37 RKLTKVERQRFKEEaemLKGLQHPNIVRFYdfweSCAKG-----------------KRCIVLV-------TELMTSGTLK 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 198 HYLTQYTSDWGSSLR-MALSLAQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLAlvlpgltqppa 275
Cdd:cd14032   93 TYLKRFKVMKPKVLRsWCRQILKGLLFLHTR-------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLA----------- 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767973831 276 wtpTQPQGPAAIMEAGTQRYMAPEL----LDKTLDLQDWGMAL 314
Cdd:cd14032  155 ---TLKRASFAKSVIGTPEFMAPEMyeehYDESVDVYAFGMCM 194
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
213-331 1.84e-06

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: 49.64  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgltqPPAWTPTQpqgpAAIMEAGT 292
Cdd:cd14149  113 IARQTAQGMDYLHAK---------NIIHRDMKSNNIFLHEGLTVKIGDFGLATV------KSRWSGSQ----QVEQPTGS 173
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767973831 293 QRYMAPELldktLDLQDWGMALRRADIYSLALLLWEILS 331
Cdd:cd14149  174 ILWMAPEV----IRMQDNNPFSFQSDVYSYGIVLYELMT 208
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
212-344 2.08e-06

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: 49.34  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGlalVLPGLTQPPAWTPTqpqgpaaimeaG 291
Cdd:cd06621  109 KIAESVLKGLSYLHSRK---------IIHRDIKPSNILLTRKGQVKLCDFG---VSGELVNSLAGTFT-----------G 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767973831 292 TQRYMAPELLDKtldlQDWGMAlrrADIYSLALLLWEILSRCPDLRPDSSPPP 344
Cdd:cd06621  166 TSYYMAPERIQG----GPYSIT---SDVWSLGLTLLEVAQNRFPFPPEGEPPL 211
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
211-330 2.34e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 50.18  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPG--LTQppawTptqpqgpAAIM 288
Cdd:NF033483 110 VEIMIQILSALEHAHRN---------GIVHRDIKPQNILITKDGRVKVTDFGIARALSSttMTQ----T-------NSVL 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767973831 289 eaGTQRYMAPElldktldlQDWG-MALRRADIYSLALLLWEIL 330
Cdd:NF033483 170 --GTVHYLSPE--------QARGgTVDARSDIYSLGIVLYEML 202
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
220-330 2.41e-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: 49.20  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptqPQGPAAIMEAGTQRYMAPE 299
Cdd:cd05632  116 GLEDLHRE---------NTVYRDLKPENILLDDYGHIRISDLGLAVKI-------------PEGESIRGRVGTVGYMAPE 173
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767973831 300 LLDKtldlQDWGMAlrrADIYSLALLLWEIL 330
Cdd:cd05632  174 VLNN----QRYTLS---PDYWGLGCLIYEMI 197
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
207-334 2.51e-06

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: 48.67  E-value: 2.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDG---SCAIGDLGLALVLPGLtqpPAWTPTQpqg 283
Cdd:cd14156   88 WREKVELACDISRGMVYLHSKN---------IYHRDLNSKNCLIRVTPrgrEAVVTDFGLAREVGEM---PANDPER--- 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767973831 284 paAIMEAGTQRYMAPELL-DKTLDlqdwgmalRRADIYSLALLLWEILSRCP 334
Cdd:cd14156  153 --KLSLVGSAFWMAPEMLrGEPYD--------RKVDVFSFGIVLCEILARIP 194
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
117-331 2.95e-06

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 48.80  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 117 VAIKAFPPRSVAQ-FQA-ERALYELPGLQHDHIVRFITASRGGPGRLLSgpllvlelhpkdcvclcprgraphnSLCPIG 194
Cdd:cd05111   39 VAIKVIQDRSGRQsFQAvTDHMLAIGSLDHAYIVRLLGICPGASLQLVT-------------------------QLLPLG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 195 SLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPgltq 272
Cdd:cd05111   94 SLLDHVRQHRGSLGPQllLNWCVQIAKGMYYLEEHR---------MVHRNLAARNVLLKSPSQVQVADFGVADLLY---- 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 273 ppawtPTQPQgpAAIMEAGTQ-RYMAPELLdktldlqDWGMALRRADIYSLALLLWEILS 331
Cdd:cd05111  161 -----PDDKK--YFYSEAKTPiKWMALESI-------HFGKYTHQSDVWSYGVTVWEMMT 206
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
237-404 3.25e-06

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 48.71  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQpPAWTPTQPQGPAaimeagtqRYMAPElldktldlqdwGMALRR 316
Cdd:cd05066  126 GYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPE-AAYTTRGGKIPI--------RWTAPE-----------AIAYRK 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 317 ----ADIYSLALLLWEILSrcpdlrpdsspppfqlayeaeLGNTP---TSDELWALAVQERRRpyIPSTWRCfatdPDGL 389
Cdd:cd05066  186 ftsaSDVWSYGIVMWEVMS---------------------YGERPyweMSNQDVIKAIEEGYR--LPAPMDC----PAAL 238
                        170
                 ....*....|....*
gi 767973831 390 RELLEDCWDADPEAR 404
Cdd:cd05066  239 HQLMLDCWQKDRNER 253
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
194-404 3.98e-06

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: 48.43  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVlpgLT 271
Cdd:cd05063   91 GALDKYLRDHDGEFSSYqlVGMLRGIAAGMKYLSDMNY---------VHRDLAARNILVNSNLECKVSDFGLSRV---LE 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 272 QPPAWTPTQPQGPAAImeagtqRYMAPElldktldlqdwGMALRR----ADIYSLALLLWEILSrcpdlrpdsspppfql 347
Cdd:cd05063  159 DDPEGTYTTSGGKIPI------RWTAPE-----------AIAYRKftsaSDVWSFGIVMWEVMS---------------- 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973831 348 ayeaeLGNTPtsdeLWALAVQERRRPY-----IPSTWRCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd05063  206 -----FGERP----YWDMSNHEVMKAIndgfrLPAPMDC----PSAVYQLMLQCWQQDRARR 254
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
139-314 4.49e-06

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 48.51  E-value: 4.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 139 LPGLQHDHIVRFITASRGgpgrllsgpllvlELHPKDCVCLCprgraphNSLCPIGSLCHYLTQYTSDWGSSLR-MALSL 217
Cdd:cd14030   78 LKGLQHPNIVRFYDSWES-------------TVKGKKCIVLV-------TELMTSGTLKTYLKRFKVMKIKVLRsWCRQI 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 218 AQGLAFLHEErwqngqyKPGIAHRDLSSQNVLIR-EDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIMEAGTQRYM 296
Cdd:cd14030  138 LKGLQFLHTR-------TPPIIHRDLKCDNIFITgPTGSVKIGDLGLA--------------TLKRASFAKSVIGTPEFM 196
                        170       180
                 ....*....|....*....|..
gi 767973831 297 APEL----LDKTLDLQDWGMAL 314
Cdd:cd14030  197 APEMyeekYDESVDVYAFGMCM 218
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
99-346 4.83e-06

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 48.06  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQLQG--KLVAIKafpprSVAQFQAERALYELP---GLQHDHIVRFI----TasrggpgrllSGPL-LV 168
Cdd:cd14010    8 IGRGKHSVVYKGRRKGtiEFVAIK-----CVDKSKRPEVLNEVRlthELKHPNVLKFYewyeT----------SNHLwLV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 169 LELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQN 247
Cdd:cd14010   73 VEY-------------------CTGGDLETLLRQDGNLPESSVRKfGRDLVRGLHYIH---------SKGIIYCDLKPSN 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 248 VLIREDGSCAIGDLGLALVLPG----LTQPPAWTPTQPQGPAAIMEAGTQRYMAPELLDKtldlQDWGMAlrrADIYSLA 323
Cdd:cd14010  125 ILLDGNGTLKLSDFGLARREGEilkeLFGQFSDEGNVNKVSKKQAKRGTPYYMAPELFQG----GVHSFA---SDLWALG 197
                        250       260
                 ....*....|....*....|...
gi 767973831 324 LLLWEILsrcpdlrpdSSPPPFQ 346
Cdd:cd14010  198 CVLYEMF---------TGKPPFV 211
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
219-407 5.25e-06

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 48.20  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGTQRYMAP 298
Cdd:cd06611  114 EALNFLHSHK---------VIHRDLKAGNILLTLDGDVKLADFGVSAKN---------KSTLQKRDTFI---GTPYWMAP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELL----DKTlDLQDWgmalrRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTSDElwalavqerrrpy 374
Cdd:cd06611  173 EVVacetFKD-NPYDY-----KADIWSLGITLIELAQMEP---PHHELNPMRVLLKILKSEPPTLDQ------------- 230
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767973831 375 iPSTWRcfatdpDGLRELLEDCWDADPEARLTA 407
Cdd:cd06611  231 -PSKWS------SSFNDFLKSCLVKDPDDRPTA 256
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
142-404 5.37e-06

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: 47.80  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 142 LQHDHIVRFItasrggpGRLLSGPL-LVLELhpkdcvclcprgraphnslCPIGSLCHYLTQYtSDWGSSLRM---ALSL 217
Cdd:cd05056   64 FDHPHIVKLI-------GVITENPVwIVMEL-------------------APLGELRSYLQVN-KYSLDLASLilyAYQL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 218 AQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPTQPqgpaaimeagtQRYMA 297
Cdd:cd05056  117 STALAYLESKRF---------VHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASKGKLP-----------IKWMA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 298 PElldkTLDLQDWGMAlrrADIYSLALLLWEILSRcpdlrpdsSPPPFQlayeaelgNTPTSDELWALAVQERrrpyIPS 377
Cdd:cd05056  177 PE----SINFRRFTSA---SDVWMFGVCMWEILML--------GVKPFQ--------GVKNNDVIGRIENGER----LPM 229
                        250       260
                 ....*....|....*....|....*..
gi 767973831 378 TWRCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd05056  230 PPNC----PPTLYSLMTKCWAYDPSKR 252
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
234-426 5.81e-06

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 47.86  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 234 YKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTptqpqgpaaimeaGTQRYMAPELLDKTLDLQdwgma 313
Cdd:cd05611  114 HQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNKKFV-------------GTPDYLAPETILGVGDDK----- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 314 lrRADIYSLALLLWEILsrcpdlrpdSSPPPFqlayEAElgntpTSDELWALAvqERRRPYIPSTWRCFATdPDGlRELL 393
Cdd:cd05611  176 --MSDWWSLGCVIFEFL---------FGYPPF----HAE-----TPDAVFDNI--LSRRINWPEEVKEFCS-PEA-VDLI 231
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767973831 394 EDCWDADPEARLTAECVQQrlaalahpQESHPF 426
Cdd:cd05611  232 NRLLCMDPAKRLGANGYQE--------IKSHPF 256
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
237-420 6.47e-06

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: 48.07  E-value: 6.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgltqppawtpTQPQGPAAIM---EAGTQRYMAPELLdktLDLQDWGMA 313
Cdd:cd07849  126 NVLHRDLKPSNLLLNTNCDLKICDFGLARI------------ADPEHDHTGFlteYVATRWYRAPEIM---LNSKGYTKA 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 314 LrraDIYSLALLLWEILSRCP-----DLRPdsspppfQLAYEAELGNTPTSDELWALaVQERRRPYIPS-------TW-R 380
Cdd:cd07849  191 I---DIWSVGCILAEMLSNRPlfpgkDYLH-------QLNLILGILGTPSQEDLNCI-ISLKARNYIKSlpfkpkvPWnK 259
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767973831 381 CFA-TDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07849  260 LFPnADPKAL-DLLDKMLTFNPHKRITVE------EALAHP 293
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
114-373 6.57e-06

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: 47.71  E-value: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFP--------PRSVAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLSgplLVLELHPkdcvclcprGRA 185
Cdd:cd06653   27 GRELAVKQVPfdpdsqetSKEVNALECEIQL--LKNLRHDRIVQYYGCLRDPEEKKLS---IFVEYMP---------GGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 186 PHNSLCPIGSLCHYLTQytsdwgsslRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAL 265
Cdd:cd06653   93 VKDQLKAYGALTENVTR---------RYTRQILQGVSYLHSNM---------IVHRDIKGANILRDSAGNVKLGDFGASK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 266 VLPGLTQppawtptqpQGPAAIMEAGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSRCPDLRP-DSSPPP 344
Cdd:cd06653  155 RIQTICM---------SGTGIKSVTGTPYWMSPEVISG----EGYG---RKADVWSVACTVVEMLTEKPPWAEyEAMAAI 218
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 767973831 345 FQLAYEAELGNTPTS------DELWALAVQERRRP 373
Cdd:cd06653  219 FKIATQPTKPQLPDGvsdacrDFLRQIFVEEKRRP 253
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
214-406 6.75e-06

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 47.87  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgLTQPPAWTPTQPQGPAaimeagtq 293
Cdd:cd05054  144 SFQVARGMEFLASRK---------CIHRDLAARNILLSENNVVKICDFGLARDI--YKDPDYVRKGDARLPL-------- 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 294 RYMAPE-LLDKTLDLQdwgmalrrADIYSLALLLWEILSrcpdlrpdsspppfqlayeaeLGNTP----TSDELWALAVQ 368
Cdd:cd05054  205 KWMAPEsIFDKVYTTQ--------SDVWSFGVLLWEIFS---------------------LGASPypgvQMDEEFCRRLK 255
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767973831 369 ERRRPYIPStwrcFATDPdgLRELLEDCWDADPEARLT 406
Cdd:cd05054  256 EGTRMRAPE----YTTPE--IYQIMLDCWHGEPKERPT 287
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
200-420 7.02e-06

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: 47.47  E-value: 7.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 200 LTQYTSDWGS-----SLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGS--CAIGDLGLALVlpgltq 272
Cdd:cd14098   88 LMDFIMAWGAipeqhARELTKQILEAMAYTH---------SMGITHRDLKPENILITQDDPviVKISDFGLAKV------ 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 273 ppawtptqpQGPAAIMEA--GTQRYMAPELLdKTLDLQDWGMALRRADIYSLALLLWEILSRCPDLRPDSSPPPFQLAYE 350
Cdd:cd14098  153 ---------IHTGTFLVTfcGTMAYLAPEIL-MSKEQNLQGGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRK 222
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 351 AELGNTPTSDelwaLAVQERRRPYIPStwrcfatdpdglreLLedcwDADPEARLTAecvqqrLAALAHP 420
Cdd:cd14098  223 GRYTQPPLVD----FNISEEAIDFILR--------------LL----DVDPEKRMTA------AQALDHP 264
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
240-420 7.24e-06

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: 47.78  E-value: 7.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 240 HRDLSSQNVLIREDGSCAIGDLGLALvlpgltqppAWTPTQPQGPAAIMEAGTQR-YMAPELLdktLDLQDWGMALrraD 318
Cdd:cd07857  128 HRDLKPGNLLVNADCELKICDFGLAR---------GFSENPGENAGFMTEYVATRwYRAPEIM---LSFQSYTKAI---D 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 319 IYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTSDEL--------WALAVQERRRPYIPSTWRCFATDPDGLr 390
Cdd:cd07857  193 VWSVGCILAELLGRKPVFKGKDYVD--QLNQILQVLGTPDEETLsrigspkaQNYIRSLPNIPKKPFESIFPNANPLAL- 269
                        170       180       190
                 ....*....|....*....|....*....|
gi 767973831 391 ELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07857  270 DLLEKLLAFDPTKRISVE------EALEHP 293
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
132-407 7.39e-06

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: 47.35  E-value: 7.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 132 AERALYELPGLQHDHIVRFITASRGGPGRLLSGPLLVLELHpkdcvclcprgraphnslCPIGSLCHYLTQYTS-DWGSS 210
Cdd:cd14012   45 LEKELESLKKLRHPNLVSYLAFSIERRGRSDGWKVYLLTEY------------------APGGSLSELLDSVGSvPLDTA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIgdlgLALVLPGLTQPPAWTPTQPqgpaAIMEA 290
Cdd:cd14012  107 RRWTLQLLEALEYLH---------RNGVVHKSLHAGNVLLDRDAGTGI----VKLTDYSLGKTLLDMCSRG----SLDEF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 291 GTQRYMAPELLDKTLDLQdwgmalRRADIYSLALLLWEILSRCPDLRPDSSPPPFqlayeaelgntPTSDELwalavqer 370
Cdd:cd14012  170 KQTYWLPPELAQGSKSPT------RKTDVWDLGLLFLQMLFGLDVLEKYTSPNPV-----------LVSLDL-------- 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 767973831 371 rrpyipstwrcfatdPDGLRELLEDCWDADPEARLTA 407
Cdd:cd14012  225 ---------------SASLQDFLSKCLSLDPKKRPTA 246
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
214-420 7.45e-06

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 47.98  E-value: 7.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL--VLPGLTqppawTPTQpqgpaaimeAG 291
Cdd:cd05590  102 AAEITSALMFLHDK---------GIIYRDLKLDNVLLDHEGHCKLADFGMCKegIFNGKT-----TSTF---------CG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 292 TQRYMAPELLDKTLdlqdWGMALrraDIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAELGNTPTSDELwalavqerr 371
Cdd:cd05590  159 TPDYIAPEILQEML----YGPSV---DWWAMGVLLYEML---------CGHAPFEAENEDDLFEAILNDEV--------- 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 767973831 372 rpyIPSTWRCFATDpdglrELLEDCWDADPEARLTAECVQQRLAALAHP 420
Cdd:cd05590  214 ---VYPTWLSQDAV-----DILKAFMTKNPTMRLGSLTLGGEEAILRHP 254
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
212-410 7.70e-06

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 47.32  E-value: 7.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIReDGSCA---IGDLGLalvlpgltqppawtpTQPQGPAAIM 288
Cdd:cd13987   95 RCAAQLASALDFMHSKN---------LVHRDIKPENVLLF-DKDCRrvkLCDFGL---------------TRRVGSTVKR 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 289 EAGTQRYMAPELLDktLDLQDWGMALRRADIYSLALLLWEILSRC-PDLRPDSSPPPFQlAYEAelgntptsdelWalav 367
Cdd:cd13987  150 VSGTIPYTAPEVCE--AKKNEGFVVDPSIDVWAFGVLLFCCLTGNfPWEKADSDDQFYE-EFVR-----------W---- 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767973831 368 QERRRPYIPSTWRCFAtdPDGLR---ELLEdcwdADPEARLTAECV 410
Cdd:cd13987  212 QKRKNTAVPSQWRRFT--PKALRmfkKLLA----PEPERRCSIKEV 251
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
194-426 7.90e-06

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: 47.23  E-value: 7.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqp 273
Cdd:cd06647   89 GSLTDVVTETCMDEGQIAAVCRECLQALEFLHSN---------QVIHRDIKSDNILLGMDGSVKLTDFGFCAQI------ 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 274 pawTPTQPQGPAAImeaGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAEL 353
Cdd:cd06647  154 ---TPEQSKRSTMV---GTPYWMAPEVVTR----KAYG---PKVDIWSLGIMAIEMVEGEP---PYLNENPLRALYLIAT 217
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973831 354 GNTPTsdelwaLAVQERRRPYipstwrcfatdpdgLRELLEDCWDADPEARLTAECVQQrlaalahpqesHPF 426
Cdd:cd06647  218 NGTPE------LQNPEKLSAI--------------FRDFLNRCLEMDVEKRGSAKELLQ-----------HPF 259
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
213-414 8.40e-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: 47.37  E-value: 8.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLP--------GLTQPPAWTptqpqGP 284
Cdd:cd05069  113 MAAQIADGMAYIERMNY---------IHRDLRAANILVGDNLVCKIADFGLARLIEdneytarqGAKFPIKWT-----AP 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 285 AAIMeagtqrymapelldktldlqdWGMALRRADIYSLALLLWEILSRcpdlrpdsspppfqlayeaelGNTPTSDELWA 364
Cdd:cd05069  179 EAAL---------------------YGRFTIKSDVWSFGILLTELVTK---------------------GRVPYPGMVNR 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767973831 365 LAVQERRRPY-IPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd05069  217 EVLEQVERGYrMPCPQGC----PESLHELMKLCWKKDPDERPTFEYIQSFL 263
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
212-334 9.02e-06

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: 47.33  E-value: 9.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCA---IGDLGLAlvlPGLTQPPAWTPTQPqgPAAIM 288
Cdd:cd14174  104 RVVRDIASALDFLHTK---------GIAHRDLKPENILCESPDKVSpvkICDFDLG---SGVKLNSACTPITT--PELTT 169
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767973831 289 EAGTQRYMAPELLDKTLDlqDWGMALRRADIYSLALLLWEILSRCP 334
Cdd:cd14174  170 PCGSAEYMAPEVVEVFTD--EATFYDKRCDLWSLGVILYIMLSGYP 213
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
200-420 9.29e-06

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 47.30  E-value: 9.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 200 LTQYTSDWGSSLRM------ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPgltqp 273
Cdd:cd07873   86 LKQYLDDCGNSINMhnvklfLFQLLRGLAYCHRRK---------VLHRDLKPQNLLINERGELKLADFGLARAKS----- 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 274 pawTPTQPQGPaaimEAGTQRYMAPELLDKTLDLQDwgmalrRADIYSLALLLWEILSRCPdLRPDSSPPPfQLAYEAEL 353
Cdd:cd07873  152 ---IPTKTYSN----EVVTLWYRPPDILLGSTDYST------QIDMWGVGCIFYEMSTGRP-LFPGSTVEE-QLHFIFRI 216
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 354 GNTPTSDELWALAVQERRRPYIPSTWRCFAT-------DPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07873  217 LGTPTEETWPGILSNEEFKSYNYPKYRADALhnhaprlDSDGA-DLLSKLLQFEGRKRISAE------EAMKHP 283
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
214-330 9.79e-06

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 47.35  E-value: 9.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptqPQGPAAIMEAGTQ 293
Cdd:cd05605  108 AAEITCGLEHLHSER---------IVYRDLKPENILLDDHGHVRISDLGLAVEI-------------PEGETIRGRVGTV 165
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767973831 294 RYMAPELLDKTLdlqdWGMAlrrADIYSLALLLWEIL 330
Cdd:cd05605  166 GYMAPEVVKNER----YTFS---PDWWGLGCLIYEMI 195
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
217-420 1.06e-05

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: 47.17  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqpPAWTPTQPQgpaaimeAGTQR-- 294
Cdd:cd07840  113 LLEGLQYLHSN---------GILHRDIKGSNILINNDGVLKLADFGLA---------RPYTKENNA-------DYTNRvi 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 295 ---YMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPPFQLAYEAeLGnTPTsDELWA------L 365
Cdd:cd07840  168 tlwYRPPELL---LGATRYGPEV---DMWSVGCILAELFTGKPIFQGKTELEQLEKIFEL-CG-SPT-EENWPgvsdlpW 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 366 AVQERRRPYIPSTWRCF---ATDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07840  239 FENLKPKKPYKRRLREVfknVIDPSAL-DLLDKLLTLDPKKRISAD------QALQHE 289
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
214-444 1.08e-05

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 47.32  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTqppaWTPTQPQGPAAImeagtq 293
Cdd:cd05100  140 AYQVARGMEYLASQK---------CIHRDLAARNVLVTEDNVMKIADFGLARDVHNID----YYKKTTNGRLPV------ 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 294 RYMAPE-LLDKTLDLQdwgmalrrADIYSLALLLWEILSrcpdlrPDSSPPPfqlayeaelgNTPTsDELWALaVQERRR 372
Cdd:cd05100  201 KWMAPEaLFDRVYTHQ--------SDVWSFGVLLWEIFT------LGGSPYP----------GIPV-EELFKL-LKEGHR 254
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 373 PYIPstwrcfATDPDGLRELLEDCWDADPEARLTAECVQQ---RLAALAHPQE----SHPFPESCPrGCPPlCPEDCTS 444
Cdd:cd05100  255 MDKP------ANCTHELYMIMRECWHAVPSQRPTFKQLVEdldRVLTVTSTDEyldlSVPFEQYSP-GCPD-SPSSCSS 325
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
220-330 1.13e-05

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 47.21  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL--VLPGLTqppawTPTQpqgpaaimeAGTQRYMA 297
Cdd:cd05570  108 ALQFLHER---------GIIYRDLKLDNVLLDAEGHIKIADFGMCKegIWGGNT-----TSTF---------CGTPDYIA 164
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767973831 298 PELLDKtldlQDWGMAlrrADIYSLALLLWEIL 330
Cdd:cd05570  165 PEILRE----QDYGFS---VDWWALGVLLYEML 190
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
177-269 1.24e-05

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 46.98  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 177 VCLCPRGRAPhNSLCPIGSLCHYLTQYTSDWGSSLRM--ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDG 254
Cdd:cd05110   77 VCLSPTIQLV-TQLMPHGCLLDYVHEHKDNIGSQLLLnwCVQIAKGMMYLEERR---------LVHRDLAARNVLVKSPN 146
                         90
                 ....*....|....*
gi 767973831 255 SCAIGDLGLALVLPG 269
Cdd:cd05110  147 HVKITDFGLARLLEG 161
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
96-358 1.30e-05

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: 46.93  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAGQLQGKL---VAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRggpgrlLSGPL-LVL 169
Cdd:cd14202    7 KDLIGHGAFAVVFKGRHKEKHdleVAVKCINKKNLAKSQTllGKEIKILKELKHENIVALYDFQE------IANSVyLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 170 ELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSSLRMALS-LAQGLAFLHEErwqngqykpGIAHRDLSSQNV 248
Cdd:cd14202   81 EY-------------------CNGGDLADYLHTMRTLSEDTIRLFLQqIAGAMKMLHSK---------GIIHRDLKPQNI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 249 LIREDGS---------CAIGDLGLALVLPGLTQppawtptqpqgpAAIMeAGTQRYMAPE-LLDKTLDlqdwgmalRRAD 318
Cdd:cd14202  133 LLSYSGGrksnpnnirIKIADFGFARYLQNNMM------------AATL-CGSPMYMAPEvIMSQHYD--------AKAD 191
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767973831 319 IYSLALLLWEILSRCPDLRPdSSPPPFQLAYEAELGNTPT 358
Cdd:cd14202  192 LWSIGTIIYQCLTGKAPFQA-SSPQDLRLFYEKNKSLSPN 230
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
116-418 1.33e-05

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: 46.96  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 116 LVAIKAFPPRS---VAQFQAERALyeLPGLQHDHIVRFITASrggpgrLLSGPL-LVLELHPKDCVCLCPRGRAPHNSLC 191
Cdd:cd05093   37 LVAVKTLKDASdnaRKDFHREAEL--LTNLQHEHIVKFYGVC------VEGDPLiMVFEYMKHGDLNKFLRAHGPDAVLM 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 192 PIGSLCHYLTQytsdwGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLA------- 264
Cdd:cd05093  109 AEGNRPAELTQ-----SQMLHIAQQIAAGMVYLASQHF---------VHRDLATRNCLVGENLLVKIGDFGMSrdvystd 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 -LVLPGLTQ-PPAWTPtqpqgPAAIMeagtQRYMAPElldktldlqdwgmalrrADIYSLALLLWEILSRcpdlrpdSSP 342
Cdd:cd05093  175 yYRVGGHTMlPIRWMP-----PESIM----YRKFTTE-----------------SDVWSLGVVLWEIFTY-------GKQ 221
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 343 PPFQLayeaelgntpTSDELWALAVQER--RRPyipstwrcfATDPDGLRELLEDCWDADPEARLTAECVQQRLAALA 418
Cdd:cd05093  222 PWYQL----------SNNEVIECITQGRvlQRP---------RTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLA 280
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
99-426 1.35e-05

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 46.83  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  99 IREGGHAVVWAGQ--LQGKLVAIKAFPPRS------VAQFQAERALyeLPGLQHDHIVRF---ITASRggpgrllsgPL- 166
Cdd:cd05579    1 ISRGAYGRVYLAKkkSTGDLYAIKVIKKRDmirknqVDSVLAERNI--LSQAQNPFVVKLyysFQGKK---------NLy 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 167 LVLE-LHPKDCVCLcprgraphnsLCPIGSLCHYL-TQYTSDwgsslrmalsLAQGLAFLHEErwqngqykpGIAHRDLS 244
Cdd:cd05579   70 LVMEyLPGGDLYSL----------LENVGALDEDVaRIYIAE----------IVLALEYLHSH---------GIIHRDLK 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIREDGSCAIGDLGLALVlpGLTQPPAWTPTQPQGPAAIMEA-----GTQRYMAPELLDKtldlQDWGMAlrrADI 319
Cdd:cd05579  121 PDNILIDANGHLKLTDFGLSKV--GLVRRQIKLSIQKKSNGAPEKEdrrivGTPDYLAPEILLG----QGHGKT---VDW 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 320 YSLALLLWEILSRCpdlrpdsspPPFQlayeaelGNTPtsDELWAlAVQERRRPYipstwrcfatdPDGLrELLEDCWDA 399
Cdd:cd05579  192 WSLGVILYEFLVGI---------PPFH-------AETP--EEIFQ-NILNGKIEW-----------PEDP-EVSDEAKDL 240
                        330       340       350
                 ....*....|....*....|....*....|....
gi 767973831 400 -------DPEARLTAECVQQrlaalahpQESHPF 426
Cdd:cd05579  241 isklltpDPEKRLGAKGIEE--------IKNHPF 266
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
213-408 1.36e-05

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: 46.97  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGT 292
Cdd:cd06640  106 MLKEILKGLDYLHSEK---------KIHRDIKAANVLLSEQGDVKLADFGVAGQL---------TDTQIKRNTFV---GT 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 293 QRYMAPELLDKTldlqdwgMALRRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTsdelwalAVQERRR 372
Cdd:cd06640  165 PFWMAPEVIQQS-------AYDSKADIWSLGITAIELAKGEP---PNSDMHPMRVLFLIPKNNPPT-------LVGDFSK 227
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767973831 373 PYipstwrcfatdpdglRELLEDCWDADPEARLTAE 408
Cdd:cd06640  228 PF---------------KEFIDACLNKDPSFRPTAK 248
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
200-420 1.38e-05

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


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 46.93  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 200 LTQYTSDWGSSLRM------ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPgltqp 273
Cdd:cd07871   89 LKQYLDNCGNLMSMhnvkifMFQLLRGLSYCHKRK---------ILHRDLKPQNLLINEKGELKLADFGLARAKS----- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 274 pawTPTQPQGPaaimEAGTQRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPPFQLAYeaEL 353
Cdd:cd07871  155 ---VPTKTYSN----EVVTLWYRPPDVL---LGSTEYSTPI---DMWGVGCILYEMATGRPMFPGSTVKEELHLIF--RL 219
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 354 GNTPTSDELWALAVQERRRPYIPSTWRCFA-------TDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07871  220 LGTPTEETWPGVTSNEEFRSYLFPQYRAQPlinhaprLDTDGI-DLLSSLLLYETKSRISAE------AALRHS 286
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
190-415 1.38e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 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: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 46.87  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSLCHYLTQY-----------TSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAI 258
Cdd:cd14206   78 FCQLGDLKRYLRAQrkadgmtpdlpTRDLRTLQRMAYEITLGLLHLHKNNY---------IHSDLALRNCLLTSDLTVRI 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 259 GDLGLALVLPG----LTQPPAWTPTqpqgpaaimeagtqRYMAPELLDK---TLDLQDwgmALRRADIYSLALLLWEILs 331
Cdd:cd14206  149 GDYGLSHNNYKedyyLTPDRLWIPL--------------RWVAPELLDElhgNLIVVD---QSKESNVWSLGVTIWELF- 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 332 rcpdlrpdsspppfqlayeaELGNTP----TSDELWALAVQERR----RPyipstwRCFATDPDGLRELLEDCWdADPEA 403
Cdd:cd14206  211 --------------------EFGAQPyrhlSDEEVLTFVVREQQmklaKP------RLKLPYADYWYEIMQSCW-LPPSQ 263
                        250
                 ....*....|..
gi 767973831 404 RLTAECVQQRLA 415
Cdd:cd14206  264 RPSVEELHLQLS 275
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
217-329 1.39e-05

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 46.65  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIReDGSCAIGDLGLALVLPGLTQppawtptqpqgpAAIMEAGTQRYM 296
Cdd:cd08222  115 LLLAVQYMHERR---------ILHRDLKAKNIFLK-NNVIKVGDFGISRILMGTSD------------LATTFTGTPYYM 172
                         90       100       110
                 ....*....|....*....|....*....|...
gi 767973831 297 APELLDKtldlQDWGmalRRADIYSLALLLWEI 329
Cdd:cd08222  173 SPEVLKH----EGYN---SKSDIWSLGCILYEM 198
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
95-426 1.45e-05

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: 46.50  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  95 CEQVIREGGHA-VVWAGQLQGKLVAIKafppRSVAQFqAERALYELPGLQ----HDHIVRFITASRGGPGRLLSgpllvL 169
Cdd:cd13982    5 SPKVLGYGSEGtIVFRGTFDGRPVAVK----RLLPEF-FDFADREVQLLResdeHPNVIRYFCTEKDRQFLYIA-----L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 170 ELhpkdCVClcprgraphnslcpigSLCHYLTQYTSDWGS------SLRMALSLAQGLAFLHEErwqngqykpGIAHRDL 243
Cdd:cd13982   75 EL----CAA----------------SLQDLVESPRESKLFlrpglePVRLLRQIASGLAHLHSL---------NIVHRDL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 244 SSQNVLIREDGSCA-----IGDLGLALVLPGLTQppawTPTQPQGPaaimeAGTQRYMAPELLDktldlQDWGMALRRA- 317
Cdd:cd13982  126 KPQNILISTPNAHGnvramISDFGLCKKLDVGRS----SFSRRSGV-----AGTSGWIAPEMLS-----GSTKRRQTRAv 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 318 DIYSLALLLWEILSRCPDlrpdssppPFQLAYEAE---LGNTPTSDELwalavqERRRPYIPStwrcfatdpdgLRELLE 394
Cdd:cd13982  192 DIFSLGCVFYYVLSGGSH--------PFGDKLEREaniLKGKYSLDKL------LSLGEHGPE-----------AQDLIE 246
                        330       340       350
                 ....*....|....*....|....*....|..
gi 767973831 395 DCWDADPEARLTAECVqqrlaalahpqESHPF 426
Cdd:cd13982  247 RMIDFDPEKRPSAEEV-----------LNHPF 267
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
219-420 1.50e-05

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


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 46.80  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEerwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgltqppawtptqpQGPAAIMEAGTQRYMAP 298
Cdd:cd07856  119 RGLKYVHS---------AGVIHRDLKPSNILVNENCDLKICDFGLARI---------------QDPQMTGYVSTRYYRAP 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPdLRPDSSPPPfQLAYEAELGNTPTSDELWALAVQER-------- 370
Cdd:cd07856  175 EIM---LTWQKYDVEV---DIWSAGCIFAEMLEGKP-LFPGKDHVN-QFSIITELLGTPPDDVINTICSENTlrfvqslp 246
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767973831 371 RRPYIPSTWRCFATDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07856  247 KRERVPFSEKFKNADPDAI-DLLEKMLVFDPKKRISAA------EALAHP 289
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
211-404 1.59e-05

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: 46.56  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLglalvlpGLTQPPAWTPTQPQGPAAIMEA 290
Cdd:cd05062  122 IQMAGEIADGMAYLNANKF---------VHRDLAARNCMVAEDFTVKIGDF-------GMTRDIYETDYYRKGGKGLLPV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 291 gtqRYMAPElldktlDLQDwGMALRRADIYSLALLLWEI--LSRCPdLRPDSSPPPFQLAYEAELGNTPTSdelwalavq 368
Cdd:cd05062  186 ---RWMSPE------SLKD-GVFTTYSDVWSFGVVLWEIatLAEQP-YQGMSNEQVLRFVMEGGLLDKPDN--------- 245
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767973831 369 errrpyipstwrCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd05062  246 ------------C----PDMLFELMRMCWQYNPKMR 265
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
214-312 1.66e-05

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 46.52  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptqPQGPAAIMEAGTQ 293
Cdd:cd05631  108 AAELCCGLEDLQRER---------IVYRDLKPENILLDDRGHIRISDLGLAVQI-------------PEGETVRGRVGTV 165
                         90       100
                 ....*....|....*....|..
gi 767973831 294 RYMAPELLDK---TLDLQDWGM 312
Cdd:cd05631  166 GYMAPEVINNekyTFSPDWWGL 187
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
207-406 1.77e-05

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 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: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 46.90  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 207 WGSSLRM------ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlPGLTQPPAWTptq 280
Cdd:cd05102  165 WQSPLTMedlicySFQVARGMEFLASRK---------CIHRDLAARNILLSENNVVKICDFGLA---RDIYKDPDYV--- 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 281 PQGPAAImeagTQRYMAPE-LLDKTLDLQdwgmalrrADIYSLALLLWEILSRcpdlrpDSSP-PPFQLayeaelgntpt 358
Cdd:cd05102  230 RKGSARL----PLKWMAPEsIFDKVYTTQ--------SDVWSFGVLLWEIFSL------GASPyPGVQI----------- 280
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767973831 359 sDELWALAVQERRRPYIPStwrcFATDPdgLRELLEDCWDADPEARLT 406
Cdd:cd05102  281 -NEEFCQRLKDGTRMRAPE----YATPE--IYRIMLSCWHGDPKERPT 321
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
213-436 1.82e-05

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: 46.59  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEeRWqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPgltqppawTPTQPQGPAAImeagT 292
Cdd:cd07845  113 LMLQLLRGLQYLHE-NF--------IIHRDLKVSNLLLTDKGCLKIADFGLARTYG--------LPAKPMTPKVV----T 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 293 QRYMAPELL--DKTLDlqdwgmalRRADIYSLALLLWEILSRCPdLRPDSSPPPfQLAYEAELGNTPtSDELW----AL- 365
Cdd:cd07845  172 LWYRAPELLlgCTTYT--------TAIDMWAVGCILAELLAHKP-LLPGKSEIE-QLDLIIQLLGTP-NESIWpgfsDLp 240
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 366 AVQE---RRRPYIPSTWRCFATDPDGLReLLEDCWDADPEARLTAEcvqqrlAALAHPQeshpFPEScPRGCPP 436
Cdd:cd07845  241 LVGKftlPKQPYNNLKHKFPWLSEAGLR-LLNFLLMYDPKKRATAE------EALESSY----FKEK-PLPCEP 302
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
217-420 2.22e-05

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 46.17  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGS------CAIgDLGLALVLPGLTQPPAwtptqpqGPAAIMEA 290
Cdd:cd14173  109 IASALDFLHNK---------GIAHRDLKPENILCEHPNQvspvkiCDF-DLGSGIKLNSDCSPIS-------TPELLTPC 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 291 GTQRYMAPELLDKTldLQDWGMALRRADIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAELG-----NTPTSDELWAL 365
Cdd:cd14173  172 GSAEYMAPEVVEAF--NEEASIYDKRCDLWSLGVILYIML---------SGYPPFVGRCGSDCGwdrgeACPACQNMLFE 240
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 366 AVQERRRPYIPSTWrcfATDPDGLRELLEDCWDADPEARLTAECVQQrlaalaHP 420
Cdd:cd14173  241 SIQEGKYEFPEKDW---AHISCAAKDLISKLLVRDAKQRLSAAQVLQ------HP 286
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
98-302 2.37e-05

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: 45.96  E-value: 2.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQ--LQGKLVAIKAF----PPRSVAQFQAERALYELPGlqHDHIVRFITASRGGP---GRLLSGPLLV 168
Cdd:cd14036    7 VIAEGGFAFVYEAQdvGTGKEYALKRLlsneEEKNKAIIQEINFMKKLSG--HPNIVQFCSAASIGKeesDQGQAEYLLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 169 LELHPKDCVCLCPRGRAPHNSLCpigslchyltqytsdwGSSLRMALSLAQGLAFLHEErwqngqyKPGIAHRDLSSQNV 248
Cdd:cd14036   85 TELCKGQLVDFVKKVEAPGPFSP----------------DTVLKIFYQTCRAVQHMHKQ-------SPPIIHRDLKIENL 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 249 LIREDGSCAIGDLGLALVLPgLTQPPAWTPTQ-PQGPAAIMEAGTQRYMAPELLD 302
Cdd:cd14036  142 LIGNQGQIKLCDFGSATTEA-HYPDYSWSAQKrSLVEDEITRNTTPMYRTPEMID 195
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
96-330 2.63e-05

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 45.74  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  96 EQVIREGGHAVVWAGQL--QGKLVAIK--AFPPRSVAQ-FQAE-RALYELPGlqHDHIVRFI--TASRGGPGRLLSgpLL 167
Cdd:cd14037    8 EKYLAEGGFAHVYLVKTsnGGNRAALKrvYVNDEHDLNvCKREiEIMKRLSG--HKNIVGYIdsSANRSGNGVYEV--LL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 168 VLELhpkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHeerwqngQYKPGIAHRDLS 244
Cdd:cd14037   84 LMEY-------------------CKGGGVIDLMNQRLQTGLTEseiLKIFCDVCEAVAAMH-------YLKPPLIHRDLK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIREDGSCAIGDLGLAlvlpgltQPPAWTPTQPQGPAA----IMEAGTQRYMAPELLD----KTLDLqdwgmalrR 316
Cdd:cd14037  138 VENVLISDSGNYKLCDFGSA-------TTKILPPQTKQGVTYveedIKKYTTLQYRAPEMIDlyrgKPITE--------K 202
                        250
                 ....*....|....
gi 767973831 317 ADIYSLALLLWEIL 330
Cdd:cd14037  203 SDIWALGCLLYKLC 216
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
217-331 3.05e-05

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 45.51  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGltqppawtptqpQGPAAIMEAGTQRYM 296
Cdd:cd08223  111 IAMALQYMHERN---------ILHRDLKTQNIFLTKSNIIKVGDLGIARVLES------------SSDMATTLIGTPYYM 169
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767973831 297 APELL-DKTLDlqdwgmalRRADIYSLALLLWEILS 331
Cdd:cd08223  170 SPELFsNKPYN--------HKSDVWALGCCVYEMAT 197
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
219-408 3.15e-05

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: 45.82  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGTQRYMAP 298
Cdd:cd06642  112 KGLDYLHSER---------KIHRDIKAANVLLSEQGDVKLADFGVAGQL---------TDTQIKRNTFV---GTPFWMAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLDKTLdlQDWgmalrRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTSDelwalavQERRRPYipst 378
Cdd:cd06642  171 EVIKQSA--YDF-----KADIWSLGITAIELAKGEP---PNSDLHPMRVLFLIPKNSPPTLE-------GQHSKPF---- 229
                        170       180       190
                 ....*....|....*....|....*....|
gi 767973831 379 wrcfatdpdglRELLEDCWDADPEARLTAE 408
Cdd:cd06642  230 -----------KEFVEACLNKDPRFRPTAK 248
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
114-334 3.27e-05

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: 45.42  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKA--FPPRS------VAQFQAERALyeLPGLQHDHIVRFITASRGGPGRLLSgplLVLELHPkdcvclcprGRA 185
Cdd:cd06652   27 GRELAVKQvqFDPESpetskeVNALECEIQL--LKNLLHERIVQYYGCLRDPQERTLS---IFMEYMP---------GGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 186 PHNSLCPIGSLCHYLTQytsdwgsslRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAL 265
Cdd:cd06652   93 IKDQLKSYGALTENVTR---------KYTRQILEGVHYLHSNM---------IVHRDIKGANILRDSVGNVKLGDFGASK 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 266 VLPGLTQppawtptqpQGPAAIMEAGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSRCP 334
Cdd:cd06652  155 RLQTICL---------SGTGMKSVTGTPYWMSPEVISG----EGYG---RKADIWSVGCTVVEMLTEKP 207
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
215-408 3.27e-05

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 45.91  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlPGLTQPPAWTPTQPQGPAAIMEAGTQR 294
Cdd:PTZ00024 126 LQILNGLNVLH---------KWYFMHRDLSPANIFINSKGICKIADFGLA---RRYGYPPYSDTLSKDETMQRREEMTSK 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 295 -----YMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPdLRPDSSPPPfQLAYEAELGNTPTSDElWALAVqe 369
Cdd:PTZ00024 194 vvtlwYRAPELL---MGAEKYHFAV---DMWSVGCIFAELLTGKP-LFPGENEID-QLGRIFELLGTPNEDN-WPQAK-- 262
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767973831 370 rrrpYIPSTWRCFATDPDGLRELL----EDCWD-------ADPEARLTAE 408
Cdd:PTZ00024 263 ----KLPLYTEFTPRKPKDLKTIFpnasDDAIDllqsllkLNPLERISAK 308
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
114-408 3.67e-05

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: 45.42  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFP--------PRSVAQFQAERALyeLPGLQHDHIVRFITASRGgPGRLLsgplLVLELHPkdcvclcprGRA 185
Cdd:cd06625   25 GRELAVKQVEidpinteaSKEVKALECEIQL--LKNLQHERIVQYYGCLQD-EKSLS----IFMEYMP---------GGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 186 PHNSLCPIGSLCHYLT-QYTsdwgsslRMALslaQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 264
Cdd:cd06625   89 VKDEIKAYGALTENVTrKYT-------RQIL---EGLAYLHSNM---------IVHRDIKGANILRDSNGNVKLGDFGAS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 265 LVLPgltqppawTPTQPQGPAAIMeaGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSrcpdlrpdSSPPP 344
Cdd:cd06625  150 KRLQ--------TICSSTGMKSVT--GTPYWMSPEVING----EGYG---RKADIWSVGCTVVEMLT--------TKPPW 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 345 FQLAYEAELGNTPTsdelwalavqERRRPYIPSTwrcfaTDPDgLRELLEDCWDADPEARLTAE 408
Cdd:cd06625  205 AEFEPMAAIFKIAT----------QPTNPQLPPH-----VSED-ARDFLSLIFVRNKKQRPSAE 252
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
217-420 3.72e-05

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: 45.54  E-value: 3.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTqPPA--WTPTqpqgpaaimeAGTQR 294
Cdd:cd07859  112 LLRALKYIHTA---------NVFHRDLKPKNILANADCKLKICDFGLARVAFNDT-PTAifWTDY----------VATRW 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 295 YMAPELLDKTldlqdWGMALRRADIYSLALLLWEILSRCPdLRPDSSpPPFQLAYEAELGNTPTSDELWALAVQERRR-- 372
Cdd:cd07859  172 YRAPELCGSF-----FSKYTPAIDIWSIGCIFAEVLTGKP-LFPGKN-VVHQLDLITDLLGTPSPETISRVRNEKARRyl 244
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767973831 373 ------PYIPSTWRCFATDPDGLReLLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07859  245 ssmrkkQPVPFSQKFPNADPLALR-LLERLLAFDPKDRPTAE------EALADP 291
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
219-420 3.73e-05

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: 45.49  E-value: 3.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpGLtqpPAWTPTQpqgpaaimEAGTQRYMAP 298
Cdd:cd07861  112 QGILFCHSRR---------VLHRDLKPQNLLIDNKGVIKLADFGLARAF-GI---PVRVYTH--------EVVTLWYRAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTsDELWALAVQerrRPYIPST 378
Cdd:cd07861  171 EVL---LGSPRYSTPV---DIWSIGTIFAEMATKKPLFHGDSEID--QLFRIFRILGTPT-EDIWPGVTS---LPDYKNT 238
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767973831 379 WRCFAT----------DPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07861  239 FPKWKKgslrtavknlDEDGL-DLLEKMLIYDPAKRISAK------KALVHP 283
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
237-420 3.94e-05

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 45.40  E-value: 3.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVL---IREDGSCAIGDLGLALVlpgltqppawtptqpQGPAAIMEA--GTQRYMAPELLDKtldlQDWG 311
Cdd:cd14167  121 GIVHRDLKPENLLyysLDEDSKIMISDFGLSKI---------------EGSGSVMSTacGTPGYVAPEVLAQ----KPYS 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 312 MALrraDIYSLALLLWEILSRCPDLRPDSSPPPFQLAYEAELgntptsdelwalavqERRRPYipstWRCFAtdpDGLRE 391
Cdd:cd14167  182 KAV---DCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEY---------------EFDSPY----WDDIS---DSAKD 236
                        170       180
                 ....*....|....*....|....*....
gi 767973831 392 LLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14167  237 FIQHLMEKDPEKRFTCE------QALQHP 259
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
101-416 3.99e-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: 45.34  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 101 EGGHAVVWAG--QLQGKLVAIKAFPPRSV--AQFQAERALYELPGLQHDHIVRF--ITASRggpgrllSGPLLVLELHPK 174
Cdd:cd07870   10 EGSYATVYKGisRINGQLVALKVISMKTEegVPFTAIREASLLKGLKHANIVLLhdIIHTK-------ETLTFVFEYMHT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 175 DcvclcprgraphnslcpigsLCHYLTQYTSDWGS-SLRMAL-SLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIRE 252
Cdd:cd07870   83 D--------------------LAQYMIQHPGGLHPyNVRLFMfQLLRGLAYIHGQH---------ILHRDLKPQNLLISY 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 253 DGSCAIGDLGLALVLPgltqppawTPTQPQGPaaimEAGTQRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSR 332
Cdd:cd07870  134 LGELKLADFGLARAKS--------IPSQTYSS----EVVTLWYRPPDVL---LGATDYSSAL---DIWGAGCIFIEMLQG 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 333 CPdLRPDSSPPPFQLAYEAELGNTPTSDELWALAVQERRRPyipsTWRCFATDPdglreLLEDCWDADPEARLTAECVQQ 412
Cdd:cd07870  196 QP-AFPGVSDVFEQLEKIWTVLGVPTEDTWPGVSKLPNYKP----EWFLPCKPQ-----QLRVVWKRLSRPPKAEDLASQ 265

                 ....
gi 767973831 413 RLAA 416
Cdd:cd07870  266 MLMM 269
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
117-408 4.04e-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: 44.97  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 117 VAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVR---------FItasrggpgrllsgpLLVLELhpkdcvclcprgr 184
Cdd:cd14121   24 VAVKCVSKSSLNKASTENLLTEielLKKLKHPHIVElkdfqwdeeHI--------------YLIMEY------------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 185 aphnslCPIGSLCHYLTQYTSDWGSSLRMALS-LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI--REDGSCAIGDL 261
Cdd:cd14121   77 ------CSGGDLSRFIRSRRTLPESTVRRFLQqLASALQFLREH---------NISHMDLKPQNLLLssRYNPVLKLADF 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 262 GLAlvlpgltqppawtptQPQGPAAIMEA--GTQRYMAPE-LLDKTLDlqdwgmalRRADIYSLALLLWEILsrcpdlrp 338
Cdd:cd14121  142 GFA---------------QHLKPNDEAHSlrGSPLYMAPEmILKKKYD--------ARVDLWSVGVILYECL-------- 190
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 339 dSSPPPFQLAYEAELgntptsdelwALAVQERRRPYIPSTWRCFATDPDGLRELLEdcwdADPEARLTAE 408
Cdd:cd14121  191 -FGRAPFASRSFEEL----------EEKIRSSKPIEIPTRPELSADCRDLLLRLLQ----RDPDRRISFE 245
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
192-413 4.14e-05

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 45.20  E-value: 4.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 192 PIGSLCHYLTQYTS----DWGSSLRMALSLAQGLAFLHeerwqngQYKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVL 267
Cdd:cd14159   75 PNGSLEDRLHCQVScpclSWSQRLHVLLGTARAIQYLH-------SDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFS 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 268 -----PGLTQPPAWTPTQpqgpaaimeAGTQRYMAPELLdKTLDLqdwGMALrraDIYSLALLLWEILSRCPDLRPDSSP 342
Cdd:cd14159  148 rrpkqPGMSSTLARTQTV---------RGTLAYLPEEYV-KTGTL---SVEI---DVYSFGVVLLELLTGRRAMEVDSCS 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 343 PPFQL----AYEAELGNTPT----SDELWALAVQER--RRPYIPSTWRCfatDPDGLRELledcwdadpeARLTAECVQQ 412
Cdd:cd14159  212 PTKYLkdlvKEEEEAQHTPTtmthSAEAQAAQLATSicQKHLDPQAGPC---PPELGIEI----------SQLACRCLHR 278

                 .
gi 767973831 413 R 413
Cdd:cd14159  279 R 279
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
219-322 4.57e-05

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: 44.95  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIME--AGTQRYM 296
Cdd:cd06612  110 KGLEYLHSNK---------KIHRDIKAGNILLNEEGQAKLADFGVS--------------GQLTDTMAKRNtvIGTPFWM 166
                         90       100
                 ....*....|....*....|....*..
gi 767973831 297 APELLDKT-LDlqdwgmalRRADIYSL 322
Cdd:cd06612  167 APEVIQEIgYN--------NKADIWSL 185
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
216-460 4.57e-05

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: 45.36  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 216 SLAQGLAFLHeerWQngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGTQRY 295
Cdd:cd06659  125 AVLQALAYLH---SQ------GVIHRDIKSDSILLTLDGRVKLSDFGFCAQI---------SKDVPKRKSLV---GTPYW 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 296 MAPELLDKTLdlqdWGMALrraDIYSLALLLWEILsrcpdlrpDSSPPPFQlayeaelgNTPTSdelwalaVQERRRPYI 375
Cdd:cd06659  184 MAPEVISRCP----YGTEV---DIWSLGIMVIEMV--------DGEPPYFS--------DSPVQ-------AMKRLRDSP 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 376 PSTWRCFATDPDGLRELLEDCWDADPEARLTAECVQQrlaalahpqesHPFPESCprGCPplcpeDCTsipAPTILPCRP 455
Cdd:cd06659  234 PPKLKNSHKASPVLRDFLERMLVRDPQERATAQELLD-----------HPFLLQT--GLP-----ECL---VPLIQQYRK 292

                 ....*
gi 767973831 456 QRSAC 460
Cdd:cd06659  293 RTSTC 297
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
217-408 4.93e-05

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 45.06  E-value: 4.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGTQRYM 296
Cdd:cd06641  110 ILKGLDYLHSEK---------KIHRDIKAANVLLSEHGEVKLADFGVAGQL---------TDTQIKRN*FV---GTPFWM 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLDKTldlqdwgMALRRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTSDELWAlavqerrrpyip 376
Cdd:cd06641  169 APEVIKQS-------AYDSKADIWSLGITAIELARGEP---PHSELHPMKVLFLIPKNNPPTLEGNYS------------ 226
                        170       180       190
                 ....*....|....*....|....*....|..
gi 767973831 377 stwrcfatdpDGLRELLEDCWDADPEARLTAE 408
Cdd:cd06641  227 ----------KPLKEFVEACLNKEPSFRPTAK 248
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
197-342 4.94e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 45.25  E-value: 4.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 197 CHYLTQYTSDWGSSLRM---ALSLAQ----------GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGL 263
Cdd:PHA03209 133 CMVLPHYSSDLYTYLTKrsrPLPIDQaliiekqileGLRYLHAQR---------IIHRDVKTENIFINDVDQVCIGDLGA 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 264 AlvlpgltQPPAwtptqpQGPAAIMEAGTQRYMAPELLDKtlDLQDwgmalRRADIYSLALLLWEILSRCPDL--RPDSS 341
Cdd:PHA03209 204 A-------QFPV------VAPAFLGLAGTVETNAPEVLAR--DKYN-----SKADIWSAGIVLFEMLAYPSTIfeDPPST 263

                 .
gi 767973831 342 P 342
Cdd:PHA03209 264 P 264
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
221-353 6.15e-05

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 44.79  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 221 LAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL--VLPGLTqppawTPTQpqgpaaimeAGTQRYMAP 298
Cdd:cd05591  109 LMFLHRH---------GVIYRDLKLDNILLDAEGHCKLADFGMCKegILNGKT-----TTTF---------CGTPDYIAP 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 299 ELLDKtldlQDWGMALrraDIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAEL 353
Cdd:cd05591  166 EILQE----LEYGPSV---DWWALGVLMYEMM---------AGQPPFEADNEDDL 204
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
213-404 6.18e-05

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 44.86  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTpTQPQGPAAImeagt 292
Cdd:cd05065  111 MLRGIAAGMKYLSEMNY---------VHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYT-SSLGGKIPI----- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 293 qRYMAPElldktldlqdwGMALRR----ADIYSLALLLWEILSrcpdlrpdsspppfqlayeaeLGNTP---TSDELWAL 365
Cdd:cd05065  176 -RWTAPE-----------AIAYRKftsaSDVWSYGIVMWEVMS---------------------YGERPywdMSNQDVIN 222
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767973831 366 AVQERRRpyIPSTWRCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd05065  223 AIEQDYR--LPPPMDC----PTALHQLMLDCWQKDRNLR 255
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
217-334 6.39e-05

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: 44.57  E-value: 6.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIME--AGTQR 294
Cdd:cd14199  135 LIKGIEYLHYQK---------IIHRDVKPSNLLVGEDGHIKIADFGVS--------------NEFEGSDALLTntVGTPA 191
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767973831 295 YMAPELLDKTLDLqdwgMALRRADIYSLALLLW-EILSRCP 334
Cdd:cd14199  192 FMAPETLSETRKI----FSGKALDVWAMGVTLYcFVFGQCP 228
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
219-420 6.65e-05

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: 45.03  E-value: 6.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEerwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppAWTPTQPQGPAAimeagTQRYMAP 298
Cdd:cd07877  131 RGLKYIHS---------ADIIHRDLKPSNLAVNEDCELKILDFGLA----------RHTDDEMTGYVA-----TRWYRAP 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELldktldLQDWGMALRRADIYSLALLLWEILSRcPDLRPDSSPPPfQLAYEAELGNTPTSDELWALAVQERRR-----P 373
Cdd:cd07877  187 EI------MLNWMHYNQTVDIWSVGCIMAELLTG-RTLFPGTDHID-QLKLILRLVGTPGAELLKKISSESARNyiqslT 258
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767973831 374 YIPStwRCFA-----TDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07877  259 QMPK--MNFAnvfigANPLAV-DLLEKMLVLDSDKRITAA------QALAHA 301
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
103-301 7.09e-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: 44.75  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 103 GHAVVWAGQLQGKLVAIKAFPPR-SVAQFQAERALYE---LPGLQHDHIVRFITASRG----GPGRLlsgPLLVLELhpk 174
Cdd:cd13989    7 GYVTLWKHQDTGEYVAIKKCRQElSPSDKNRERWCLEvqiMKKLNHPNVVSARDVPPEleklSPNDL---PLLAMEY--- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 175 dcvclcprgraphnslCPIGSLCHYLTQYTSDWG---SSLRMALS-LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLI 250
Cdd:cd13989   81 ----------------CSGGDLRKVLNQPENCCGlkeSEVRTLLSdISSAISYLHENR---------IIHRDLKPENIVL 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767973831 251 REDGSCAIG---DLGLALVLpgltqppawtptqPQGPAAIMEAGTQRYMAPELL 301
Cdd:cd13989  136 QQGGGRVIYkliDLGYAKEL-------------DQGSLCTSFVGTLQYLAPELF 176
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
190-331 7.45e-05

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. 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: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 44.63  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 267
Cdd:cd05108   89 LMPFGCLLDYVREHKDNIGSQylLNWCVQIAKGMNYLEDRR---------LVHRDLAARNVLVKTPQHVKITDFGLAKLL 159
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 268 PGltQPPAWTPTQPQGPAaimeagtqRYMAPE-LLDKTLDLQdwgmalrrADIYSLALLLWEILS 331
Cdd:cd05108  160 GA--EEKEYHAEGGKVPI--------KWMALEsILHRIYTHQ--------SDVWSYGVTVWELMT 206
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
114-420 8.05e-05

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: 44.44  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 114 GKLVAIKAFPPRSVAQFQAERALYELPGLQ----HDHIVRFI----TASRGGPgrLLsgpLLVLELHPKDCVCLCPR-GR 184
Cdd:cd07837   26 GKLVALKKTRLEMEEEGVPSTALREVSLLQmlsqSIYIVRLLdvehVEENGKP--LL---YLVFEYLDTDLKKFIDSyGR 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 185 APHNSLcPIGSLCHYLTQytsdwgsslrmalsLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLI-REDGSCAIGDLGL 263
Cdd:cd07837  101 GPHNPL-PAKTIQSFMYQ--------------LCKGVAHCH---------SHGVMHRDLKPQNLLVdKQKGLLKIADLGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 264 --ALVLPgltqPPAWTptqpqgpaaiMEAGTQRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPDLRPDSS 341
Cdd:cd07837  157 grAFTIP----IKSYT----------HEIVTLWYRAPEVL---LGSTHYSTPV---DMWSVGCIFAEMSRKQPLFPGDSE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 342 PPpfQLAYEAELGNTPTsDELWAlAVQERRRPYIPSTW------RCFAT-DPDGLrELLEDCWDADPEARLTAEcvqqrl 414
Cdd:cd07837  217 LQ--QLLHIFRLLGTPN-EEVWP-GVSKLRDWHEYPQWkpqdlsRAVPDlEPEGV-DLLTKMLAYDPAKRISAK------ 285

                 ....*.
gi 767973831 415 AALAHP 420
Cdd:cd07837  286 AALQHP 291
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
191-330 8.06e-05

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: 44.23  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYLTQYTSDWGSSLRMAL-SLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpg 269
Cdd:cd14188   83 CSRRSMAHILKARKVLTEPEVRYYLrQIVSGLKYLHEQE---------ILHRDLKLGNFFINENMELKVGDFGLAARL-- 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973831 270 ltqppawtptQPQGPAAIMEAGTQRYMAPELLDKtldlQDWGMalrRADIYSLALLLWEIL 330
Cdd:cd14188  152 ----------EPLEHRRRTICGTPNYLSPEVLNK----QGHGC---ESDIWALGCVMYTML 195
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
94-404 8.36e-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: 44.34  E-value: 8.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  94 ECEQVIREGGHAVVWAGQLQ--GKLVAIKAFPPRSVAQFQAERALYE---LPGLQHDHIVRFITASRggPGRLLSgplLV 168
Cdd:cd08220    3 EKIRVVGRGAYGTVYLCRRKddNKLVIIKQIPVEQMTKEERQAALNEvkvLSMLHHPNIIEYYESFL--EDKALM---IV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 169 LELHPKdcvclcprgraphnslcpiGSLCHYLTQYTSDWGSS---LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSS 245
Cdd:cd08220   78 MEYAPG-------------------GTLFEYIQQRKGSLLSEeeiLHFFVQILLALHHVHSKQ---------ILHRDLKT 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 246 QNVLI-REDGSCAIGDLGLALVLPglTQPPAWTPTqpqgpaaimeaGTQRYMAPELLDKTLDLQdwgmalrRADIYSLAL 324
Cdd:cd08220  130 QNILLnKKRTVVKIGDFGISKILS--SKSKAYTVV-----------GTPCYISPELCEGKPYNQ-------KSDIWALGC 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 325 LLWEILSrcpdlrpdsspppFQLAYEAElgNTPtsdelwALAVQERRRPYIPSTWRcFATDpdgLRELLEDCWDADPEAR 404
Cdd:cd08220  190 VLYELAS-------------LKRAFEAA--NLP------ALVLKIMRGTFAPISDR-YSEE---LRHLILSMLHLDPNKR 244
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
191-344 8.45e-05

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 44.32  E-value: 8.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 191 CPIGSLCHYLTQ--YTSDWGSSLRMALSLAQGLAFLHEerwqngqykPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLP 268
Cdd:cd14043   78 CSRGSLEDLLRNddMKLDWMFKSSLLLDLIKGMRYLHH---------RGIVHGRLKSRNCVVDGRFVLKITDYGYNEILE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 269 GLTQPPAwtPTQPQgpaaimeagTQRYMAPELLDktlDLQDWGMALRRADIYSLALLLWEILSRCP-----DLRPD---- 339
Cdd:cd14043  149 AQNLPLP--EPAPE---------ELLWTAPELLR---DPRLERRGTFPGDVFSFAIIMQEVIVRGApycmlGLSPEeiie 214

                 ....*..
gi 767973831 340 --SSPPP 344
Cdd:cd14043  215 kvRSPPP 221
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
217-334 8.54e-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: 44.27  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptqpQGPAAIME--AGTQR 294
Cdd:cd14118  124 IVLGIEYLHYQ---------KIIHRDIKPSNLLLGDDGHVKIADFGVSNEF--------------EGDDALLSstAGTPA 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767973831 295 YMAPELLDKTLDLQDwGMALrraDIYSLALLLWE-ILSRCP 334
Cdd:cd14118  181 FMAPEALSESRKKFS-GKAL---DIWAMGVTLYCfVFGRCP 217
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
217-420 8.89e-05

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: 44.45  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgLTQPPaWTPTqpqgpaaimeAGTQRYM 296
Cdd:cd07830  108 ILQGLAHIH---------KHGFFHRDLKPENLLVSGPEVVKIADFGLAREI--RSRPP-YTDY----------VSTRWYR 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLdktldlqdwgmaLRRA------DIYSLALLLWEILSrcpdLRpdsspPPFQLAYEAE--------LGnTPTSDEl 362
Cdd:cd07830  166 APEIL------------LRSTsysspvDIWALGCIMAELYT----LR-----PLFPGSSEIDqlykicsvLG-TPTKQD- 222
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 363 W----ALAVQ-ERRRPYIPST--WRCFATDPDGLRELLEDCWDADPEARLTAecvQQrlaALAHP 420
Cdd:cd07830  223 WpegyKLASKlGFRFPQFAPTslHQLIPNASPEAIDLIKDMLRWDPKKRPTA---SQ---ALQHP 281
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
215-420 9.72e-05

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 44.14  E-value: 9.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAQGLAFLHEeRWqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA----LVLPGLTQPPAwtptqpqgpaaimea 290
Cdd:cd07843  113 LQLLSGVAHLHD-NW--------ILHRDLKTSNLLLNNRGILKICDFGLAreygSPLKPYTQLVV--------------- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 291 gTQRYMAPELLdktLDLQDWGMALrraDIYSLALLLWEILSRCPdLRPDSSPPPfQLAYEAELGNTPTsDELW------- 363
Cdd:cd07843  169 -TLWYRAPELL---LGAKEYSTAI---DMWSVGCIFAELLTKKP-LFPGKSEID-QLNKIFKLLGTPT-EKIWpgfselp 238
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 364 -ALAVQERRRPY--IPSTWRCFATDPDGLrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07843  239 gAKKKTFTKYPYnqLRKKFPALSLSDNGF-DLLNRLLTYDPAKRISAE------DALKHP 291
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
219-346 1.01e-04

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: 44.15  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawTPTQPQGPAAIMEAGTQRYMAP 298
Cdd:cd14187  118 LGCQYLHRNR---------VIHRDLKLGNLFLNDDMEVKIGDFGLA------------TKVEYDGERKKTLCGTPNYIAP 176
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767973831 299 ELLDKTldlqdwGMALrRADIYSLALLLWEILsrcpdlrpdSSPPPFQ 346
Cdd:cd14187  177 EVLSKK------GHSF-EVDIWSIGCIMYTLL---------VGKPPFE 208
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
194-334 1.11e-04

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: 44.14  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLT-QYTSDWGSSLRMALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltq 272
Cdd:cd14182   95 GELFDYLTeKVTLSEKETRKIMRALLEVICALH---------KLNIVHRDLKPENILLDDDMNIKLTDFGFSCQL----- 160
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973831 273 ppawtptqPQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMAlRRADIYSLALLLWEILSRCP 334
Cdd:cd14182  161 --------DPGEKLREVCGTPGYLAPEIIECSMDDNHPGYG-KEVDMWSTGVIMYTLLAGSP 213
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
98-350 1.18e-04

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: 43.84  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831  98 VIREGGHAVVWAGQLQGKL---VAIKAFPPRSVAQFQA--ERALYELPGLQHDHIVRFITASRggpgrLLSGPLLVLELh 172
Cdd:cd14201   13 LVGHGAFAVVFKGRHRKKTdweVAIKSINKKNLSKSQIllGKEIKILKELQHENIVALYDVQE-----MPNSVFLVMEY- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 173 pkdcvclcprgraphnslCPIGSLCHYLTQYTSDWGSSLRMAL-SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI- 250
Cdd:cd14201   87 ------------------CNGGDLADYLQAKGTLSEDTIRVFLqQIAAAMRILHSK---------GIIHRDLKPQNILLs 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 251 ---REDGSCA-----IGDLGLALVLpgltqppawtptQPQGPAAIMeAGTQRYMAPE-LLDKTLDlqdwgmalRRADIYS 321
Cdd:cd14201  140 yasRKKSSVSgirikIADFGFARYL------------QSNMMAATL-CGSPMYMAPEvIMSQHYD--------AKADLWS 198
                        250       260
                 ....*....|....*....|....*....
gi 767973831 322 LALLLWEILSRCPDLRPDsSPPPFQLAYE 350
Cdd:cd14201  199 IGTVIYQCLVGKPPFQAN-SPQDLRMFYE 226
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
237-346 1.22e-04

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: 43.75  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQppAWTptqpqgpaaimEAGTQRYMAPE-LLDKTLDlqdwgmalR 315
Cdd:cd05572  113 GIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRK--TWT-----------FCGTPEYVAPEiILNKGYD--------F 171
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767973831 316 RADIYSLALLLWEILsrcpdlrpdSSPPPFQ 346
Cdd:cd05572  172 SVDYWSLGILLYELL---------TGRPPFG 193
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
237-420 1.23e-04

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: 43.97  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIRE-DGSCAIGDLGLA--------------LVLPGLTQPPAWT-PTQ-PQGPAAIMEAgtqrYMAPE 299
Cdd:cd14013  140 GIVHRDVKPQNIIVSEgDGQFKIIDLGAAadlriginyipkefLLDPRYAPPEQYImSTQtPSAPPAPVAA----ALSPV 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 300 LldktldlqdWGMAL-RRADIYSLALLLweiLSRC-PDLRPDSSPPPFQLAYEAelgntpTSDELWALAVQERRRPYIPS 377
Cdd:cd14013  216 L---------WQMNLpDRFDMYSAGVIL---LQMAfPNLRSDSNLIAFNRQLKQ------CDYDLNAWRMLVEPRASADL 277
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 767973831 378 TWRCFATDPDGLR--ELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14013  278 REGFEILDLDDGAgwDLVTKLIRYKPRGRLSAS------AALAHP 316
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
216-420 1.31e-04

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: 43.36  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 216 SLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLI-REDGSCAIGDLGLAlvlpgltqppAWTPTQPQGPAAimEAGTQR 294
Cdd:cd14019  109 NLFKALKHVHSF---------GIIHRDVKPGNFLYnRETGKGVLVDFGLA----------QREEDRPEQRAP--RAGTRG 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 295 YMAPELLDKTldlQDWGMALrraDIYSLALLLWEILSRCpdlrpdssPPPFQLAYE----AELGNTPTSDELWalavqer 370
Cdd:cd14019  168 FRAPEVLFKC---PHQTTAI---DIWSAGVILLSILSGR--------FPFFFSSDDidalAEIATIFGSDEAY------- 226
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767973831 371 rrpyipstwrcfatdpdglrELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14019  227 --------------------DLLDKLLELDPSKRITAE------EALKHP 250
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
219-426 1.32e-04

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: 43.86  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqpPAWTPTQPQGPAAImeaGTQRYMAP 298
Cdd:cd06643  114 EALVYLHENK---------IIHRDLKAGNILFTLDGDIKLADFGVS---------AKNTRTLQRRDSFI---GTPYWMAP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELL------DKTLDLqdwgmalrRADIYSLALLLWEILSRCPdlrPDSSPPPFQLAYEAELGNTPTSDElwalavqerrr 372
Cdd:cd06643  173 EVVmcetskDRPYDY--------KADVWSLGVTLIEMAQIEP---PHHELNPMRVLLKIAKSEPPTLAQ----------- 230
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767973831 373 pyiPSTWrcfatDPDgLRELLEDCWDADPEARLTAECVQQrlaalahpqesHPF 426
Cdd:cd06643  231 ---PSRW-----SPE-FKDFLRKCLEKNVDARWTTSQLLQ-----------HPF 264
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
215-264 1.32e-04

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: 43.58  E-value: 1.32e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 264
Cdd:cd07839  106 FQLLKGLAFCHSHN---------VLHRDLKPQNLLINKNGELKLADFGLA 146
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
220-406 1.36e-04

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


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 43.78  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIME--AGTQRYMA 297
Cdd:cd14200  136 GIEYLHYQK---------IVHRDIKPSNLLLGDDGHVKIADFGVS--------------NQFEGNDALLSstAGTPAFMA 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 298 PELLDKTldlqDWGMALRRADIYSLALLLW-EILSRCPDLrpdsspPPFQLAYEAELGNTPTSdelwalavqerrrpyIP 376
Cdd:cd14200  193 PETLSDS----GQSFSGKALDVWAMGVTLYcFVYGKCPFI------DEFILALHNKIKNKPVE---------------FP 247
                        170       180       190
                 ....*....|....*....|....*....|
gi 767973831 377 STwrcfATDPDGLRELLEDCWDADPEARLT 406
Cdd:cd14200  248 EE----PEISEELKDLILKMLDKNPETRIT 273
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
192-407 1.47e-04

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: 43.57  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 192 PIGSLCHYLTQYTS-DWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGS-CAIGDLGLALVLPg 269
Cdd:cd06630   86 AGGSVASLLSKYGAfSENVIINYTLQILRGLAYLHDNQ---------IIHRDLKGANLLVDSTGQrLRIADFGAAARLA- 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 270 lTQPPAWTPTQPQgpaaimEAGTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILSRCPDLRPDSSPPPFQLAY 349
Cdd:cd06630  156 -SKGTGAGEFQGQ------LLGTIAFMAPEVLRG----EQYG---RSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIF 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 350 EAELGNTPtsdelwalavqerrrPYIPSTWRcfatdpDGLRELLEDCWDADPEARLTA 407
Cdd:cd06630  222 KIASATTP---------------PPIPEHLS------PGLRDVTLRCLELQPEDRPPA 258
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
212-406 1.48e-04

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 43.68  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIMEAG 291
Cdd:cd06622  106 RITYAVVKGLKFLKEEH--------NIIHRDVKPTNVLVNGNGQVKLCDFGVS--------------GNLVASLAKTNIG 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 292 TQRYMAPELLdKTLDLQDWGMALRRADIYSLALLLWEILSRCPDLRPDSSPPPF-QLAyeaelgntptsdelwalAVQER 370
Cdd:cd06622  164 CQSYMAPERI-KSGGPNQNPTYTVQSDVWSLGLSILEMALGRYPYPPETYANIFaQLS-----------------AIVDG 225
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767973831 371 RRPYIPSTWRCFATDpdglreLLEDCWDADPEARLT 406
Cdd:cd06622  226 DPPTLPSGYSDDAQD------FVAKCLNKIPNRRPT 255
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
213-420 1.51e-04

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: 43.48  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTqppawtptqpqgpAAIMEAGT 292
Cdd:cd07862  115 MMFQLLRGLDFLHSHR---------VVHRDLKPQNILVTSSGQIKLADFGLARIYSFQM-------------ALTSVVVT 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 293 QRYMAPELLdktldLQDwgMALRRADIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPtSDELWALAVQERRR 372
Cdd:cd07862  173 LWYRAPEVL-----LQS--SYATPVDLWSVGCIFAEMFRRKPLFRGSSDVD--QLGKILDVIGLP-GEEDWPRDVALPRQ 242
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767973831 373 PYIPSTWRC---FATDPDGL-RELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07862  243 AFHSKSAQPiekFVTDIDELgKDLLLKCLTFNPAKRISAY------SALSHP 288
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
237-420 1.63e-04

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: 43.34  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIR---EDGSCAIGDLGLALVlpgltqppawtptQPQGPAAiMEAGTQRYMAPELLDKtldlQDWGMA 313
Cdd:cd14169  121 GIVHRDLKPENLLYAtpfEDSKIMISDFGLSKI-------------EAQGMLS-TACGTPGYVAPELLEQ----KPYGKA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 314 LrraDIYSLALLLWEILSRCPDLRPDSSPPPFQLAYEAELgntptsdelwalavqERRRPYipstWRCFA-TDPDGLREL 392
Cdd:cd14169  183 V---DVWAIGVISYILLCGYPPFYDENDSELFNQILKAEY---------------EFDSPY----WDDISeSAKDFIRHL 240
                        170       180
                 ....*....|....*....|....*...
gi 767973831 393 LEdcwdADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14169  241 LE----RDPEKRFTCE------QALQHP 258
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
220-350 1.81e-04

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: 43.04  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgLTQPPAWTPTQpqgpaaimeAGTQRYMAPE 299
Cdd:cd08219  112 GVQHIHEKR---------VLHRDIKSKNIFLTQNGKVKLGDFGSARL---LTSPGAYACTY---------VGTPYYVPPE 170
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973831 300 LLDkTLDLQDwgmalrRADIYSLALLLWEILSRCPDLRPDS-------------SPPPFQLAYE 350
Cdd:cd08219  171 IWE-NMPYNN------KSDIWSLGCILYELCTLKHPFQANSwknlilkvcqgsyKPLPSHYSYE 227
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
190-267 1.85e-04

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which 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, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 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: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 43.47  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 190 LCPIGSLCHYLTQYTSDWGSS--LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVL 267
Cdd:cd05109   89 LMPYGCLLDYVRENKDRIGSQdlLNWCVQIAKGMSYLEEVR---------LVHRDLAARNVLVKSPNHVKITDFGLARLL 159
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
217-420 1.97e-04

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: 43.41  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgLTQPPAWTPTqpqgpaaimeAGTQRYM 296
Cdd:cd07863  117 FLRGLDFLHANC---------IVHRDLKPENILVTSGGQVKLADFGLARI---YSCQMALTPV----------VVTLWYR 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELLdktldLQDwgMALRRADIYSLALLLWEILSRCPDLRPDSSPPpfQLAYEAELGNTPTSDElWALAVQERRRPYIP 376
Cdd:cd07863  175 APEVL-----LQS--TYATPVDMWSVGCIFAEMFRRKPLFCGNSEAD--QLGKIFDLIGLPPEDD-WPRDVTLPRGAFSP 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767973831 377 STWR----CFATDPDGLRELLEDCWDADPEARLTAecvqqrLAALAHP 420
Cdd:cd07863  245 RGPRpvqsVVPEIEESGAQLLLEMLTFNPHKRISA------FRALQHP 286
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
217-420 2.12e-04

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: 43.01  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDG----SCAIGDLGLALVL---PGLTQPPAWTPTqpqgpaaime 289
Cdd:cd14091  103 LTKTVEYLHSQ---------GVVHRDLKPSNILYADESgdpeSLRICDFGFAKQLraeNGLLMTPCYTAN---------- 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 290 agtqrYMAPELLDKtldlQDWGMAlrrADIYSLALLLWEILSRCpdlrpdsspPPFqlAYeaelGNTPTSDELWAlAVQE 369
Cdd:cd14091  164 -----FVAPEVLKK----QGYDAA---CDIWSLGVLLYTMLAGY---------TPF--AS----GPNDTPEVILA-RIGS 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767973831 370 RRRPYIPSTWrcfATDPDGLRELLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14091  216 GKIDLSGGNW---DHVSDSAKDLVRKMLHVDPSQRPTAA------QVLQHP 257
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
219-336 2.14e-04

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: 43.09  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptqpqGPAAIMeAGTQRYMAP 298
Cdd:cd06634  126 QGLAYLHSH---------NMIHRDVKAGNILLTEPGLVKLGDFGSASIM---------------APANSF-VGTPYWMAP 180
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767973831 299 ELLDKtldlQDWGMALRRADIYSLALLLWEILSRCPDL 336
Cdd:cd06634  181 EVILA----MDEGQYDGKVDVWSLGITCIELAERKPPL 214
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
175-330 2.24e-04

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: 43.51  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 175 DC---VCLCPRGRAPhNSLCPI------GSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHEERwqngqykpgIAHRDLS 244
Cdd:cd05633   66 DCpfiVCMTYAFHTP-DKLCFIldlmngGDLHYHLSQHGVFSEKEMRFyATEIILGLEHMHNRF---------VVYRDLK 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 245 SQNVLIREDGSCAIGDLGLALvlpgltqppAWTPTQPQGpaaimEAGTQRYMAPELLDKtldlqdwGMAL-RRADIYSLA 323
Cdd:cd05633  136 PANILLDEHGHVRISDLGLAC---------DFSKKKPHA-----SVGTHGYMAPEVLQK-------GTAYdSSADWFSLG 194

                 ....*..
gi 767973831 324 LLLWEIL 330
Cdd:cd05633  195 CMLFKLL 201
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
219-336 2.29e-04

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: 43.10  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgltqppawtptqpQGPAAIMeAGTQRYMAP 298
Cdd:cd06633  132 QGLAYLHSH---------NMIHRDIKAGNILLTEPGQVKLADFGSASI---------------ASPANSF-VGTPYWMAP 186
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767973831 299 ELLDKtldlQDWGMALRRADIYSLALLLWEILSRCPDL 336
Cdd:cd06633  187 EVILA----MDEGQYDGKVDIWSLGITCIELAERKPPL 220
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
211-417 2.65e-04

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: 42.67  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEERwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLA----LVLPGLTQPPAWtptqpQGPAA 286
Cdd:cd13986  109 LHIFLGICRGLKAMHEPE------LVPYAHRDIKPGNVLLSEDDEPILMDLGSMnparIEIEGRREALAL-----QDWAA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 287 imEAGTQRYMAPELLD----KTLDlqdwgmalRRADIYSLALLLWEILSrcpdlrpDSSPppfqlaYEAELGntpTSDEL 362
Cdd:cd13986  178 --EHCTMPYRAPELFDvkshCTID--------EKTDIWSLGCTLYALMY-------GESP------FERIFQ---KGDSL 231
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767973831 363 wALAVQERR-RPYIPSTWrcfatdPDGLRELLEDCWDADPEARLTAECVQQRLAAL 417
Cdd:cd13986  232 -ALAVLSGNySFPDNSRY------SEELHQLVKSMLVVNPAERPSIDDLLSRVHDL 280
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
194-330 3.33e-04

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


Pssm-ID: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 42.42  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALvlpgltq 272
Cdd:cd05606   83 GDLHYHLSQHGVFSEAEMRFyAAEVILGLEHMHNR---------FIVYRDLKPANILLDEHGHVRISDLGLAC------- 146
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 273 ppAWTPTQPQgpAAImeaGTQRYMAPELLDKtldlqdwGMAL-RRADIYSLALLLWEIL 330
Cdd:cd05606  147 --DFSKKKPH--ASV---GTHGYMAPEVLQK-------GVAYdSSADWFSLGCMLYKLL 191
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
217-331 3.36e-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: 42.77  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawTPTQPQGPAAIMEAGTQRYM 296
Cdd:cd05582  106 LALALDHLH---------SLGIIYRDLKPENILLDEDGHIKLTDFGLS------------KESIDHEKKAYSFCGTVEYM 164
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767973831 297 APELLDKtldlQDWGMAlrrADIYSLALLLWEILS 331
Cdd:cd05582  165 APEVVNR----RGHTQS---ADWWSFGVLMFEMLT 192
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
213-337 3.72e-04

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: 42.29  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIRE--DGSCAI--GDLGLALVLPGltqpPAWTPtqpqgpaaim 288
Cdd:cd14183  109 MLYNLASAIKYLHSL---------NIVHRDIKPENLLVYEhqDGSKSLklGDFGLATVVDG----PLYTV---------- 165
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767973831 289 eAGTQRYMAPELLDKTldlqdwGMALrRADIYSLALLLWEILSRCPDLR 337
Cdd:cd14183  166 -CGTPTYVAPEIIAET------GYGL-KVDIWAAGVITYILLCGFPPFR 206
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
214-353 4.13e-04

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 42.29  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltQPPAWtptqpQGPAAIMEAGTQ 293
Cdd:cd05616  107 AAEIAIGLFFLQSK---------GIIYRDLKLDNVMLDSEGHIKIADFGMC-------KENIW-----DGVTTKTFCGTP 165
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 294 RYMAPELldktLDLQDWGmalRRADIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAEL 353
Cdd:cd05616  166 DYIAPEI----IAYQPYG---KSVDWWAFGVLLYEML---------AGQAPFEGEDEDEL 209
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
200-264 4.31e-04

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 42.29  E-value: 4.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973831 200 LTQYTSDWGSSLRM------ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLA 264
Cdd:cd07872   90 LKQYMDDCGNIMSMhnvkifLYQILRGLAYCHRRK---------VLHRDLKPQNLLINERGELKLADFGLA 151
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
238-331 4.44e-04

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: 42.11  E-value: 4.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 238 IAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptQPQGPAAIMEAGTQRYMAPELLD-KTLDlqdwgmalRR 316
Cdd:cd08218  122 ILHRDIKSQNIFLTKDGIIKLGDFGIARVL------------NSTVELARTCIGTPYYLSPEICEnKPYN--------NK 181
                         90
                 ....*....|....*
gi 767973831 317 ADIYSLALLLWEILS 331
Cdd:cd08218  182 SDIWALGCVLYEMCT 196
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
194-330 4.53e-04

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: 42.34  E-value: 4.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTQYTSDWGSSLRM-ALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALvlpgltq 272
Cdd:cd14223   88 GDLHYHLSQHGVFSEAEMRFyAAEIILGLEHMHSRF---------VVYRDLKPANILLDEFGHVRISDLGLAC------- 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 273 ppAWTPTQPQGpaaimEAGTQRYMAPELLDKtldlqdwGMAL-RRADIYSLALLLWEIL 330
Cdd:cd14223  152 --DFSKKKPHA-----SVGTHGYMAPEVLQK-------GVAYdSSADWFSLGCMLFKLL 196
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
219-336 5.67e-04

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 41.67  E-value: 5.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLA-LVLPgltqppawtptqpqgpaAIMEAGTQRYMA 297
Cdd:cd06607  112 QGLAYLHSH---------NRIHRDVKAGNILLTEPGTVKLADFGSAsLVCP-----------------ANSFVGTPYWMA 165
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767973831 298 PELLdktLDLqDWGMALRRADIYSLALLLWEILSRCPDL 336
Cdd:cd06607  166 PEVI---LAM-DEGQYDGKVDVWSLGITCIELAERKPPL 200
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
212-329 5.78e-04

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: 41.98  E-value: 5.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpG-LTQPPAWTPTqpqgpaaimeA 290
Cdd:cd06618  118 KMTVSIVKALHYLKE--------KHGVIHRDVKPSNILLDESGNVKLCDFGIS----GrLVDSKAKTRS----------A 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767973831 291 GTQRYMAPELLD-KTLDLQDWgmalrRADIYSLALLLWEI 329
Cdd:cd06618  176 GCAAYMAPERIDpPDNPKYDI-----RADVWSLGISLVEL 210
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
214-353 6.04e-04

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


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 41.91  E-value: 6.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawTPTQPQGPAAIMEAGTQ 293
Cdd:cd05615  117 AAEISVGLFFLH---------KKGIIYRDLKLDNVMLDSEGHIKIADFGMC------------KEHMVEGVTTRTFCGTP 175
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 294 RYMAPELldktLDLQDWGmalRRADIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAEL 353
Cdd:cd05615  176 DYIAPEI----IAYQPYG---RSVDWWAYGVLLYEML---------AGQPPFDGEDEDEL 219
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
211-329 6.20e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 41.90  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPP--AWtptqpqgpaaim 288
Cdd:PHA03212 185 LAIERSVLRAIQYLHENR---------IIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANKyyGW------------ 243
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767973831 289 eAGTQRYMAPELLDKtldlQDWGMALrraDIYSLALLLWEI 329
Cdd:PHA03212 244 -AGTIATNAPELLAR----DPYGPAV---DIWSAGIVLFEM 276
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
237-353 6.21e-04

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 41.65  E-value: 6.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTqppaWTptqpqgpaaimEAGTQRYMAPELldktldLQDWGMAlRR 316
Cdd:cd05612  121 EIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRT----WT-----------LCGTPEYLAPEV------IQSKGHN-KA 178
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767973831 317 ADIYSLALLLWEILSRCPDLRPDSsppPFQLaYEAEL 353
Cdd:cd05612  179 VDWWALGILIYEMLVGYPPFFDDN---PFGI-YEKIL 211
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
215-329 6.37e-04

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: 41.48  E-value: 6.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCA-IGDLGLALVLPGLTQppawtptqpqgpAAIMEAGTQ 293
Cdd:cd08225  108 VQISLGLKHIHDRK---------ILHRDIKSQNIFLSKNGMVAkLGDFGIARQLNDSME------------LAYTCVGTP 166
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767973831 294 RYMAPELL-DKTLDlqdwgmalRRADIYSLALLLWEI 329
Cdd:cd08225  167 YYLSPEICqNRPYN--------NKTDIWSLGCVLYEL 195
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
215-329 6.51e-04

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: 41.55  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQppawtptqpqgpAAIMEAGTQR 294
Cdd:cd08228  113 VQLCSAVEHMHSRR---------VMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTT------------AAHSLVGTPY 171
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767973831 295 YMAPELLDKTldlqdwGMALrRADIYSLALLLWEI 329
Cdd:cd08228  172 YMSPERIHEN------GYNF-KSDIWSLGCLLYEM 199
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
219-408 6.78e-04

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: 41.57  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptqpqGPAAIMeAGTQRYMAP 298
Cdd:cd06635  136 QGLAYLHSHN---------MIHRDIKAGNILLTEPGQVKLADFGSASIA---------------SPANSF-VGTPYWMAP 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLDKtldlQDWGMALRRADIYSLALLLWEILSRcpdlrpdsSPPPFqlayeaelgNTPTSDELWALAVQErrRPYIPST 378
Cdd:cd06635  191 EVILA----MDEGQYDGKVDVWSLGITCIELAER--------KPPLF---------NMNAMSALYHIAQNE--SPTLQSN 247
                        170       180       190
                 ....*....|....*....|....*....|.
gi 767973831 379 -WRcfatdpDGLRELLEDCWDADPEARLTAE 408
Cdd:cd06635  248 eWS------DYFRNFVDSCLQKIPQDRPTSE 272
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
103-342 7.23e-04

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 41.49  E-value: 7.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 103 GHAVVWAGQLQGKLVAIKA----FPPRSVAQFQAERALyeLPGLQHDHIVrfitASRGGPGRLLsgpllvlELHPKDCVC 178
Cdd:cd14038    8 GNVLRWINQETGEQVAIKQcrqeLSPKNRERWCLEIQI--MKRLNHPNVV----AARDVPEGLQ-------KLAPNDLPL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 179 LCprgraphNSLCPIGSLCHYLTQYTSDWG---SSLRMALS-LAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDG 254
Cdd:cd14038   75 LA-------MEYCQGGDLRKYLNQFENCCGlreGAILTLLSdISSALRYLHENR---------IIHRDLKPENIVLQQGE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 255 SCAIG---DLGLALVLPgltqppawtptqpQGPAAIMEAGTQRYMAPELLDKtldlQDWGMALrraDIYSLALLLWEILS 331
Cdd:cd14038  139 QRLIHkiiDLGYAKELD-------------QGSLCTSFVGTLQYLAPELLEQ----QKYTVTV---DYWSFGTLAFECIT 198
                        250
                 ....*....|.
gi 767973831 332 RCPDLRPDSSP 342
Cdd:cd14038  199 GFRPFLPNWQP 209
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
237-420 8.42e-04

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: 41.22  E-value: 8.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIR---EDGSCAIGDLGLALVLpgltqppawtptqpqGPAAIMEA--GTQRYMAPELLdKTLDLQDWG 311
Cdd:cd14084  131 GIIHRDLKPENVLLSsqeEECLIKITDFGLSKIL---------------GETSLMKTlcGTPTYLAPEVL-RSFGTEGYT 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 312 malRRADIYSLALLLWEILSRCpdlrpdsspPPFQLAYEaelgNTPTSDElwalaVQERRRPYIPSTWRCFATDPdglRE 391
Cdd:cd14084  195 ---RAVDCWSLGVILFICLSGY---------PPFSEEYT----QMSLKEQ-----ILSGKYTFIPKAWKNVSEEA---KD 250
                        170       180
                 ....*....|....*....|....*....
gi 767973831 392 LLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd14084  251 LVKKMLVVDPSRRPSIE------EALEHP 273
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
182-414 8.75e-04

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 41.36  E-value: 8.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 182 RGRAPHN--SLCPIGSLCHYLTQYTSDWG--SSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCA 257
Cdd:cd05050  100 RHRSPRAqcSLSHSTSSARKCGLNPLPLSctEQLCIAKQVAAGMAYLSERKF---------VHRDLATRNCLVGENMVVK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 258 IGDLGLALVLpgltqppawtPTQPQGPAAIMEAGTQRYMAPE-LLDKTLDLQdwgmalrrADIYSLALLLWEILSRcpDL 336
Cdd:cd05050  171 IADFGLSRNI----------YSADYYKASENDAIPIRWMPPEsIFYNRYTTE--------SDVWAYGVVLWEIFSY--GM 230
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973831 337 RPDSSPPPFQLAYEAELGNTPTsdelwalavqerrrpyipstwrCFATDPDGLRELLEDCWDADPEARLTAECVQQRL 414
Cdd:cd05050  231 QPYYGMAHEEVIYYVRDGNVLS----------------------CPDNCPLELYNLMRLCWSKLPSDRPSFASINRIL 286
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
204-404 8.90e-04

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 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: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 41.46  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 204 TSDWGSSLRMALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqpPAWTPTQPQG 283
Cdd:cd05096  134 AISYSSLLHVALQIASGMKYLSSLNF---------VHRDLATRNCLVGENLTIKIADFGMSRNL------YAGDYYRIQG 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 284 PAAImeagTQRYMAPELLDKtldlqdwGMALRRADIYSLALLLWEILSRCPDlrpdsspPPFqlayeAELGNTPTSDELW 363
Cdd:cd05096  199 RAVL----PIRWMAWECILM-------GKFTTASDVWAFGVTLWEILMLCKE-------QPY-----GELTDEQVIENAG 255
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 767973831 364 ALAVQERRRPYIPSTWRCfatdPDGLRELLEDCWDADPEAR 404
Cdd:cd05096  256 EFFRDQGRQVYLFRPPPC----PQGLYELMLQCWSRDCRER 292
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
219-408 1.11e-03

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: 40.69  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpGLTQPPAWTptqpqgpaaimEAGTQRYMAP 298
Cdd:cd06609  109 LGLEYLHSEG---------KIHRDIKAANILLSEEGDVKLADFGVSGQL-TSTMSKRNT-----------FVGTPFWMAP 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELLDKT-LDLqdwgmalrRADIYSLALllweilsrcpdlrpdsspppfqLAYEAELGNTPTSD--ELWALAVQERRRPyi 375
Cdd:cd06609  168 EVIKQSgYDE--------KADIWSLGI----------------------TAIELAKGEPPLSDlhPMRVLFLIPKNNP-- 215
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767973831 376 PSTWRCFATDPdgLRELLEDCWDADPEARLTAE 408
Cdd:cd06609  216 PSLEGNKFSKP--FKDFVELCLNKDPKERPSAK 246
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
219-333 1.16e-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: 40.80  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEErwqngqykpGIAHRDLSSQNVL---IREDGSCAIGDLGLALVLpgltqppawtptqpqGPAA-IME-AGTQ 293
Cdd:cd14106  119 EGVQYLHER---------NIVHLDLKPQNILltsEFPLGDIKLCDFGISRVI---------------GEGEeIREiLGTP 174
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767973831 294 RYMAPELLD-KTLDLQdwgmalrrADIYSLALLLWEILSRC 333
Cdd:cd14106  175 DYVAPEILSyEPISLA--------TDMWSIGVLTYVLLTGH 207
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
217-330 1.40e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 40.98  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPP---AWtptqpqgpaaimeAGTQ 293
Cdd:PHA03207 194 LLEALAYLHGR---------GIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDTPqcyGW-------------SGTL 251
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767973831 294 RYMAPELLdkTLDlqdwgMALRRADIYSLALLLWEIL 330
Cdd:PHA03207 252 ETNSPELL--ALD-----PYCAKTDIWSAGLVLFEMS 281
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
219-420 1.43e-03

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: 40.71  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppAWTPTQPQGPAAimeagTQRYMAP 298
Cdd:cd07880  129 KGLKYIH---------AAGIIHRDLKPGNLAVNEDCELKILDFGLA----------RQTDSEMTGYVV-----TRWYRAP 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 299 ELldktldLQDWGMALRRADIYSLALLLWEILSRCPDLRpdSSPPPFQLAYEAELGNTPTSDELWALAVQERRRpYIPST 378
Cdd:cd07880  185 EV------ILNWMHYTQTVDIWSVGCIMAEMLTGKPLFK--GHDHLDQLMEIMKVTGTPSKEFVQKLQSEDAKN-YVKKL 255
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767973831 379 WRCFATD---------PDGLReLLEDCWDADPEARLTAEcvqqrlAALAHP 420
Cdd:cd07880  256 PRFRKKDfrsllpnanPLAVN-VLEKMLVLDAESRITAA------EALAHP 299
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
237-420 1.46e-03

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 40.93  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 237 GIAHRDLSSQNVLIRE-DGSCAIGDLGLA--------------LVLPGLTQPPAW-----TPTQPQGPAAIMeagtqryM 296
Cdd:PLN03225 275 GIVHRDVKPQNIIFSEgSGSFKIIDLGAAadlrvginyipkefLLDPRYAAPEQYimstqTPSAPSAPVATA-------L 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 297 APELldktldlqdWGMAL-RRADIYSLALLLweiLSRC-PDLRPDSSpppfQLAYEAELGNTPTSDELWALAVQERRRPY 374
Cdd:PLN03225 348 SPVL---------WQLNLpDRFDIYSAGLIF---LQMAfPNLRSDSN----LIQFNRQLKRNDYDLVAWRKLVEPRASPD 411
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767973831 375 IPSTWRCFATDPDGLRELLEDCWDADPEARLTAecvqqrLAALAHP 420
Cdd:PLN03225 412 LRRGFEVLDLDGGAGWELLKSMMRFKGRQRISA------KAALAHP 451
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
219-332 1.60e-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: 40.50  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHeerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVlpgltqppawtptQPQGPAAIM--EAGTQRYM 296
Cdd:cd07853  114 RGLKYLH---------SAGILHRDIKPGNLLVNSNCVLKICDFGLARV-------------EEPDESKHMtqEVVTQYYR 171
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767973831 297 APELLdktLDLQDWGMALrraDIYSLALLLWEILSR 332
Cdd:cd07853  172 APEIL---MGSRHYTSAV---DIWSVGCIFAELLGR 201
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
194-411 1.69e-03

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: 40.44  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 194 GSLCHYLTqytSDWGSSLR------MALSLAQGLAFLHEERWqngqykpgiAHRDLSSQNVLIREDGSCAIGDLGLALVL 267
Cdd:cd05071   88 GSLLDFLK---GEMGKYLRlpqlvdMAAQIASGMAYVERMNY---------VHRDLRAANILVGENLVCKVADFGLARLI 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 268 P--------GLTQPPAWTptqpqGPAAIMeagtqrymapelldktldlqdWGMALRRADIYSLALLLWEILSRcpdlrpd 339
Cdd:cd05071  156 EdneytarqGAKFPIKWT-----APEAAL---------------------YGRFTIKSDVWSFGILLTELTTK------- 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973831 340 sspppfqlayeaelGNTPTSDELWALAVQERRRPY-IPSTWRCfatdPDGLRELLEDCWDADPEARLTAECVQ 411
Cdd:cd05071  203 --------------GRVPYPGMVNREVLDQVERGYrMPCPPEC----PESLHDLMCQCWRKEPEERPTFEYLQ 257
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
214-334 1.78e-03

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


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 40.39  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 214 ALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL--VLPGLTqppawTPTQpqgpaaimeAG 291
Cdd:cd05617  122 AAEICIALNFLHER---------GIIYRDLKLDNVLLDADGHIKLTDYGMCKegLGPGDT-----TSTF---------CG 178
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767973831 292 TQRYMAPELLDKtldlQDWGMALrraDIYSLALLLWEILS-RCP 334
Cdd:cd05617  179 TPNYIAPEILRG----EEYGFSV---DWWALGVLMFEMMAgRSP 215
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
205-453 1.82e-03

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: 40.24  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 205 SDWGSSLRMAlSLAQGLAFLHEerwqngqykPGIAHRDLSSQNVLIREDGSCA---IGDLGLALVLPGLTQpPAWTPtqp 281
Cdd:cd14180   99 SESEASQLMR-SLVSAVSFMHE---------AGVVHRDLKPENILYADESDGAvlkVIDFGFARLRPQGSR-PLQTP--- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 282 qgpaaimeAGTQRYMAPELL-DKTLDlqdwgmalRRADIYSLALLLWEILsrcpdlrpdSSPPPFQLAyEAELGNTPTSD 360
Cdd:cd14180  165 --------CFTLQYAAPELFsNQGYD--------ESCDLWSLGVILYTML---------SGQVPFQSK-RGKMFHNHAAD 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 361 ELwaLAVQERRRPYIPSTWRCFATDPdglRELLEDCWDADPEARLtaecvqqRLAALahpQESHPFPESCPRGCPPLCPE 440
Cdd:cd14180  219 IM--HKIKEGDFSLEGEAWKGVSEEA---KDLVRGLLTVDPAKRL-------KLSEL---RESDWLQGGSALSSTPLMTP 283
                        250
                 ....*....|...
gi 767973831 441 DCTSIPAPTILPC 453
Cdd:cd14180  284 DVLESSGPAVRTG 296
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
218-344 1.98e-03

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: 39.98  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 218 AQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGTQRYMA 297
Cdd:cd06608  123 LRGLAYLHENK---------VIHRDIKGQNILLTEEAEVKLVDFGVSAQL---------DSTLGRRNTFI---GTPYWMA 181
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973831 298 PEL------LDKTLDlqdwgmalRRADIYSLALLLWEILSRCP---DLRPD-------SSPPP 344
Cdd:cd06608  182 PEViacdqqPDASYD--------ARCDVWSLGITAIELADGKPplcDMHPMralfkipRNPPP 236
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
220-426 2.07e-03

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 40.10  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL--VLPGLTqppawTPTQpqgpaaimeAGTQRYMA 297
Cdd:cd05588  108 ALNFLHEK---------GIIYRDLKLDNVLLDSEGHIKLTDYGMCKegLRPGDT-----TSTF---------CGTPNYIA 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 298 PELLDKtldlQDWGMALrraDIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAELGNTPTSDELWALAVQERRRpyIPS 377
Cdd:cd05588  165 PEILRG----EDYGFSV---DWWALGVLMFEML---------AGRSPFDIVGSSDNPDQNTEDYLFQVILEKPIR--IPR 226
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 378 TWRCFATdpdglrELLEDCWDADPEARLTaeCvqqrlaalaHPQE------SHPF 426
Cdd:cd05588  227 SLSVKAA------SVLKGFLNKNPAERLG--C---------HPQTgfadiqSHPF 264
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
213-346 2.08e-03

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


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 40.02  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 213 MALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawTPTQPQGPAAIMEAGT 292
Cdd:cd06658  123 VCLSVLRALSYLHNQ---------GVIHRDIKSDSILLTSDGRIKLSDFGFC------------AQVSKEVPKRKSLVGT 181
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767973831 293 QRYMAPELLDKTldlqDWGMALrraDIYSLALLLWEILSRCPdlrPDSSPPPFQ 346
Cdd:cd06658  182 PYWMAPEVISRL----PYGTEV---DIWSLGIMVIEMIDGEP---PYFNEPPLQ 225
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
212-359 2.26e-03

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: 40.04  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 212 RMALSLAQGLAFLHEerwqngqyKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIMEAG 291
Cdd:cd06650  107 KVSIAVIKGLTYLRE--------KHKIMHRDVKPSNILVNSRGEIKLCDFGVS--------------GQLIDSMANSFVG 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973831 292 TQRYMAPELLDKT-LDLQdwgmalrrADIYSLALLLWEI-LSRCPDLRPDSS--PPPFQLAYEAELGNTPTS 359
Cdd:cd06650  165 TRSYMSPERLQGThYSVQ--------SDIWSMGLSLVEMaVGRYPIPPPDAKelELMFGCQVEGDAAETPPR 228
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
234-329 2.28e-03

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 40.25  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 234 YKPGIAHRDLSSQNVLIREDGSCAIGDLGLAlvLPGLTQpPAWTPTQpqgpaaimeAGTQRYMAPELLdktLDLQDWGma 313
Cdd:cd05586  113 HKNDIVYRDLKPENILLDANGHIALCDFGLS--KADLTD-NKTTNTF---------CGTTEYLAPEVL---LDEKGYT-- 175
                         90
                 ....*....|....*.
gi 767973831 314 lRRADIYSLALLLWEI 329
Cdd:cd05586  176 -KMVDFWSLGVLVFEM 190
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
238-334 2.36e-03

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: 40.06  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 238 IAHRDLSSQNVLIREDGSCAIGDLGLAlvLPGLTQppawtptqpqgpAAIMEA--GTQRYMAPELLDKtldlQDWGmalR 315
Cdd:cd05593  136 IVYRDLKLENLMLDKDGHIKITDFGLC--KEGITD------------AATMKTfcGTPEYLAPEVLED----NDYG---R 194
                         90       100
                 ....*....|....*....|
gi 767973831 316 RADIYSLALLLWEIL-SRCP 334
Cdd:cd05593  195 AVDWWGLGVVMYEMMcGRLP 214
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
234-331 2.47e-03

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 39.98  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 234 YKPGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgLTQppawtptqpQGPAAIMEAGTQRYMAPELLDKTLDLQDwgma 313
Cdd:cd05613  122 HKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEF--LLD---------ENERAYSFCGTIEYMAPEIVRGGDSGHD---- 186
                         90
                 ....*....|....*...
gi 767973831 314 lRRADIYSLALLLWEILS 331
Cdd:cd05613  187 -KAVDWWSLGVLMYELLT 203
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
108-332 2.48e-03

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 39.61  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 108 WAGQLQGKLVAIKAFPPRSVAQFQAERALYElpGLQHDHIVRFITAsrggpgrllsgpllvlelhpkdcvCLCPrgraPH 187
Cdd:cd14153   21 WHGEVAIRLIDIERDNEEQLKAFKREVMAYR--QTRHENVVLFMGA------------------------CMSP----PH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 188 nsLCPIGSLCHYLTQYTS--------DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIrEDGSCAIG 259
Cdd:cd14153   71 --LAIITSLCKGRTLYSVvrdakvvlDVNKTRQIAQEIVKGMGYLHAK---------GILHKDLKSKNVFY-DNGKVVIT 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973831 260 DLGLaLVLPGLTQPPAwtptqpQGPAAIMEAGTQRYMAPELLDK-TLDLQDWGMAL-RRADIYSLALLLWEILSR 332
Cdd:cd14153  139 DFGL-FTISGVLQAGR------REDKLRIQSGWLCHLAPEIIRQlSPETEEDKLPFsKHSDVFAFGTIWYELHAR 206
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
234-333 2.68e-03

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 39.68  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 234 YKPGIAHRDLSSQNVLIREDGSCAIGDLGLA-LVLPGLTQppawtptqpqgpAAIMEAGTQRYMAPELL-------DKTL 305
Cdd:cd05583  116 HKLGIIYRDIKLENILLDSEGHVVLTDFGLSkEFLPGEND------------RAYSFCGTIEYMAPEVVrggsdghDKAV 183
                         90       100
                 ....*....|....*....|....*...
gi 767973831 306 dlqDWgmalrradiYSLALLLWEILSRC 333
Cdd:cd05583  184 ---DW---------WSLGVLTYELLTGA 199
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
216-407 2.69e-03

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: 39.45  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 216 SLAQGLAFLHeerwqngqyKPGIAHRDLSSQNVLIRE---DGSCAIG----DLGLALVLPGLtqppawtptqpqGPAAIM 288
Cdd:cd14097  108 SLASAVAYLH---------KNDIVHRDLKLENILVKSsiiDNNDKLNikvtDFGLSVQKYGL------------GEDMLQ 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 289 EA-GTQRYMAPELLDKtldlQDWGmalRRADIYSLALLLWEILsrCPDlrpdsspPPFQLAYEAELGNTPTSDELwalav 367
Cdd:cd14097  167 ETcGTPIYMAPEVISA----HGYS---QQCDIWSIGVIMYMLL--CGE-------PPFVAKSEEKLFEEIRKGDL----- 225
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 767973831 368 qerrrPYIPSTWrcfATDPDGLRELLEDCWDADPEARLTA 407
Cdd:cd14097  226 -----TFTQSVW---QSVSDAAKNVLQQLLKVDPAHRMTA 257
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
217-301 2.72e-03

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: 39.47  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawtptqPQGPAAIMEA---GTQ 293
Cdd:cd14080  111 LALAVQYLHSL---------DIAHRDLKCENILLDSNNNVKLSDFGFARLC-------------PDDDGDVLSKtfcGSA 168

                 ....*...
gi 767973831 294 RYMAPELL 301
Cdd:cd14080  169 AYAAPEIL 176
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
215-426 2.72e-03

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 40.02  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 215 LSLAqgLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAL--VLPGLTQPPAwtptqpqgpaaimeAGT 292
Cdd:cd05618  130 ISLA--LNYLHER---------GIIYRDLKLDNVLLDSEGHIKLTDYGMCKegLRPGDTTSTF--------------CGT 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 293 QRYMAPELLDKtldlQDWGMALrraDIYSLALLLWEILsrcpdlrpdSSPPPFQLAYEAELGNTPTSDELWALAVQERRR 372
Cdd:cd05618  185 PNYIAPEILRG----EDYGFSV---DWWALGVLMFEMM---------AGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIR 248
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 373 pyIPSTWRCFATdpdglrELLEDCWDADPEARLTaecvqqrlaalAHPQ------ESHPF 426
Cdd:cd05618  249 --IPRSLSVKAA------SVLKSFLNKDPKERLG-----------CHPQtgfadiQGHPF 289
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
219-333 2.75e-03

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 39.42  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGS-CAIGDLGLALVLpgltQPPAWTPTQPQGPAAimeAGTQRYMA 297
Cdd:cd13991  109 EGLEYLHSRK---------ILHGDVKADNVLLSSDGSdAFLCDFGHAECL----DPDGLGKSLFTGDYI---PGTETHMA 172
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 767973831 298 PEL-LDKTLDlqdwgmalRRADIYSLALLLWEILSRC 333
Cdd:cd13991  173 PEVvLGKPCD--------AKVDVWSSCCMMLHMLNGC 201
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
238-329 3.52e-03

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: 39.27  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 238 IAHRDLSSQNVLIREDGSCAIGDLGLA--LVlpgltqppawtptqpQGPAAIMEAGTQRYMAPELLDKTLDLQDWGMalr 315
Cdd:cd06616  131 IIHRDVKPSNILLDRNGNIKLCDFGISgqLV---------------DSIAKTRDAGCRPYMAPERIDPSASRDGYDV--- 192
                         90
                 ....*....|....
gi 767973831 316 RADIYSLALLLWEI 329
Cdd:cd06616  193 RSDVWSLGITLYEV 206
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
217-334 4.55e-03

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


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 39.24  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEERwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAAIMEA--GTQR 294
Cdd:cd05594  134 IVSALDYLHSEK--------NVVYRDLKLENLMLDKDGHIKITDFGLC--------------KEGIKDGATMKTfcGTPE 191
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767973831 295 YMAPELLDKtldlQDWGmalRRADIYSLALLLWEIL-SRCP 334
Cdd:cd05594  192 YLAPEVLED----NDYG---RAVDWWGLGVVMYEMMcGRLP 225
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
219-322 5.05e-03

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: 38.83  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 219 QGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLpgltqppawTPTQPQGPAAImeaGTQRYMAP 298
Cdd:cd06613  108 KGLAYLHST---------GKIHRDIKGANILLTEDGDVKLADFGVSAQL---------TATIAKRKSFI---GTPYWMAP 166
                         90       100
                 ....*....|....*....|....
gi 767973831 299 ELldktLDLQDWGMALRRADIYSL 322
Cdd:cd06613  167 EV----AAVERKGGYDGKCDIWAL 186
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
221-350 5.37e-03

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 39.03  E-value: 5.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 221 LAF--LHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTqppawtptqpqgpaaIMEAGTQRYMAP 298
Cdd:PTZ00263 129 LAFeyLHSK---------DIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRT---------------FTLCGTPEYLAP 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767973831 299 ELldktldLQDWGMAlRRADIYSLALLLWEILSRCPDLRPDSsppPFQLaYE 350
Cdd:PTZ00263 185 EV------IQSKGHG-KAVDWWTMGVLLYEFIAGYPPFFDDT---PFRI-YE 225
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
220-340 5.95e-03

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: 38.30  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 220 GLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDLGLAlvlpgltqppawtpTQPQGPAA--IMEAGTQRYMA 297
Cdd:cd14186  114 GMLYLHSH---------GILHRDLTLSNLLLTRNMNIKIADFGLA--------------TQLKMPHEkhFTMCGTPNYIS 170
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767973831 298 PELLDKTLDlqdwGMalrRADIYSLALLLWEILSRCPDLRPDS 340
Cdd:cd14186  171 PEIATRSAH----GL---ESDVWSLGCMFYTLLVGRPPFDTDT 206
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
238-334 6.33e-03

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 38.81  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 238 IAHRDLSSQNVLIREDGSCAIGDLGLALVLPGLTQPPAWTPtqpqgpaaimeagtqRYMAPELLdktLDLQDWgmalRRA 317
Cdd:PTZ00426 152 IVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTYTLCGTP---------------EYIAPEIL---LNVGHG----KAA 209
                         90
                 ....*....|....*..
gi 767973831 318 DIYSLALLLWEILSRCP 334
Cdd:PTZ00426 210 DWWTLGIFIYEILVGCP 226
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
211-301 6.33e-03

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: 38.28  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 211 LRMALSlaqGLAFLHeerwqngqyKPGIAHRDLSSQNVLI---REDGSCAIGDLGLAlvlpgltqppawtPTQPQGPAAI 287
Cdd:cd14087  103 LQMVLD---GVKYLH---------GLGITHRDLKPENLLYyhpGPDSKIMITDFGLA-------------STRKKGPNCL 157
                         90
                 ....*....|....*.
gi 767973831 288 MEA--GTQRYMAPELL 301
Cdd:cd14087  158 MKTtcGTPEYIAPEIL 173
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
206-419 6.78e-03

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 38.92  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 206 DWGSSLRMALSLAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCAIGDL-GLALVLPGLTQPpawtptqpqgp 284
Cdd:COG4248  119 DWLFLLRTARNLAAAVAALHAA---------GYVHGDVNPSNILVSDTALVTLIDTdSFQVRDPGKVYR----------- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 285 aaiMEAGTQRYMAPELLDKTLDLqdwgmALRRA--DIYSLALLLWEILsrcpdLRPDSsppPFQLAYEAElGNTPTSDEL 362
Cdd:COG4248  179 ---CVVGTPEFTPPELQGKSFAR-----VDRTEehDRFGLAVLIFQLL-----MEGRH---PFSGVYQGD-GDDPTLEER 241
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 363 walaVQERRRPYIPSTWRCFATDPD---------GLRELLEDCW---DADPEARLTAecvQQRLAALAH 419
Cdd:COG4248  242 ----IAMGHFVYHPNRRVLIRPPPRaipyeilhpYLQELFERAFidgHHNPQLRPSA---KEWEAALAE 303
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
234-264 8.06e-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: 38.14  E-value: 8.06e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767973831 234 YKPGIAHRDLSSQNVLIREDGSCAIGDLGLA 264
Cdd:cd14073  118 HKNGVVHRDLKLENILLDQNGNAKIADFGLS 148
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
217-331 8.11e-03

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: 38.44  E-value: 8.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973831 217 LAQGLAFLHEErwqngqykpGIAHRDLSSQNVLIREDGSCA---IGDLGLALVLPGltQPPAWTPtqpqgpaaimeAGTQ 293
Cdd:cd14092  108 LVSAVSFMHSK---------GVVHRDLKPENLLFTDEDDDAeikIVDFGFARLKPE--NQPLKTP-----------CFTL 165
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767973831 294 RYMAPELLDKTLDLQDWGMAlrrADIYSLALLLWEILS 331
Cdd:cd14092  166 PYAAPEVLKQALSTQGYDES---CDLWSLGVILYTMLS 200
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
194-262 8.64e-03

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: 36.65  E-value: 8.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973831 194 GSLCHYLTQYTSDWGSSLRMALSLAQGLAFLHEERwqngqykpgIAHRDLSSQNVLIREDGSCAIGDLG 262
Cdd:cd13968   77 GTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFH---------LIHRDLNNDNILLSEDGNVKLIDFG 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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